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<XML>
  <JOURNAL>   
    <YEAR>2017</YEAR>
    <VOL>9</VOL>
    <NO>2</NO>
    <MOSALSAL>33</MOSALSAL>
    <PAGE_NO>64</PAGE_NO>  
    <ARTICLES>

<ARTICLE>
    <TitleE>Research in Iran: An Overview</TitleE>
    <TitleF></TitleF>
    <TitleLang_ID>2</TitleLang_ID>
    <ABSTRACTS>

        <ABSTRACT>
            <Language_ID>2</Language_ID>
            <CONTENT>&lt;p&gt;Islamic Iran, on the Horizon of the 2025 Outlook Document, should obtain first regional rank in economic, social, scientific, and cultural domains. Country&amp;rsquo;s noticeable growth in scientific production and dynamic movement of Iranian scientists and specialists in scientific frontiers resulted in the country earning first rank in regional scientific production, leaving behind Turkey, in the year 2011, 14 years ahead of the Horizontal Outlook prediction. In the year 2016, Iran, with publication of 51187 articles in the Scopus database, acquired 16th world-wide ranking. In the same year, citation to the Iranian articles was 28965, has achieved 18th international ranking and 1st regional ranking. Overall, Iran, in the year 2016, has been responsible for an equivalent of 1.7% of the world&amp;rsquo;s total scientific production. Certainly, preserving Iran&amp;rsquo;s scientific growth trend is an important and fundamental subject and should consistently be brought to attention and consideration of government officials and policy makers in the research arena. There is no doubt; this support should include both basic and clinical studies &lt;sup&gt;1-3&lt;/sup&gt;.&lt;br /&gt;
Presence of national universities in international ranking institutions is considered one of the credible indicators for international scientific production for universities. Multiple international ranking institutions exist and university ranks in these institutions is considered to represent their qualitative and quantitative scientific production standing. One of the in-ternational ranking institutions, Essential Science Indicators (ESI), evaluates and ranks universities based on institution&amp;rsquo;s citation standing for the past ten years in the ISI database. From the sixty present national universities, currently thirteen national medical science universities are among world&amp;rsquo;s top universities in ESI. Before, this number was less and limited to a few universities. Among the top 500 universities in the world, just Tehran University of Medical Sciences is present.&lt;br /&gt;
Scientific production of Islamic Iran&amp;rsquo;s scientists holds the needed potential and wealth to be the world&amp;rsquo;s reference in sci-ence and knowledge.&amp;nbsp; Based on this and by following guidelines of the supreme leader of the Islamic revolution, preservation, persistence, and reinforcement of the scientific production debate has unavoidable urgency and priority in academic and scientific circles and gatherings. Therefore, we must support innovative and technological institutes more than before.&lt;/p&gt;
</CONTENT>
        </ABSTRACT>
    </ABSTRACTS>
    <PAGES>
        <PAGE>
            <FPAGE>49</FPAGE>
            <TPAGE>49</TPAGE>
        </PAGE>
    </PAGES>
    <AUTHORS>
        <AUTHOR>
<Name>Shahin</Name>
<MidName></MidName>
<Family>Akhondzadeh</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Psychiatric Research Center, Roozbeh Hospital, South Kargar Street</Organization>
</Organizations>
<Universities>
<University>Psychiatric Research Center, Roozbeh Hospital, South Kargar Street</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR>
    </AUTHORS>
    <KEYWORDS>
        <KEYWORD><KeyText>Editorial</KeyText></KEYWORD>
    </KEYWORDS>
    <PDFFileName>267.pdf</PDFFileName>
    <REFRENCES>
        <REFRENCE>
            <REF>Akhondzadeh S. Hippocampal synaptic plasticity and cognition. J Clin Pharm Ther 1999;24(4):241-248.##Akhondzadeh S, Malek-Hosseini M, Ghoreishi A, Raznahan M, Rezazadeh SA. Effect of ritanserin, a 5HT2A/2C antagonist, on negative symptoms of schizophrenia: a double-blind randomized placebo-controlled study. Prog Neuropsychopharmacol Biol Psychiatry 2008;32(8):1879-1883.##Ghaleiha A, Entezari N, Modabbernia A, Najand B, Askari N, Tabrizi M, et al. Memantine add-on in moderate to se-vere obsessive-compulsive disorder: randomized double-blind placebo-controlled study. J Psychiatr Res 2013;47(2):175-180.##</REF>
        </REFRENCE>
    </REFRENCES>
</ARTICLE>

<ARTICLE>
    <TitleE>Current State of Cartilage Tissue Engineering  using Nanofibrous Scaffolds and Stem Cells</TitleE>
    <TitleF></TitleF>
    <TitleLang_ID>2</TitleLang_ID>
    <ABSTRACTS>

        <ABSTRACT>
            <Language_ID>2</Language_ID>
            <CONTENT>&lt;p&gt;Cartilage is an avascular, aneural, and alymphatic connective tissue with a limited capacity caused by low mitotic activity of its resident cells, chondrocytes. Natural repair of full thickness cartilage defects usually leads to the formation of fibrocartilage with lower function and mechanical force compared with the original hyaline cartilage and further deterioration can occur. Tissue engineering and regenerative medicine is a promising strategy to repair bone and articular cartilage defects and rehabilitate joint functions by focusing on the optimal combination of cells, material scaffolds, and signaling molecules. The unique physical and topographical properties of nanoﬁbrous structures allow them to mimic the extracellular matrix of native cartilage, making an appropriate resemblance to induce cartilage tissue regeneration and reconstruction. To improve simulation of native cartilage, the incorporation of nanofibrous scaffolds with suitable corresponsive cells could be effective. In this review article, an attempt was made to present the current state of cartilage tissue engineering using nanofibrous scaffolds and stem cells as high proliferative immune privilege cells with chondrogenic differentiation ability. The comprehensive information was retrieved by search of relevant subject headings in Medline/Pubmed and Elsevier databases.&lt;/p&gt;
</CONTENT>
        </ABSTRACT>
    </ABSTRACTS>
    <PAGES>
        <PAGE>
            <FPAGE>50</FPAGE>
            <TPAGE>65</TPAGE>
        </PAGE>
    </PAGES>
    <AUTHORS>
        <AUTHOR>
<Name>Somaieh</Name>
<MidName></MidName>
<Family>Kazemnejad</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Reproductive Biotechnology Research Center, Avicenna Research Institute, ACECR</Organization>
</Organizations>
<Universities>
<University>Reproductive Biotechnology Research Center, Avicenna Research Institute, ACECR</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Manijeh</Name>
<MidName></MidName>
<Family>Khanmohammadi</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Reproductive Biotechnology Research Center, Avicenna Research Institute, ACECR</Organization>
</Organizations>
<Universities>
<University>Reproductive Biotechnology Research Center, Avicenna Research Institute, ACECR</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Nafiseh</Name>
<MidName></MidName>
<Family>Baheiraei</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Department of Anatomical Sciences, Faculty of Medical Sciences, Tarbiat Modares University</Organization>
</Organizations>
<Universities>
<University>Department of Anatomical Sciences, Faculty of Medical Sciences, Tarbiat Modares University</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Shaghayegh</Name>
<MidName></MidName>
<Family>Arasteh</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Reproductive Biotechnology Research Center, Avicenna Research Institute, ACECR</Organization>
</Organizations>
<Universities>
<University>Reproductive Biotechnology Research Center, Avicenna Research Institute, ACECR</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR>
    </AUTHORS>
    <KEYWORDS>
        <KEYWORD><KeyText>Cartilage</KeyText></KEYWORD><KEYWORD><KeyText>Nanofibers</KeyText></KEYWORD><KEYWORD><KeyText>Scaffolds</KeyText></KEYWORD><KEYWORD><KeyText>Stem cells</KeyText></KEYWORD><KEYWORD><KeyText>Tissue engineering</KeyText></KEYWORD>
    </KEYWORDS>
    <PDFFileName>268.pdf</PDFFileName>
    <REFRENCES>
        <REFRENCE>
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Immune evasion by neocartilage-derived chondrocytes: Implications for biologic repair of joint articular cartilage. Stem Cell Res 2010;4(1):57-68.##Nauta AJ, Fibbe WE. Immunomodulatory properties of mesenchymal stromal cells. Blood 2007;110(10):3499-3506.##Estes BT, Diekman BO, Gimble JM, Guilak F. Isolation of adipose-derived stem cells and their induction to a chondrogenic phenotype. Nat Protoc 2010;5(7):1294-1311.##Li WJ, Jiang YJ, Tuan RS. Cell-nanofiber-based cartilage tissue engineering using improved cell seeding, growth factor, and bioreactor technologies. Tissue Eng Part A 2008;14(5):639-648.## Thorvaldsson A, Stenhamre H, Gatenholm P, Walkenstr&#246;m P. Electrospinning of highly porous scaffolds for cartilage regeneration. Biomacromolecules 2008;9(3):1044-1049.##Shin HJ, Lee CH, Cho IH, Kim YJ, Lee YJ, Kim IA, et al. Electrospun PLGA nanofiber scaffolds for articular cartilage reconstruction: mechanical stability, degradation and cellular responses under mechanical stimulation in vitro. J Biomater Sci Polym Ed 2006;17(1-2):103-119.##Zheng X, Yang F, Wang S, Lu S, Zhang W, Liu S, et al. Fabrication and cell affinity of biomimetic structured PLGA/articular cartilage ECM composite scaffold. J Mater Sci Mater Med 2011;22(3):693-704.##Bean AC, Tuan RS. Fiber diameter and seeding density influence chondrogenic differentiation of mesenchymal stem cells seeded on electrospun poly (ε-caprolactone) scaffolds. Biomed Mater 2015;10(1):015018.##Garrigues NW, Little D, Sanchez-Adams J, Ruch DS, Guilak F. Electrospun cartilage‐derived matrix scaffolds for cartilage tissue engineering. J Biomed Mater Res A 2014;102(11):3998-4008.##Fong CY, Subramanian A, Gauthaman K, Venugopal J, Biswas A, Ramakrishna S, et al. Human umbilical cord Wharton’s jelly stem cells undergo enhanced chondrogenic differentiation when grown on nanofibrous scaffolds and in a sequential two-stage culture medium environment. Stem Cell Rev 2012;8(1):195-209.##Lee P, Tran K, Chang W, Shelke NB, Kumbar SG, Yu X. Influence of chondroitin sulfate and hyaluronic acid presence in nanofibers and its alignment on the bone marrow stromal cells: Cartilage regeneration. J Biomed Nanotechnol 2014;10(8):1469-1479.##Shanmugasundaram S, Chaudhry H, Arinzeh TL. Microscale versus nanoscale scaffold architecture for mesenchymal stem cell chondrogenesis. Tissue Eng Part A 2011;17(5-6):831-840.##Nam J, Johnson J, Lannutti JJ, Agarwal S. Modulation of embryonic mesenchymal progenitor cell differentiation via control over pure mechanical modulus in electrospun nanofibers. Acta Biomater 2011;7(4):1516-1524.##Janjanin S, Li WJ, Morgan MT, Shanti RM, Tuan RS. Mold-shaped, nanofiber scaffold-based cartilage engineering using human mesenchymal stem cells and bioreactor. J Surg Res 2008;149(1):47-56.##Li WJ, Tuli R, Huang X, Laquerriere P, Tuan RS. Multilineage differentiation of human mesenchymal stem cells in a three-dimensional nanofibrous scaffold. Biomaterials 2005;26(25):5158-5166.##Stenhamre H, Thorvaldsson A, Enochson L, Walkenstr&#246;m P, Lindahl A, Brittberg M, et al. Nanosized fibers&#39; effect on adult human articular chondrocytes behavior. Mater Sci Eng C Mater Biol Appl 2013;33(3):1539-1545.##Wright LD, McKeon-Fischer KD, Cui Z, Nair LS, Freeman JW. PDLA/PLLA and PDLA/PCL nanofibers with a chitosan-based hydrogel in composite scaffolds for tissue engineered cartilage. J Tissue Eng Regen Med 2014;8(12):946-954.##Chen JP, Su CH. Surface modification of electrospun PLLA nanofibers by plasma treatment and cationized gelatin immobilization for cartilage tissue engineering. Acta Biomater 2011;7(1):234-243.##Richardson SM, Curran JM, Chen R, Vaughan-Thomas A, Hunt JA, Freemont AJ, et al. The differentiation of bone marrow mesenchymal stem cells into chondrocyte-like cells on poly-L-lactic acid (PLLA) scaffolds. Biomaterials 2006;27(22):4069-4078.##</REF>
        </REFRENCE>
    </REFRENCES>
</ARTICLE>

<ARTICLE>
    <TitleE>Gestational Exposure to Silymarin Increases Susceptibility of BALB/c Mice Fetuses to Apoptosis</TitleE>
    <TitleF></TitleF>
    <TitleLang_ID>2</TitleLang_ID>
    <ABSTRACTS>

        <ABSTRACT>
            <Language_ID>2</Language_ID>
            <CONTENT>&lt;p&gt;Background: Silymarin is a flavonolignan that has been the subject of research to evaluate the beneficial properties for decades. Silymarin has been known for its potent cytoprotective, hepatoprotective and antioxidant activities. The goal of the present study was to gain a deeper understanding of possible molecular mechanisms of apoptosis of the injuries induced by silymarin on BALB/c mice fetuses.&lt;br /&gt;
Methods: The present experimental study was carried out in virgin female BALB/c mice. The animals were divided randomly into 4 groups. Three test groups were injected intraperitoneally with silymarin at doses of 50, 100 and 200 &lt;em&gt;mg/kg/day&lt;/em&gt; during gestational days 6-15. The control group received the solvent by the same route at equivalent volume. Western blot analysis was conducted to determine the levels of caspase-3 and caspase-8 in fetal heart, kidney, lungs and brain tissue.&lt;br /&gt;
Results: The results of this study showed that silymarin administration during organogenesis at doses of 50, 100 and 200 &lt;em&gt;mg/kg&lt;/em&gt; can significantly increase the protein levels of caspase-3 and 8 in heart, kidneys and brain tissues of mice fetuses compared with control group (p&amp;lt;0.001). Silymarin exposure could not change the level of apoptotic markers in fetal lung tissue.&lt;br /&gt;
Conclusion: According to the results, programmed cell death, especially via the intrinsic pathway, plays a pivotal role in the pathogenesis of silymarin-induced malformations in some tissue including heart, kidneys and brain. More studies are needed to determine other molecular mechanisms underlying silymarin- induced embryo toxicity.&lt;/p&gt;
</CONTENT>
        </ABSTRACT>
    </ABSTRACTS>
    <PAGES>
        <PAGE>
            <FPAGE>66</FPAGE>
            <TPAGE>70</TPAGE>
        </PAGE>
    </PAGES>
    <AUTHORS>
        <AUTHOR>
<Name>Mahbobe</Name>
<MidName></MidName>
<Family>Gholami</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Department of Pharmacodynamics and Toxicology, Faculty of Pharmacy, Mashhad University of Medical SciencesDepartment of Nursing, Facutly of Midwifery, Neyshabur University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Department of Pharmacodynamics and Toxicology, Faculty of Pharmacy, Mashhad University of Medical SciencesDepartment of Nursing, Facutly of Midwifery, Neyshabur University of Medical Sciences</University>
</Universities>
<Countries>
<Country>IranIran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Seyed Adel</Name>
<MidName></MidName>
<Family>Moallem</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Department of Pharmacodynamics and Toxicology, Faculty of Pharmacy, Mashhad University of Medical SciencesPharmaceutical Research Center, Mashhad University of Medical SciencesPharmaceutical Research Center, Faculty of Pharmacy, Mashhad University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Department of Pharmacodynamics and Toxicology, Faculty of Pharmacy, Mashhad University of Medical SciencesPharmaceutical Research Center, Mashhad University of Medical SciencesPharmaceutical Research Center, Faculty of Pharmacy, Mashhad University of Medical Sciences</University>
</Universities>
<Countries>
<Country>IranIranIran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Mohammad</Name>
<MidName></MidName>
<Family>Afshar</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Department of Anatomy, Birjand University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Department of Anatomy, Birjand University of Medical Sciences</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Leila</Name>
<MidName></MidName>
<Family>Etemad</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Pharmaceutical Research Center, Mashhad University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Pharmaceutical Research Center, Mashhad University of Medical Sciences</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Gholamreza</Name>
<MidName></MidName>
<Family>Karimi</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Pharmaceutical Research Center, Faculty of Pharmacy, Mashhad University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Pharmaceutical Research Center, Faculty of Pharmacy, Mashhad University of Medical Sciences</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR>
    </AUTHORS>
    <KEYWORDS>
        <KEYWORD><KeyText>Apoptosis</KeyText></KEYWORD><KEYWORD><KeyText>Fetus</KeyText></KEYWORD><KEYWORD><KeyText>Silymarin</KeyText></KEYWORD><KEYWORD><KeyText>Teratogenicity</KeyText></KEYWORD>
    </KEYWORDS>
    <PDFFileName>269.pdf</PDFFileName>
    <REFRENCES>
        <REFRENCE>
            <REF>Valenzuela A, Garrido A. Biochemical bases of the pharmacological action of the flavonoid silymarin and of its structural isomer silibinin. Biol Res 1994;27(2):105-112.##Morazzoni P, Bombardelli E. Silybum marianum (Carduus marianus). Fitoterapia 1995;66(1):3-42.##Gavind P, Sahni YP. A review on hepatoprotective activity of silymarin‏. Int J Res Ayurveda Pharm 2011;2(1):75-79.##Greenlee H, Abascal K, Yarnell E, Ladas E. Clinical application of Silybum marianum in oncology. Integr Cancer Ther 2007;6(2):158-165.##Valenzuela A, Lagos C, Schmidt K, Videla LA. Silymarin protection against hepatic lipid peroxidation induced by acute ethanol intoxication in the rat. Biochem Pharmacol 1985;34(12):2209-2212.##Das SK, Vasudevan DM. Protective effects of silymarin, a milk thistle (Silybium marianum) derivative on ethanol-induced oxidative stress in liver. Indian J Biochem Biophys 2006;43(5):306-311.##Dixit N, Baboota S, Kohli K, Ahmad S, Javed A. Silymarin: A review of pharmacological aspects and bioavailability enhancement approaches. Indian J Pharmacol 2007;39(4):172-179.##Iosio T, Voinovich D, Perissutti B, Serdoz F, Hasa D, Grabnar I, et al. Oral bioavailability of silymarin phytocomplex formulated as self-emulsifying pellets. Phytomedicine 2011;18(6):505-512.##Fraschini F, Demartini G, Esposti D. Pharmacology of silymarin. Clin Drug Investig 2002;22(1):51-65.##Gholami M, Moallem SA, Afshar M, Amoueian S, Etemad L, Karimi G. Teratogenic effects of silymarin on mouse fetuses. Avicenna J Phytomed 2016;6(5):542-549.##Gholami M, Moallem SA, Afshar M, Etemad L, Karimi G. Maternal exposure to silymarin leads to pathological changes in mouse fetuses. Pharmacology Online 2015;2:38-43.##Etemad L, Jafarian AH, Moallem SA. Pathogenesis of pregabalin-induced limb defects in mouse embryos. J Pharm Pharm Sci 2015;18(5):882-889.##McIlwain DR, Berger T, Mak TW. Caspase functions in cell death and disease. Cold Spring Harb Perspect Biol 2013;5(4):a008656.##Katiyar SK, Roy AM, Baliga MS. Silymarin induces apoptosis primarily through a p53-dependent pathway involving Bcl-2/Bax, cytochrome c release, and caspase activation. Mol Cancer Ther 2005;4(2):207-216.##Ramakrishnan G, Lo Muzio L, Elinos-B&#225;ez CM, Jagan S, Augustine TA, Kamaraj S, et al. Silymarin inhibited proliferation and induced apoptosis in hepatic cancer cells. Cell Prolif 2009;42(2):229-240.##Kalla PK, Chitti S, Aghamirzaei ST, Senthilkumar R, Arjunan S. Anti-cancer activity of silymarin on MCF-7 and NCIH-23 cell lines. Adv Biol Res 2014;8(2):57-61.##Fan L, Ma Y, Liu Y, Zheng D, Huang G. Silymarin induces cell cycle arrest and apoptosis in ovarian cancer cells. Eur J Pharmacol 2014;743:79-88.##Agarwal C, Tyagi A, Kaur M, Agarwal R. Silibinin inhibits constitutive activation of Stat3, and causes caspase activation and apoptotic death of human prostate carcinoma DU145 cells. Carcinogenesis 2007;28(7):1463-1470.##Tyagi A, Singh RP, Agarwal C, Agarwal R. Silibinin activates p53-caspase 2 pathway and causes caspase-mediated cleavage of Cip1/p21 in apoptosis induction in bladder transitional-cell papilloma RT4 cells: evidence for a regulatory loop between p53 and caspase 2. Carcinogenesis 2006;27(11):2269-2280.##Raza SS, Khan MM, Ashafaq M, Ahmad A, Khuwaja G, Khan A, et al. Silymarin protects neurons from oxidative stress associated damages in focal cerebral ischemia: a behavioral, biochemical and immunohistological study in Wistar rats. J Neurol Sci 2011;309(1-2):45-54.##Al-Rasheed NM, Al-Rasheed NM, Faddah LM, Mohamed AM, Mohammad RA, Al-Amin M. Potential impact of silymarin in combination with chlorogenic acid and/or melatonin in combating cardiomyopathy induced by carbon tetrachloride. Saudi J Biol Sci 2014;21(3):265-274.##Homsi E, de Brito SM, Janino P. Silymarin exacerbates p53-mediated tubular apoptosis in glycerol-induced acute kidney injury in rats. Ren Fail 2010;32(5):623-632.##Li W, Mu D, Song L, Zhang J, Liang J, Wang C, et al. Molecular mechanism of silymarin-induced apoptosis in a highly metastatic lung cancer cell line anip973. Cancer Biother Radiopharm 2011;26(3):317-324.##</REF>
        </REFRENCE>
    </REFRENCES>
</ARTICLE>

<ARTICLE>
    <TitleE>Alpha Alumina Nanoparticle Conjugation to Cysteine Peptidase A and B: An Efficient Method for Autophagy Induction</TitleE>
    <TitleF></TitleF>
    <TitleLang_ID>2</TitleLang_ID>
    <ABSTRACTS>

        <ABSTRACT>
            <Language_ID>2</Language_ID>
            <CONTENT>&lt;p&gt;Background: Autophagy as a cellular pathway facilitates several immune responses against infection. It also eliminates invading pathogens through transferring content between the cytosol and the lysosomal vesicles and contributes to the cross-presentation of exogenous antigens to T lymphocytes via MHC class I pathway. Autophagy induction is one of the main targets for new drugs and future vaccine formulations. Nanoparticles are one of the candidates for autophagy induction. Cysteine Peptidase A (CPA) and Cysteine Peptidase B (CPB) are two members of papain family (Clan CA, family C1) enzyme that have been considered as a virulence factor of Leishmania (L.) major, making them suitable vaccine candidates. In this research, Leishmania major cysteine peptidase A and B (CPA and CPB) conjugation to alpha alumina nanoparticle was the main focus and their entrance efficacy to macrophages was assessed.&lt;br /&gt;
Methods: For this purpose, CPA and CPB genes were cloned in expression vectors. Related proteins were extracted from transformed &lt;em&gt;E. coli&lt;/em&gt; and purified using Ni affinity column. Alpha alumina nanoparticles were conjugated to CPA/CPB proteins using Aldehyde/Hydrazine Reaction. Autophagy induction in macrophages was assessed using acridine orange staining.&lt;br /&gt;
Results: CPA/CPB protein loading to nanoparticles was confirmed by Fourier Transform Infrared Spectroscopy. &amp;alpha;-alumina conjugated CPA/CPB antigen uptake by macrophages at different concentrations was confirmed using fluorescence microscope and flowcytometry. Highly efficient CPA/CPB protein loading to &amp;alpha;-alumina nanoparticles and rapid internalization to macrophages introduced these nanocarriers as a delivery tool. Acridine orange staining demonstrated higher autophagy induction in CPA/CPB protein conjugated with &amp;alpha;-alumina nanoparticles.&lt;br /&gt;
Conclusion: &amp;alpha;-alumina nanoparticles may be a promising adjuvant in the development of therapeutic leishmania vaccines through antigen delivery to intracellular compartments, induction of autophagy and cross presentation to CD&lt;sub&gt;8&lt;/sub&gt; lymphocytes.&lt;/p&gt;
</CONTENT>
        </ABSTRACT>
    </ABSTRACTS>
    <PAGES>
        <PAGE>
            <FPAGE>71</FPAGE>
            <TPAGE>81</TPAGE>
        </PAGE>
    </PAGES>
    <AUTHORS>
        <AUTHOR>
<Name>Fatemeh</Name>
<MidName></MidName>
<Family>Beyzay</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Department of Immunology, Faculty of Medical Sciences, Tarbiat Modares University</Organization>
</Organizations>
<Universities>
<University>Department of Immunology, Faculty of Medical Sciences, Tarbiat Modares University</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Ahmad</Name>
<MidName></MidName>
<Family>Zavaran Hosseini</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Department of Immunology, Faculty of Medical Sciences, Tarbiat Modares University</Organization>
</Organizations>
<Universities>
<University>Department of Immunology, Faculty of Medical Sciences, Tarbiat Modares University</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Sara</Name>
<MidName></MidName>
<Family>Soudi</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Department of Immunology, Faculty of Medical Sciences, Tarbiat Modares University</Organization>
</Organizations>
<Universities>
<University>Department of Immunology, Faculty of Medical Sciences, Tarbiat Modares University</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR>
    </AUTHORS>
    <KEYWORDS>
        <KEYWORD><KeyText>Autophagy</KeyText></KEYWORD><KEYWORD><KeyText>Cysteine peptidase</KeyText></KEYWORD><KEYWORD><KeyText>Macrophage</KeyText></KEYWORD>
    </KEYWORDS>
    <PDFFileName>270.pdf</PDFFileName>
    <REFRENCES>
        <REFRENCE>
            <REF>Deretic V, Saitoh T, Akira S. Autophagy in infection, inflammation and immunity. Nat Rev Immunol 2013;13(10):722-737.##Crotzer VL, Blum JS. Autophagy and its role in MHC-mediated antigen presentation. J Immunol 2009;182(6):3335-3341.##M&#252;nz C. Antigen processing via autophagy--not only for MHC class II presentation anymore? Curr Opin Immunol 2010;22(1):89-93.##Stern ST, Johnson DN. Role for nanomaterial-autophagy interaction in neurodegenerative disease. Autophagy 2008;4(8):1097-1100.##Stern ST, Adiseshaiah PP, Crist RM. Autophagy and lysosomal dysfunction as emerging mechanisms of nanomaterial toxicity. Part Fibre Toxicol 2012;9:20.##Calzolai L, Franchini F, Gilliland D, Rossi F. Protein--nanoparticle interaction: identification of the ubiquitin--Gold nanoparticle interaction site. Nano Lett 2010;10:3101-3105.##Wilczewska AZ, Niemirowicz K, Markiewicz K, Car H. Nanoparticles as drug delivery systems. Pharmacol Rep 2012;64(5):1020-1037.##Frank B, Marcu A, de Oliveira Almeida Petersen AL, Weber H, Stigloher C, Mottram JC, et al. Autophagic digestion of Leishmania major by host macrophages is associated with differential expression of BNIP3, CTSE, and the miRNAs miR-101c, miR-129, and miR-210. Parasit Vectors 2015;8:404.##Li C, Liu H, Sun Y, Wang H, Guo F, Rao S, et al. PAMAM nanoparticles promote acute lung injury by inducing autophagic cell death through the Akt-TSC2-mTOR signaling pathway. J Mol Cell Biol 2009;1(1):37-45.##Joshi P, Chakraborti S, Ramirez-Vick JE, Ansari ZA, Shanker V, Chakrabarti P, et al. The anticancer activity of chloroquine-gold nanoparticle against MCF-7 breast cancer cell. Colloids Surf B Biointerfaces 2012;95:195-200.##Wu YN, Yang LX, Shi XY, Li IC, Biazik JM, Ratinac KR, et al. The selective growth inhibition of oral cancer by iron core-gold shell nanoparticles through mitochondria-mediated autophagy. Biomaterials 2011;32(20):4565-4573.##Wei P, Zhang L, Lu Y, Man N, Wen L. C60(Nd) nanoparticles enhance chemotherapeutic susceptibility of cancer cells by modulation of autophagy. Nanotechnology 2010;21(49):495101.##English L, Chemali M, Duron J, Rondeau C, Laplante A, Gingras D, et al. Autophagy enhances the presentation of endogenous viral antigens on MHC class I molecules during HSV-1 infection. Nat Immunol 2009;10(5):480-487.##Rafati S, Salmanian AH, Hashemi K, Schaff C, Belli S, Fasel N. Identification of Leishmania major cysteine proteinases as targets of the immune response in humans. Mol Biochem Parasitol 2001;113(1):35-43.##Aghababa H, Mohabati Mobarez A, Khoramabadi N, Behmanesh M, Mahdavi M, Tebianian M, et al. A comparative approach to strategies for cloning, expression, and puriﬁcation of Mycobacterium tuberculosis mycolyl transferase 85B and evaluation of immune responses in BALB/c mice. Mol Biotechnol 2014;56(6):487-497.##Hermanson GT.  Bioconjugate techniques. 3rd ed. San Diego: Academic Press; 2008. 1200 p.##Goding JW. Conjugation of antibodies with fluoro-chromes: modifications to the standard methods. J Immunol Methods 1976;13(3-4):215-226.##Harlow E, Lane, D. Antibodies a Laboratory Manual. 1st ed. New York: Cold Spring Harbor Laboratory; 1988. 726 p.##The TH, Feltkamp TE. Conjugation of fluorescein isothiocynate to antibodies. I. Experiments on the conditions of conjugation. Immunology 1970;18(6):865-873.##Soudi S, Hosseini AZ,  Hashemi SM. Co-administration of rectal BCG and autoclaved Leishmania major induce protection in susceptible BALB/c mice. Parasite Immunol 2011;33(10):561-571.##Dameshghi S, Zavaran-Hosseinia A, Soudia S, Shirazi FJ, Nojehdehi S, Hashemi SM. Mesenchymal stem cells alter macrophage immune responses to Leishmania major infection in both susceptible and resistance mice. Immunol Lett 2016;170:15-26.##Ren Y, Huang F, Liu Y, Yang Y, Jiang Q, Xu C. Autophagy inhibition through PI3K/Akt increases apoptosis by sodium selenite in NB4 cells. BMB Rep 2009;42(9):599-604.##Sarkar S, Ravikumar B, Floto RA, Rubinsztein DC. Rapamycin and mTOR-independent autophagy inducers ameliorate toxicity of polyglutamine-expanded huntingtin and related proteinopathies. Cell Death Differ 2009:16(1):46-56.##Seglen PO, Gordon PB. 3-Methyladenine: specific inhibitor of autophagic/lysosomal protein degradation in isolated rat hepatocytes. Proc Natl Acad Sci USA 1982;79(6):1889-1892.##Hariharan M, Varghese N, Cherian B, Sreenivasan PV, Paul J, Antony A. Synthesis and characterisation of CaCo3 (Calcite) Nano Particles from Cockle Shells using Chitosan as Precursor. Int J Sci Res Publ 2014;4(10):1-5.##Karim MR, Rahman MA, Miah MAJ, Ahmad H, Yanagisawa M, Ito M. Synthesis of γ-alumina particles and surface characterization. The Open Colloid Sci J 2011;4:32-36.##Hariharan M, Varghese N, Cherian B, Paul J, Benny AS. Effect of chitosan on the size distribution of alpha alumina nano particles. Int J Chem Sci Appl 2014;5(3):126-131.##Chuang CC, Shiu JS, Lin JL. Interaction of hydrazine and ammonia with TiO2. Phys Chem Chem Phys 2000;2:2629-2633.##Dirtu D, Odochian L, Pui A, Humelnicu I. Thermal decomposition of ammonia. N2H4-an intermediate reaction product. Eur J Chem 2006;4(4):10-14.##Bhowmick S, Ali N. Recent developments in leishmaniasis vaccine delivery systems. Expert Opin Drug Deliv 2008;5(7):789-803.##Doroud D, Rafati S. Leishmaniasis: focus on the design of nanoparticulate vaccine delivery systems. Expert Rev of Vaccines 2012;11(1):69-86.##Besteiro S, Williams RA, Coombs GH, Mottram JC. Protein turnover and differentiation in Leishmania. Int J Parasitol 2007;37(10):1063-1075.##Williams RA, Tetley L, Mottram JC, Coombs GH. Cysteine peptidases CPA and CPB are vital for autophagy and differentiation in Leishmania mexicana. Mol Microbiol 2006;61(3):655-674.##Li H, Li Y, Jiao J, Hu HM. Alpha-alumina nanoparticle induce efficient autophagy-dependent cross-presentation and potent antitumor response. Nat Nanotechnol 2011;6(10):645-650.##Ghosn EE, Cassado AA, Govoni GR, Fukuhara T, Yang Y, Monack DM, et al. Two physically, functionally, and developmentally distinct peritoneal macrophage subsets. Proc Natl Acad Sci USA 2010;107(6):2568-2573.##Dong E, Wang Y, Yang ST, Yuan Y, Nie H, Chang Y, et al. Toxicity of nano gamma alumina to neural stem cells. J Nanosci Nanotechnol 2011;11(9):7848-7856.##Chen L, Zhang B, Toborek M. Autophagy is involved in nanoalumina- induced cerebrovascular toxicity. Nanomedicine 2013;9(2):212-221.##Franchi L, N&#250;&#241;ez G. The Nlrp3 inflammasome is critical for aluminium hydroxide-mediated IL-1beta secretion but dispensable for adjuvant activity. Eur J Immunol 2008;38(8):2085-2089.##Shi CS, Shenderov K, Huang NN, Kabat J, Abu-Asab M, Fitzgerald KA, et al. Activation of autophagy by inflammatory signals limits IL-1beta production by targeting ubiquitinated inflammasomes for destruction. Nat Immunol 2012;13(3):255-263.##</REF>
        </REFRENCE>
    </REFRENCES>
</ARTICLE>

<ARTICLE>
    <TitleE>Efficient Media for High Lipase Production: One Variable at a Time Approach</TitleE>
    <TitleF></TitleF>
    <TitleLang_ID>2</TitleLang_ID>
    <ABSTRACTS>

        <ABSTRACT>
            <Language_ID>2</Language_ID>
            <CONTENT>&lt;p&gt;Background: Lipase enzymes have applications in a wide range of industries. A crucial determining factor of industrial prices of these enzymes is the culture media composition that is constantly under review by researchers. In this work, for maximum lipase production by &lt;em&gt;Bacillus sp. ZR-5&lt;/em&gt;, culture media compositions were optimized using &amp;quot;one variable at a time&amp;quot; strategy.&lt;br /&gt;
Methods: For this purpose, the culture medium parameters such as low and high cost carbon and nitrogen sources, substrates and incubation times were evaluated.&lt;br /&gt;
Results: Maximum lipase activity was achieved after 24&lt;em&gt; hr&lt;/em&gt; of incubation with 1.5% of glucose syrup (1600&amp;plusmn;69.1 &lt;em&gt;u/mg&lt;/em&gt;), 1% of fish powder (1238&amp;plusmn;36.7 &lt;em&gt;u/mg&lt;/em&gt;) and olive oil (1407&amp;plusmn;2.1 &lt;em&gt;u/mg&lt;/em&gt;) as low cost carbon and nitrogen sources and substrate, respectively.&lt;br /&gt;
Conclusion: Our results show a significant increase in lipase activity with usage of low cost sources; this could help in reducing the media prices for industrial application of lipase enzyme.&lt;/p&gt;
</CONTENT>
        </ABSTRACT>
    </ABSTRACTS>
    <PAGES>
        <PAGE>
            <FPAGE>82</FPAGE>
            <TPAGE>86</TPAGE>
        </PAGE>
    </PAGES>
    <AUTHORS>
        <AUTHOR>
<Name>Safoura</Name>
<MidName></MidName>
<Family>Soleymani</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Department of Pharmaceutical Biotechnology, Isfahan Pharmaceutical Sciences Research Center, Faculty of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Department of Pharmaceutical Biotechnology, Isfahan Pharmaceutical Sciences Research Center, Faculty of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Houri</Name>
<MidName></MidName>
<Family>Alizadeh</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Department of Pharmaceutical Biotechnology, Isfahan Pharmaceutical Sciences Research Center, Faculty of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Department of Pharmaceutical Biotechnology, Isfahan Pharmaceutical Sciences Research Center, Faculty of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Hossein</Name>
<MidName></MidName>
<Family>Mohammadian</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Department of Pharmaceutical Biotechnology, Isfahan Pharmaceutical Sciences Research Center, Faculty of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Department of Pharmaceutical Biotechnology, Isfahan Pharmaceutical Sciences Research Center, Faculty of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Emad</Name>
<MidName></MidName>
<Family>Rabbani</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Department of Biology, Faculty of Basic Sciences, University of Isfahan</Organization>
</Organizations>
<Universities>
<University>Department of Biology, Faculty of Basic Sciences, University of Isfahan</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Fatemeh</Name>
<MidName></MidName>
<Family>Moazen</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Department of Pharmaceutical Biotechnology, Isfahan Pharmaceutical Sciences Research Center, Faculty of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Department of Pharmaceutical Biotechnology, Isfahan Pharmaceutical Sciences Research Center, Faculty of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Hamid</Name>
<MidName></MidName>
<Family>MirMohammad Sadeghi</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Department of Pharmaceutical Biotechnology, Isfahan Pharmaceutical Sciences Research Center, Faculty of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Department of Pharmaceutical Biotechnology, Isfahan Pharmaceutical Sciences Research Center, Faculty of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Ziaedin</Name>
<MidName></MidName>
<Family>Samsam Shariat</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Department of Biochemistry, Faculty of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Department of Biochemistry, Faculty of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Zahra</Name>
<MidName></MidName>
<Family>Etemadifar</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Department of Biology, Faculty of Basic Sciences, University of Isfahan</Organization>
</Organizations>
<Universities>
<University>Department of Biology, Faculty of Basic Sciences, University of Isfahan</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Mohammed</Name>
<MidName></MidName>
<Family>Rabbani</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Department of Pharmaceutical Biotechnology, Isfahan Pharmaceutical Sciences Research Center, Faculty of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Department of Pharmaceutical Biotechnology, Isfahan Pharmaceutical Sciences Research Center, Faculty of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR>
    </AUTHORS>
    <KEYWORDS>
        <KEYWORD><KeyText>&lt;i&gt; Basillus pumilus ZR-5&lt;/i&gt;</KeyText></KEYWORD><KEYWORD><KeyText>Culture media</KeyText></KEYWORD><KEYWORD><KeyText>Lipase enzyme </KeyText></KEYWORD>
    </KEYWORDS>
    <PDFFileName>271.pdf</PDFFileName>
    <REFRENCES>
        <REFRENCE>
            <REF>Gupta R, Gupta N, Rathi P. Bacterial lipases: an overview of production, purification and biochemical properties. Appl Microbiol Biotechnol 2004;64(6):763-781.##Mukesh Kumar DJ, Rajan R, Priyadarshini S, Lawrence L, Sandhiyachittybabu, Kalaichelvan PT. Characterization of lipase and protease from Serratia marcescens DEPTK21 and its destaining capability. Asian J Exp Biol Sci 2012;3(3):621-628.##Hasan F, Hameed A. Optimization of lipase production from Bacillus sp. Pak J Bot 2001;3:789-795.##Jaeger KE, Eggert T. Lipases for biotechnology. Curr Opin Biotechnol 2002;13(4):390-397.##Gupta R, Beg QK, Lorenz P. Bacterial alkaline proteases: molecular approaches and industrial applications. Appl Microbiol Biotechnol 2002;59(1):15-32.##Rajkumar R, Jayappriyan KR, Rengasamy R. Purification and characterization of a protease produced by Bacillus megaterium RRM2: application in detergent and dehairing industries. J Basic Microbiol 2011;51(6):614-624.##Ebrahimpour A, Abd Rahman RN, Ean Ch&#39;ng DH, Basri M, Salleh AB. A modeling study by response surface methodology and artificial neural network on culture parameters optimization for thermostable lipase production from a newly isolated thermophilic Geobacillus sp. strain ARM. BMC Biotechnol 2008;8:96.##Eggert T, van Pouderoyen G, Pencreac&#39;h G, Douchet I, Verger R, Dijkstra BW, et al. Biochemical properties and three-dimensional structures of two extracellular lipolytic enzymes from Bacillus subtilis. Colloids Surf B Biointerfaces 2002;26(1-2):37-46.##Sangeetha R, Arulpandi I, Geetha A. Bacterial lipases as potential industrial biocatalysts: An overview. Res J Microbiol 2011;6(1):1-24.##Hasan F, Shah AA, Hameed A. Methods for detection and characterization of lipases: A comprehensive review. Biotechnol Adv 2009;27(6):782-798.##Khoramnia A, Lai Ming O, Ebrahimpour A, Tanduba CJ, Voon TS, Mukhlis S. Thermostable lipase from a newly isolated Staphylococcus xylosus strain; process optimization and characterization using RSM and ANN. Electron J Biotechnol 2010;13:15-16.##Haddar A, Fakhfakh-Zouari N, Hmidet N, Frikha F, Nasri M, Kamoun AS. Low-cost fermentation medium for alkaline protease production by Bacillus mojavensis A21 using hulled grain of wheat and sardinella peptone. J Biosci Bioeng 2010;110(3):288-294.##Sabat S, Murthy VK, Pavithra M, Mayur P, Chandavar A. Production and characterisation of extracellular lipase from Bacillus stearothermophilus MTCC 37 under different fermentation conditions. Int J Eng Res Appl 2012;2(3):1775-1781.##Samad MYA, Razak CNA, Salleh AB, Zin Wan Yunus WM, Ampon K, Basri M. A plate assay for primary screening of lipase activity. J Microbiol Methods 1989;9(1):51-56.##Sharma D, Sharma B, Shukla AK. Biotechnological approach of microbial lipase: a review. Biotechnology 2011;10(1):23-40.##Holm C, Osterlund T, Laurell H, Contreras JA. Molecular mechanisms regulating hormone-sensitive lipase and lipolysis. Annu Rev Nutr 2000;20:365-393.##Gandhi NN. Applications of lipase. J Am Oil Chem Soc 1997;74(6):621-634.##Thakur S. Lipases, its sources, properties and applications: a review. Int J Sci Eng Res 2012;3(7):1-29.##Lima VM, Krieger N, Sarquis MIM, Mitchell DA, Ramos LP, Fontana JD. Effect of nitrogen and carbon sources on lipase production by Penicillium aurantiogriseum. Food Technol Biotechnol 2003;41(2):105-110.##Messias JM, da Costa BZ, de Lima VM, Dekker RF, Rezende MI, Krieger N, et al. Screening Botryosphaeria species for lipases: production of lipase by Botryosphaeria ribis EC-01 grown on soybean oil and other carbon sources. Enzyme Microb Technol 2009;45(6-7):426-431.##Nair S, Kumar P. Molecular characterization of a lipase-producing Bacillus pumilus strain (NMSN-1d) utilizing colloidal water-dispersible polyurethane. World J Microbiol Biotechnol 2007;23(10):1441-1449.##Thomas A, Mathew M, Valsa A, Mohan S, Manjula R. Optimisation of growth conditions for the production of extracellular lipase by Bacillus mycoides. Indian J Microbiol 2003;43(1):67-69.##Saxena R, Ghosh P, Gupta R, Davidson WS, Bradoo S, Gulati R. Microbial lipases: potential biocatalysts for the future industry. Curr Sci 1999;77(1):101-115.##Costa E, TeixidE N, Usall J, AtarAt E, Vi, V I. The effect of nitrogen and carbon sources on growth of the biocontrol agent Pantoea agglomerans strain CPA-2. Lett Appl Microbiol 2002;35(2):117-120.##Sirisha E, Rajasekar N, Narasu ML. Isolation and optimization of lipase producing bacteria from oil contaminated soils. Adv Biol Res 2010;4(5):249-252.##Song QX, Lin JP, Rong YP, Wei DZ. [Studies on lipase production from Candida rugosa]. Sheng Wu Gong Cheng Xue Bao. 2001;17(1):101-104. Chinese.##Zhang H, Zhang F, Li Z. Gene analysis, optimized production and property of marine lipase from Bacillus pumilus B106 associated with South China Sea sponge Halichondria rugosa. World J Microbiol Biotechnol 2009;25(7):1267-1274.##Bora L, Kalita M. Production of extra cellular lipase from Bacillus sp LBN 4 by solid state fermentation. Internet J Microbiol 2008;7(2):1-4.##</REF>
        </REFRENCE>
    </REFRENCES>
</ARTICLE>

<ARTICLE>
    <TitleE>Evaluation of IgY Antibody as a Polyspecific Coombs-Reagent</TitleE>
    <TitleF></TitleF>
    <TitleLang_ID>2</TitleLang_ID>
    <ABSTRACTS>

        <ABSTRACT>
            <Language_ID>2</Language_ID>
            <CONTENT>&lt;p&gt;Background: During the last twenty years, the extraction of specific egg yolk (IgY) antibodies from the immunized chickens has been accepted as a useful alternative to the immunization of mammals. The aim of the present study was immunizing the chickens with Human Umbilical Cord Serum (HUCS) and the extraction of specific anti-human globulins (IgG, C3b, and C3d) antibodies from egg yolk in order to obtain polyspecific Coombs reagent.&lt;br /&gt;
Methods: The novelty of this work was the achievement of a polyclonal reagent through a very cheap alternative method in accordance with all ethical regulations required for obtaining it. Three Leghorn hens (21 weeks old) were immunized four times for a period of 66 days with 20uL of HUCS mixed with PBS/FCA or FIA each time. The extraction of IgY antibodies was performed according to the method of lipid precipitation of yolk and using water soluble fraction as the reagent material. The resulting IgY antibody&amp;nbsp; was characterized by SDS-PAGE and immunoelectrophoresis and tested for the presence of hetero-agglutinins by means of direct agglutination using human erythrocytes of all blood groups treated with 0.1% papain and for indirect Coombs-test to evaluate its specificity to fractions (C3b, C3d, C4d) of human complement and human IgG, respectively.&lt;br /&gt;
Results: Our findings show, that, the reagent obtained contains IgY and other 3 proteins (SDS-PAGE), and reacts specifically with plasma proteins, that migrate in &amp;beta; and &amp;upsih; regions. In immunoelectrophoresis, in addition, there is the presence of low hetero-agglutinins levels in IgY-preparation (3 lots), and the possibility to produce high amount (more than 500 &lt;em&gt;ml/egg&lt;/em&gt;) of polyspecific Coombs-reagent in chickens is also discussed.&lt;br /&gt;
Conclusion: IgY-preparation (3 lots), and the possibility to produce high amount (more than 500 ml/egg) of polyspecific Coombs-reagent in chickens with the originality to achieve a polyclonal reagent through a very cheap alternative method in accordance with all ethical regulations required for obtaining it, was also discussed.&lt;/p&gt;
</CONTENT>
        </ABSTRACT>
    </ABSTRACTS>
    <PAGES>
        <PAGE>
            <FPAGE>87</FPAGE>
            <TPAGE>93</TPAGE>
        </PAGE>
    </PAGES>
    <AUTHORS>
        <AUTHOR>
<Name>Guti&#233;rrez</Name>
<MidName></MidName>
<Family>Calzado Esteban Justo</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Laboratory of Antibodies and Experimental Biomodels, Center of Molecular Immunology</Organization>
</Organizations>
<Universities>
<University>Laboratory of Antibodies and Experimental Biomodels, Center of Molecular Immunology</University>
</Universities>
<Countries>
<Country>Cuba</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Toledano</Name>
<MidName></MidName>
<Family>Heredia Marlene</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Laboratory of Antibodies and Experimental Biomodels, Center of Molecular Immunology</Organization>
</Organizations>
<Universities>
<University>Laboratory of Antibodies and Experimental Biomodels, Center of Molecular Immunology</University>
</Universities>
<Countries>
<Country>Cuba</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Fernadez</Name>
<MidName></MidName>
<Family>Duharte Jeorge</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Laboratory of Antibodies and Experimental Biomodels, Center of Molecular Immunology</Organization>
</Organizations>
<Universities>
<University>Laboratory of Antibodies and Experimental Biomodels, Center of Molecular Immunology</University>
</Universities>
<Countries>
<Country>Cuba</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Amir-Hassan</Name>
<MidName></MidName>
<Family>Zarnani</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Reproductive Biotechnology Research Center, Avicenna Research Institute, ACECR</Organization>
</Organizations>
<Universities>
<University>Reproductive Biotechnology Research Center, Avicenna Research Institute, ACECR</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR>
    </AUTHORS>
    <KEYWORDS>
        <KEYWORD><KeyText>Chicken</KeyText></KEYWORD><KEYWORD><KeyText>Egg yolk antibody</KeyText></KEYWORD><KEYWORD><KeyText>Immunization</KeyText></KEYWORD><KEYWORD><KeyText>Immunoglobulins</KeyText></KEYWORD>
    </KEYWORDS>
    <PDFFileName>272.pdf</PDFFileName>
    <REFRENCES>
        <REFRENCE>
            <REF>Dos Santos Alisson Jos&#233;. Technical Manual of AABB; USA: Bethesda, Maryland, 2006.##RougerPh, SalmonCh. La Practique de l’agglutination des erythrocytes et le test de Coombs Paris: Masson, &#233;d, 1981.##Fernandes HP, Cesar CL, Barjas-Castro Mde L. Electrical properties of the red blood cell membrane and immunohematological investigation. Rev Bras Hematol Hemoter 2011;33(4):297-301.##Stites DP, Stobo JD, Fudenberg HH, Wells JV. [Inmunolog&#237;a B&#225;sica y Cl&#237;nica]. Mexico: El manual moderno; 1985.  p. 349-351. Spanish.##Wallach J. [Interpretaci&#243;n Cl&#237;nica de las Pruebas de Laboratorio]. 4th ed. Barcelona: Masson; 2003. p. 213-226. Spanish.##Fey H, Butler R, Marty F. Immunization of pregnant cows with human IgG. Box Sang 1973;25:245-253.##Schade R, Pfister C, Halatsch R, Henklein P. Polyclonal IgY antibodies from chicken egg yolk- An alternative to the production of mammalian IgG type antibodies in rabbit. ATLA-19. 1991:403-419.##Akita EM, Nakai S. Comparison of four purification methods for the production of immunoglobulins from eggs laid by hens immunized with enterotoxigenic E. coli strain. J Immunol Methods 1993;160(2):207-214.##Fichtali J, Charter EA, Lo KV, Nakai S. Purification of antibodies from industrially separated egg yolk. J Food Sci 1993;58(6):1282-1285.##Larsson A, Bal&#246;w RM, Lindahl TL, Forsberg PO. Chicken antibodies: taking advantage of evolution--a review. Poult Sci 1993;72(10):1807-1812.##Schade R, Staak Ch, Hendriksen C, Erhard M, Hugl H, Koch G, et al. The production of avian (egg yolk) antibodies: IgY. The report and recommendations of ECVAM workshop 21. ATLA-NOTTINGHAM-24. 1996:925-934.##Charter EA, Fichtali J, Lo VK. High performance liquid chromatography analysis of egg yolk immunoglobulins. Int JBC 1995;1:199-208.##Warr GW, Mayor KE, Higgins DA. IgY: clues to the origins of modern antibodies. Immunol Today 1995;16 (8):392-398.##Grebenchtchikov N, van der Ven-Jongekrijg J, Pesman GJ, Geurts-Moespot A, van der Meer JW, Sweep FC. Development of a sensitive ELISA for the quantification of human tumour necrosis factor-a using 4 polyclonal antibodies. Eur Cytokine Netw 2005;16(3):215-222.##Jintaridth P, Srisomsap C, Vichittumaros K, Kalpravidh RW, Winichagoon P, Fucharoen S, et al.Chicken egg yolk antibodies specific for the gamma chain of human hemoglobin for diagnosis of thalassemia. Int J Hematol 2006;83(5):408-414. ##Sato Y, Nishimichi N, Nakano A, Takikawa K, Inoue N, Matsuda H, et al. Determination of LOX 1-ligand activity in mouse plasma with a chicken monoclonal antibody for ApoB. Atherosclerosis 2008;200(2):303-309.##Morar D, Tijhaar E, Negrea A, Hendriks J, van Haarlem D, Godfroid J, et al. Cloning, sequencing and expression of white rhinoceros (Ceratotherium simum) interferon-gamma (IFN-gamma) and the production of rhinoceros IFN-gamma specific antibodies. Vet Immunol Immunopathol 2007;115(1-2):146-154.##Sinnreich M, Shaw CA, Pari G, Nalbantoglu J, Holland PC, Karpati G. Localization of coxsackie virus and adenovirus receptor (CAR) in normal and regenerating human muscle. Neuromuscul Disord 2005;15(8):541-548.##Mao Y, Wu J, Skog S, Eriksson S, Zhao Y, Zhou J, et al. Expression of cell proliferating genes in patients with non-small cell lung cancer by immunohistochemistry and cDNA profiling. Oncol Rep 2005;13(5):837-846.##Esslimani-Sahla M, Kramar A, Simony Lafontaine J, Warner M, Gustafsson JA, Rochefort H. Increased estrogen receptor betacx expression during mammary carcinogenesis. Clin Cancer Res 2005;11(9):3170-3174.##Lemamy GJ, Sahla ME, Berthe ML, Roger P. Is the mannose 6-phosphate/insulin-like growth factor 2 receptor coded by a breast cancer suppressor gene? Adv Exp Med Biol 2008;617:305-310.##Xiao Y, Gao X, Gannot G, Emmert-Buck MR, Srivastava S, Wagner PD, et al. Quantitation of HER2 and telomerase biomarkers in solid tumors with IgY antibodies and nanocrystal detection. Int J Cancer 2008;122(10):2178-2186.##Xiao Y, Gao X, Taratula O, Treado S, Urbas A, Hol-brook RD, et al. Anti-HER2 IgY antibody-functionalized single-walled carbon nanotubes for detection and selective destruction of breast cancer cells. BMC Cancer 2009;9:351.##Xiao Yan, Gao X. Use of IgY antibodies and semiconductor nanocrystal detection in cancer biomarker quantitation. Biomark Med 2010;4(2):227-239.##Guti&#233;rrez Calzado E, Cruz Marino E, Samon Ch&#225;vez T, V&#225;zquez Luna E, Corona Ochoa Z, Schade R. Extraction of a monospecific coombs-reagent from chicken eggs. ALTEX 2003;20(1):21-25.##Fischbach F. A Manual of Laboratory and Diagnostic Test. 4th ed. Philadelphia: Lippincott Williams &amp; Wilkins; 1992. p. 458-656.##Margni RA. [Inmunolog&#237;a e Inmunoquimica]. 3rd ed. Buenos Aires; Medica Panamericana; 1982. 1045 p. Spanish.##Western Blotting Technical Manual. Polyacrylamide Gel Electrophoresis of proteins and total protein detection in polyacrylamide gel. UK: Amershan International Plc; 1991:7-11.##Jones JM, Kekwick RA, Goldsmith LG. Influence of polymer on the efficacy of serum albumin as a potentiator of incomplete Rh agglutinin. Nat 1969;22:510-511.##Sonnenwirth AC, Leonard J. M&#233;todos y Diagn&#243;sticos del Laboratorio Cl&#237;nico (1009-1056). 2nd ed. La Habana, Cuba: Editorial Cient&#237;fico T&#233;cnica; 1983. 188 p.##Food and Drug Administration. Recommended methods for anti human globulin evaluation. Docket No. 848-0182. March 1992. 32 p.##</REF>
        </REFRENCE>
    </REFRENCES>
</ARTICLE>

<ARTICLE>
    <TitleE>The Effect of Interactions of Single Nucleotide Polymorphisms of APOA1/APOC3 with Food Group Intakes on the Risk of Metabolic Syndrome</TitleE>
    <TitleF></TitleF>
    <TitleLang_ID>2</TitleLang_ID>
    <ABSTRACTS>

        <ABSTRACT>
            <Language_ID>2</Language_ID>
            <CONTENT>&lt;p&gt;Background: The aim of this study was to examine the interaction of dietary food groups and genetic variants of APOA1/APOC3, relative to Metabolic Syndrome (MetS) risk in adults.&lt;br /&gt;
Methods: In this matched nested case-control study, 414 MetS subjects and 414 controls were selected from among participants of Tehran Lipid and Glucose Study. Dietary intake was assessed with the use of a valid and reliable semi-quantitative food frequency questionnaire. Single Nucleotide Polymorphisms (SNPs), APOA1 (rs670, -75G&amp;gt;A and rs5069, +83C&amp;gt;T/APOC3 rs5128 C3238&amp;gt;G) were genotyped by the conventional polymerase chain reaction and restriction fragment length polymorphism.&lt;br /&gt;
Results: The mean (SD) of age was 40.7 (13) and 41.2 (13) years in male cases and controls versus 44.0 (11) and 44.0 (12) years in female case and controls. A significant interaction between intake quartiles of the sugar group and APOA1 combined group (GA+AA/CT+TT) SNPs was found; The ORs for these genotype carriers were (1, 0.44, 0.36, 0.23; P trend&amp;lt;0.001) in quartiles of intake, relative to other combined genotypes (P interaction=0.02). MetS risk appeared to be increased significantly in higher quartiles of sweet beverages and fish intakes in the GA+AA/CT+TT/CC genotypes of APOA1/APOC3 SNPs, compared to other genotypes (P interaction=0.01). The combined effect of genotypes of APOC3/APOA1 showed further decrease in MetS risk in higher quartiles of sugar group intakes (OR: 1, 0.24, 0.26, 0.14, P trend=0.001) relative to other combinations (P interaction=0.008).&lt;br /&gt;
Conclusion: Results obtained demonstrate that some dietary food groups (sugar, fish, and sweet beverages) modulate the effect of APOA1/APOC3 SNPs in relation to MetS risk.&lt;/p&gt;
</CONTENT>
        </ABSTRACT>
    </ABSTRACTS>
    <PAGES>
        <PAGE>
            <FPAGE>94</FPAGE>
            <TPAGE>103</TPAGE>
        </PAGE>
    </PAGES>
    <AUTHORS>
        <AUTHOR>
<Name>Firoozeh</Name>
<MidName></MidName>
<Family>Hosseini-Esfahani</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Nutrition and Endocrine Research Center, Research Institute for Endocrine Sciences, Shahid Beheshti University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Nutrition and Endocrine Research Center, Research Institute for Endocrine Sciences, Shahid Beheshti University of Medical Sciences</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Parvin</Name>
<MidName></MidName>
<Family>Mirmiran</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Nutrition and Endocrine Research Center, Research Institute for Endocrine Sciences, Shahid Beheshti University of Medical SciencesFaculty of Nutrition Sciences and Food Technology, National Nutrition and Food Technology Research Institute, Shahid Beheshti University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Nutrition and Endocrine Research Center, Research Institute for Endocrine Sciences, Shahid Beheshti University of Medical SciencesFaculty of Nutrition Sciences and Food Technology, National Nutrition and Food Technology Research Institute, Shahid Beheshti University of Medical Sciences</University>
</Universities>
<Countries>
<Country>IranIran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Maryam</Name>
<MidName></MidName>
<Family>S. Daneshpour</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Cellular Molecular and Endocrine Research Center, Research Institute for Endocrine Sciences, Shahid Beheshti University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Cellular Molecular and Endocrine Research Center, Research Institute for Endocrine Sciences, Shahid Beheshti University of Medical Sciences</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Azadeh</Name>
<MidName></MidName>
<Family>Mottaghi</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Nutrition and Endocrine Research Center, Research Institute for Endocrine Sciences, Shahid Beheshti University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Nutrition and Endocrine Research Center, Research Institute for Endocrine Sciences, Shahid Beheshti University of Medical Sciences</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Fereidoun</Name>
<MidName></MidName>
<Family>Azizi</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Endocrine Research Center, Research Institute for Endocrine Sciences, Shahid Beheshti University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Endocrine Research Center, Research Institute for Endocrine Sciences, Shahid Beheshti University of Medical Sciences</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR>
    </AUTHORS>
    <KEYWORDS>
        <KEYWORD><KeyText>Food</KeyText></KEYWORD><KEYWORD><KeyText>Genetic polymorphisms</KeyText></KEYWORD><KEYWORD><KeyText>Metabolic Syndrome</KeyText></KEYWORD>
    </KEYWORDS>
    <PDFFileName>273.pdf</PDFFileName>
    <REFRENCES>
        <REFRENCE>
            <REF>Mills G, Avery PJ, McCarthy MI, Hattersley AT, Levy JC, Hitman GA, et al. Heritability estimates for beta cell function and features of the insulin resistance syndrome in UK families with an increased susceptibility to type 2 diabetes. Diabetologia 2004;47(4):732-738.##Rich SS. Mapping genes in diabetes. Genetic epidemiological perspective. Diabetes 1990;39(11):1315-1319.##Al-Shaer MH, AbuSabha H. The impact of ethnicity on the lifetime risk of the metabolic syndrome and diabetes mellitus. Am J Cardiol 2005;95(6):819-820.##Poulsen P, Vaag A, Kyvik K, Beck-Nielsen H. Genetic versus environmental aetiology of the metabolic syndrome among male and female twins. Diabetologia 2001;44(5):537-543.##Phillips CM. Nutrigenetics and metabolic disease: current status and implications for personalised nutrition. Nutrients 2013;5(1):32-57.##Marcadenti A. Diet, cardiometabolic factors and type-2 diabetes mellitus: the role of genetics. Curr Diabetes Rev 2016;12(4)322-330.##Joseph J, Loscalzo J. Nutri(meta)genetics and cardiovascular disease: novel concepts in the interaction of diet and genomic variation. Curr Atheroscler Rep 2015;17(5):505.##Ginsberg HN, MacCallum PR. The obesity, metabolic syndrome, and type 2 diabetes mellitus pandemic: Part I. Increased cardiovascular disease risk and the importance of atherogenic dyslipidemia in persons with the metabolic syndrome and type 2 diabetes mellitus. J Cardiometab Syndr 2009;4(2):113-119.##Ascaso JF, Fern&#225;ndez-Cruz A, Gonz&#225;lez Santos P, Hern&#225;ndez Mijares A, Mangas Rojas A, Mill&#225;n J, et al. Significance of high density lipoprotein-cholesterol in cardiovascular risk prevention: recommendations of the HDL Forum. Am J Cardiovasc Drugs 2004;4(5):299-314.##Heng CK, Low PS, Saha N. Variations in the promoter region of the apolipoprotein A-1 gene influence plasma lipoprotein (a) levels in Asian Indian neonates from Singapore. Pediatr Res 2001;49(4):514-518.##Smach MA, Edziri H, Charfeddine B, Ben Othman L, Lammouchi T, Ltaief A, et al. Polymorphism in apoA1 influences high-density lipoprotein cholesterol levels but is not a major risk factor of alzheimer&#39;s disease. Dement Geriatr Cogn Dis Extra 2011;1(1):249-257.##Albahrani AI, Usher JJ, Alkindi M, Marks E, Ranganath L, Al-yahyaee S. ApolipoproteinA1-75 G/A (M1-) polymorphism and lipoprotein (a); anti-vs. pro-atherogenic properties. Lipids Health Dis 2007;6:19.##Chen ES, Mazzotti DR, Furuya TK, Cendoroglo MS, Ramos LR, Araujo LQ, et al. Apolipoprotein A1 gene polymorphisms as risk factors for hypertension and obesity. Clin Exp Med 2009;9(4):319-325.##Phillips CM, Goumidi L, Bertrais S, Field MR, McManus R, Hercberg S, et al. Gene-nutrient interactions and gender may modulate the association between ApoA1 and ApoB gene polymorphisms and metabolic syndrome risk. Atherosclerosis 2011;214 (2):408-414.##Hallman DM, Srinivasan SR, Chen W, Boerwinkle E, Berenson GS. Longitudinal analysis of haplotypes and polymorphisms of the APOA5 and APOC3 genes associated with variation in serum triglyceride levels: the Bogalusa Heart Study. Metabolism 2006;55(12):1574-1581.##Song Y, Zhu L, Richa M, Li P, Yang Y, Li S. Associations of the APOC3 rs5128 polymorphism with plasma APOC3 and lipid levels: a meta-analysis. Lipids Health Dis 2015;14:32.##Rudkowska I, Dewailly E, Hegele RA, Boiteau V, Dub&#233;-Linteau A, Abdous B, et al. Gene-diet interactions on plasma lipid levels in the Inuit population. Br J Nut 2013;109(05):953-961.##Azizi F, Ghanbarian A, Momenan AA, Hadaegh F, Mirmiran P, Hedayati M, et al. Prevention of non-communicable disease in a population in nutrition transition: Tehran Lipid and Glucose Study phase II. Trials 2009;10:5.##Esfahani FH, Asghari G, Mirmiran P, Azizi F. Reproducibility and relative validity of food group intake in a food frequency questionnaire developed for the Tehran Lipid and Glucose Study. J Epidemiol 2010;20(2):150-158.##Hosseini-Esfahani F, Djazaieri SA, Mirmiran P, Mehrabi Y, Azizi F. Which food patterns are predictors of obesity in Tehranian adults? J Nutr Educ Behav 2012;44(6):564-573.##Mirmiran P, Esfahani FH, Mehrabi Y, Hedayati M, Azizi F. Reliability and relative validity of an FFQ for nutrients in the Tehran lipid and glucose study. Public Health Nutr 2010;13(5):654-662.##Ainsworth BE, Haskell WL, Whitt MC, Irwin ML, Swartz AM, Strath SJ, et al. Compendium of physical activities: an update of activity codes and MET intensities. Med Sci Sports Exerc 2000;32(9 Suppl):S498-504.##Kriska AM, Knowler WC, LaPorte RE, Drash AL, Wing RR, Blair SN, et al. Development of questionnaire to examine relationship of physical activity and diabetes in Pima Indians. Diabetes Care 1990;13(4):401-411.##Momenan AA, Delshad M, Sarbazi N, Rezaei Ghaleh N, Ghanbarian A, Azizi F. Reliability and validity of the Modifiable Activity Questionnaire (MAQ) in an Iranian urban adult population. Arch Iran Med 2012;15(5):279-282.##Daneshpour MS, Faam B, Mansournia MA, Hedayati M, Halalkhor S, Mesbah-Namin SA, et al. Haplotype analysis of Apo AI-CIII-AIV gene cluster and lipids level: Tehran Lipid and Glucose Study. Endocrine 2012;41(1):103-110.##Truett GE, Heeger P, Mynatt RL, Truett AA, Walker JA, Warman ML. Preparation of PCR-quality mouse genomic DNA with hot sodium hydroxide and tris (HotSHOT). Biotechniques 2000;29(1):52, 54.##Zou Y, Hu D, Yang X, Jia X, Wang L, Cui L, et al. Relationships among apolipoprotein A1 gene polymorphisms, lipid levels and coronary atherosclerosis disease. Chin Med J (Engl) 2003;116(5):665-668.##Azizi F, Hadaegh F, Khalili D, Esteghamati A, Hosseinpanah F, Delavari A, et al. Appropriate definition of metabolic syndrome among Iranian adults: report of the Iranian National Committee of Obesity. Arch Iran Med 2010;13(5):426-428.##Grundy SM, Hansen B, Smith SC Jr, Cleeman JI, Kahn RA. Clinical management of metabolic syndrome: report of the American Heart Association/National Heart, Lung, and Blood Institute/American Diabetes Association conference on scientific issues related to management. Arterioscler Thromb Vasc Biol 2004;24(2):e19-24.##Barrio-Lopez MT, Martinez-Gonzalez MA, Fernandez-Montero A, Beunza JJ, Zazpe I, Bes-Rastrollo M. Prospective study of changes in sugar-sweetened beverage consumption and the incidence of the metabolic syndrome and its components: the SUN cohort. Br J Nutr 2013;110(9):1722-1731.##Khosravi-Boroujeni H, Sarrafzadegan N, Mohammadi-fard N, Alikhasi H, Sajjadi F, Asgari S, et al. Consump-tion of sugar-sweetened beverages in relation to the metabolic syndrome among Iranian adults. Obes Facts 2011;5(4):527-537.##Lutsey PL, Steffen LM, Stevens J. Dietary Intake and the development of the metabolic syndrome the Atherosclerosis Risk in Communities Study. Circulation 2008;117(6):754-761.##Qi Q, Chu AY, Kang JH, Jensen MK, Curhan GC, Pasquale LR, et al. Sugar-sweetened beverages and genetic risk of obesity. N Engl J Med 2012;367(15):1387-1396.##Nettleton JA, Lutsey PL, Wang Y, Lima JA, Michos ED, Jacobs DR Jr. Diet soda intake and risk of incident metabolic syndrome and type 2 diabetes in the Multi-Ethnic Study of Atherosclerosis (MESA). Diabetes Care 2009;32(4):688-694.##Dhingra R, Sullivan L, Jacques PF, Wang TJ, Fox CS, Meigs JB, et al. Soft drink consumption and risk of developing cardiometabolic risk factors and the metabolic syndrome in middle-aged adults in the community. Circulation 2007;116(5):480-488.##Soory M. Relevance of nutritional antioxidants in metabolic syndrome, ageing and cancer: potential for therapeutic targeting. Infect Disord Drug Targets 2009;9(4):400-414.##Kendall CW, Josse AR, Esfahani A, Jenkins DJ. Nuts, metabolic syndrome and diabetes. Br J Nutr 2010;104(4):465-473.##Garg A, Bonanome A, Grundy SM, Zhang ZJ, Unger RH. Comparison of a high-carbohydrate diet with a high-monounsaturated-fat diet in patients with non-insulin-dependent diabetes mellitus. N Engl J Med 1988;319(13):829-834.##Scott LW, Balasubramanyam A, Kimball KT, Aherns AK, Fordis CM Jr, Ballantyne CM. Long-term, randomized clinical trial of two diets in the metabolic syndrome and type 2 diabetes. Diabetes Care 2003;26(8):2481-2482.##Tapsell LC, Batterham MJ, Teuss G, Tan SY, Dalton S, Quick CJ, et al. Long-term effects of increased dietary polyunsaturated fat from walnuts on metabolic parameters in type II diabetes. Eur J Clin Nutr 2009;63(8):1008-1015.##Li TY, Brennan AM, Wedick NM, Mantzoros C, Rifai N, Hu FB. Regular consumption of nuts is associated with a lower risk of cardiovascular disease in women with type 2 diabetes. J Nutr 2009;139(7):1333-1338.##Estruch R, Mart&#237;nez-Gonz&#225;lez MA, Corella D, Salas-Salvad&#243; J, Ruiz-Guti&#233;rrez V, Covas MI, et al. Effects of a Mediterranean-style diet on cardiovascular risk factors: a randomized trial. Ann Intern Med 2006;145(1):1-11.##Lopez-Miranda J, Ordovas JM, Espino A, Marin C, Salas J, Lopez-Segura F, et al. Influence of mutation in human apolipoprotein A-1 gene promoter on plasma LDL cholesterol response to dietary fat. Lancet 1994;343(8908):1246-1249.##Mata P, Lopez-Miranda J, Pocovi M, Alonso R, Lahoz C, Marin C, et al. Human apolipoprotein A-I gene promotor mutation influences plasma low density lipoprotein cholesterol response to dietary fat saturation. Atherosclerosis 1998;137(2):367-376.##Bahadoran Z, Mirmiran P, Hosseini-Esfahani F, Azizi F. Fast food consumption and the risk of metabolic syndrome after 3-years of follow-up: Tehran Lipid and Glucose Study. Eur J Clin Nutr 2013;67(12):1303-1309.##Qi Q, Chu AY, Kang JH, Huang J, Rose LM, Jensen MK, et al. Fried food consumption, genetic risk, and body mass index: gene-diet interaction analysis in three US cohort studies. BMJ 2014;348:g1610.##Lai YH, Petrone AB, Pankow JS, Arnett DK, North KE, Ellison RC, et al. Association of dietary omega-3 fatty acids with prevalence of metabolic syndrome: the National Heart, Lung, and Blood Institute Family Heart Study. Clin Nutr 2013;32(6):966-969.##Mennen LI, Lafay L, Feskens EJ, Novak M, L&#233;pinay P, Balkau B. Possible protective effect of bread and dairy products on the risk of the metabolic syndrome. Nutr Res 2000;20(3):335-347.##Pašalić D, Dodig S, Corović N, Pizent A, Jurasović J, Pavlović M. High prevalence of metabolic syndrome in an elderly Croatian population - a multicentre study. Public Health Nutr 2011;14(9):1650-1657.##Haffner SM, Knapp JA, Stern MP, Hazuda HP, Rosenthal M, Franco LJ. Coffee consumption, diet, and lipids. Ame J  Epidemiol 1985;122(1):1-12.##Van Dam RM, Feskens EJ. Coffee consumption and risk of type 2 diabetes mellitus. Lancet 2002;360(9344):1477-1478.##Tuomilehto J, Hu G, Bidel S, Lindstr&#246;m J, Jousilahti P. Coffee consumption and risk of type 2 diabetes mellitus among middle-aged Finnish men and women. JAMA 2004;291(10):1213-1219.##Hino A, Adachi H, Enomoto M, Furuki K, Shigetoh Y, Ohtsuka M, et al. Habitual coffee but not green tea consumption is inversely associated with metabolic syndrome: an epidemiological study in a general Japanese population. Diabetes Res Clin Pract 2007;76(3):383-389.##Stensvold I, Tverdal A, Foss OP. The effect of coffee on blood lipids and blood pressure. Results from a Norwegian cross-sectional study, men and women, 40-42 years. J Clin Epidemiol 1989;42(9):877-884.##Salvaggio A, Periti M, Miano L, Zambelli C. Association between habitual coffee consumption and blood pressure levels. J Hypertens 1990;8(6):585-590.##</REF>
        </REFRENCE>
    </REFRENCES>
</ARTICLE>

<ARTICLE>
    <TitleE>Development of Flow Cytometry-Fluorescent In Situ Hybridization (Flow-FISH) Method for Detection of PML/RARa Chromosomal Translocation in Acute Promyelocytic Leukemia Cell Line</TitleE>
    <TitleF></TitleF>
    <TitleLang_ID>2</TitleLang_ID>
    <ABSTRACTS>

        <ABSTRACT>
            <Language_ID>2</Language_ID>
            <CONTENT>&lt;p&gt;Background: Acute Promyelocytic Leukemia (APL) is a subclass of acute myeloid leukemia. The chromosomal aberration in 95% of APL cases is t(15; 17) (q22; q21), which prevents cell differentiation. Characterization of the underlying molecular lesion is valuable in determining optimal treatment strategy. The goal of this study was to develop a new and powerful Flow- FISH technique to detect the long isoform (L) of PML-RARa fusion transcript in NB4 cell line.&lt;br /&gt;
Methods: To achieve the best condition for fixation, two different fixatives including 2% paraformaldehyde and 75% ethanol were used. 0.2% Triton X-100 and 0.2% saponin were used for the permeabilization step .In hybridization, a wide range of times and temperatures were used and probe was designed in FRET system. Results were confirmed by fluorescent microscope assay and reverse transcription PCR.&lt;br /&gt;
Results: In the present study, a novel technique was successfully optimized that combines in situ hybridization with flow cytometry to detect the presence of PML-RARa transcript. Using standard fixation and permeabilization protocol of 2% PFA and 0.2% saponin gave the best fluorescent results in flow cytometry. Also, results indicated that the optimum time and temperature for hybridization was 2 &lt;em&gt;hr&lt;/em&gt; at 42&lt;sup&gt;o&lt;/sup&gt;&lt;em&gt;C&lt;/em&gt;. The results of reverse transcription PCR and fluorescent microscopy confirmed the presence of PML-RARa transcript.&lt;br /&gt;
Conclusion: The concordance between the results of Flow-FISH and those of two other techniques including reverse transcription PCR and FISH indicated that this method would be applicable as a diagnostic test for APL in clinical samples and MRD monitoring.&lt;/p&gt;
</CONTENT>
        </ABSTRACT>
    </ABSTRACTS>
    <PAGES>
        <PAGE>
            <FPAGE>104</FPAGE>
            <TPAGE>108</TPAGE>
        </PAGE>
    </PAGES>
    <AUTHORS>
        <AUTHOR>
<Name>Fatemeh</Name>
<MidName></MidName>
<Family>Zahedipour</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Diagnostic Laboratory Sciences and Technology Research Center, Faculty of Paramedical Sciences, Shiraz University of Medical SciencesStudent Research Committee, Shiraz University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Diagnostic Laboratory Sciences and Technology Research Center, Faculty of Paramedical Sciences, Shiraz University of Medical SciencesStudent Research Committee, Shiraz University of Medical Sciences</University>
</Universities>
<Countries>
<Country>IranIran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Reza</Name>
<MidName></MidName>
<Family>Ranjbaran</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Diagnostic Laboratory Sciences and Technology Research Center, Faculty of Paramedical Sciences, Shiraz University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Diagnostic Laboratory Sciences and Technology Research Center, Faculty of Paramedical Sciences, Shiraz University of Medical Sciences</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Abbas</Name>
<MidName></MidName>
<Family>Behzad-Behbahani</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Diagnostic Laboratory Sciences and Technology Research Center, Faculty of Paramedical Sciences, Shiraz University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Diagnostic Laboratory Sciences and Technology Research Center, Faculty of Paramedical Sciences, Shiraz University of Medical Sciences</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Khalil</Name>
<MidName></MidName>
<Family>Tavakol Afshari</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Buali Research Institute, Immunology Research Center, Immunogenetic and Cell Culture Lab, Mashhad University of Medical Science</Organization>
</Organizations>
<Universities>
<University>Buali Research Institute, Immunology Research Center, Immunogenetic and Cell Culture Lab, Mashhad University of Medical Science</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Mohammad Ali</Name>
<MidName></MidName>
<Family>Okhovat</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Diagnostic Laboratory Sciences and Technology Research Center, Faculty of Paramedical Sciences, Shiraz University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Diagnostic Laboratory Sciences and Technology Research Center, Faculty of Paramedical Sciences, Shiraz University of Medical Sciences</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Gholamhossein</Name>
<MidName></MidName>
<Family>Tamadon</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Diagnostic Laboratory Sciences and Technology Research Center, Faculty of Paramedical Sciences, Shiraz University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Diagnostic Laboratory Sciences and Technology Research Center, Faculty of Paramedical Sciences, Shiraz University of Medical Sciences</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Sedigheh</Name>
<MidName></MidName>
<Family>Sharifzadeh</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Diagnostic Laboratory Sciences and Technology Research Center, Faculty of Paramedical Sciences, Shiraz University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Diagnostic Laboratory Sciences and Technology Research Center, Faculty of Paramedical Sciences, Shiraz University of Medical Sciences</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR>
    </AUTHORS>
    <KEYWORDS>
        <KEYWORD><KeyText>Acute promyelocytic leukemia</KeyText></KEYWORD><KEYWORD><KeyText>Flow cytometry</KeyText></KEYWORD><KEYWORD><KeyText>Fluorescent in situ hybridization</KeyText></KEYWORD><KEYWORD><KeyText>PML-RARalpha</KeyText></KEYWORD>
    </KEYWORDS>
    <PDFFileName>274.pdf</PDFFileName>
    <REFRENCES>
        <REFRENCE>
            <REF>Zhu J, Lallemand-Breitenbach V, de Th&#233; H. Pathways of retinoic acid- or arsenic trioxide-induced PML/RAR alpha catabolism, role of oncogene degradation in disease remission. Oncogene 2001;20(49):7257-7265.##Jurcic JG, Soignet SL, Maslak AP. Diagnosis and treatment of acute promyelocytic leukemia. Curr Oncol Rep 2007;9(5):337-344.##Di Noto R, Mirabelli P, Del Vecchio L. Flow cytometry analysis of acute promyelocytic leukemia: the power of &#39;surface hematology&#39;. Leukemia 2007;21(1):4-8.##Diverio D, Rossi V, Avvisati G, De Santis S, Pistilli A, Pane F, et al. Early detection of relapse by prospective reverse transcriptase-polymerase chain reaction analysis of the PML/RARalpha fusion gene in patients with acute promyelocytic leukemia enrolled in the GIMEMA-AIEOP multicenter &quot;AIDA&quot; trial. GIMEMA-AIEOP Multicenter &quot;AIDA&quot; Trial. Blood 1998;92(3):784-789.##Al-Mawali A, Gillis D, Lewis I. The role of multipara-meter flow cytometry for detection of minimal residual disease in acute myeloid leukemia. Am J Clin Pathol 2009;131(1):16-26.##Paietta E, Goloubeva O, Neuberg D, Bennett JM, Gallagher R, Racevskis J, et al. A surrogate marker profile for PML/RAR alpha expressing acute promyelocytic leukemia and the association of immunophenotypic markers with morphologic and molecular subtypes. Cytometry B Clin Cytom 2004;59(1):1-9.##Shen HQ, Tang YM, Song H, Shi SW, Yang SL, Xu WQ, et al. [Expressions of CD117 and CD11b in patients with APL at diagnosis and post-treatment]. Zhongguo Shi Yan Xue Ye Xue Za Zhi 2006;14(4):644-648. Chinese.##Wetzler M, McElwain BK, Stewart CC, Blumenson L, Mortazavi A, Ford LA, et al. HLA-DR antigen-negative acute myeloid leukemia. Leukemia 2003;17(4):707-715.##Foley R, Soamboonsrup P, Carter RF, Benger A, Meyer R, Walker I, et al. CD34-positive acute promyelocytic leukemia is associated with leukocytosis, microgranular/hypogranular morphology, expression of CD2 and bcr3 isoform. Am J Hematol 2001;67(1):34-41.##Romeo M, Chauffaille Mde L, Silva MR, Bahia DM, Kerbauy J. Comparison of cytogenetics with FISH in 40 myelodysplastic syndrome patients. Leuk Res 2002;26(11):993-996.##Fukutani H, Naoe T, Ohno R, Yoshida H, Kiyoi H, Miyawaki S, et al. Prognostic significance of the RT-PCR assay of PML-RARA transcripts in acute promyelocytic leukemia. The Leukemia Study Group of the Ministry of Health and Welfare (Kouseisho). Leukemia 1995;9(4):588-593.##Fenaux P, Chastang C, Chevret S, Sanz M, Dombret H, Archimbaud E, et al. A randomized comparison of all transretinoic acid (ATRA) followed by chemotherapy and ATRA plus chemotherapy and the role of maintenance therapy in newly diagnosed acute promyelocytic leukemia. The European APL Group. Blood 1999;94(4):1192-1200.##Burnett AK, Grimwade D, Solomon E, Wheatley K, Goldstone AH. Presenting white blood cell count and kinetics of molecular remission predict prognosis in acute promyelocytic leukemia treated with all-trans retinoic acid: result of the randomized MRC trial. Blood 1999;93(12):4131-4143.##Berger R, Bernheim A, Daniel MT, Valensi F, Flandrin G. Karyotype and cell phenotypes in primary acute leukemias. Blood Cells 1981;7(2):287-292.##Dong HY, Kung JX, Bhardwaj V, McGill J. Flow cytometry rapidly identifies all acute promyelocytic leukemias with high specificity independent of underlying cytogenetic abnormalities. Am J Clin Pathol 2011;135(1):76-84. ##Jurcic JG, Nimer SD, Scheinberg DA, DeBlasio T, Warrell RP Jr, Miller WH Jr. Prognostic significance of minimal residual disease detection and PML/RAR-alpha isoform type: long-term follow-up in acute promy-elocytic leukemia. Blood 2001;98(9):2651-2656.##Amidzadeh Z, Behbahani AB, Erfani N, Sharifzadeh S, Ranjbaran R, Moezi L, et al. Assessment of different permeabilization methods of minimizing damage to the adherent cells for detection of intracellular RNA by flow cytometry. Avicenna J Med Biotech 2014;6(1):38-46.##Ranjbaran R, Okhovat MA, Abbasi M, Moezzi L, Aboualizadeh F, Amidzadeh Z, et al. Detection of t(9;22) b2a2 fusion transcript by flow cytometry. Int J Lab Hematol 2016;38(4):403-411.##</REF>
        </REFRENCE>
    </REFRENCES>
</ARTICLE>

<ARTICLE>
    <TitleE>Can Aptameric Ligands Specific to Plasma Coagulation Factor VII Bind the Recombinant Form with High Affinity: Affinity Measurement by Fluorescence Method</TitleE>
    <TitleF></TitleF>
    <TitleLang_ID>2</TitleLang_ID>
    <ABSTRACTS>

        <ABSTRACT>
            <Language_ID>2</Language_ID>
            <CONTENT>&lt;p&gt;Background: Among diverse protein purification systems, affinity chromatography is the most attractive one in the purification process of coagulation factors. Coagulation factor VII is a plasma serine protease that has a significant role in natural human hemostasis and its recombinant form such as AryoSeven&lt;sup&gt;TM&lt;/sup&gt;, has been applied in clinical treatment of bleeding disorders. Immunoaffinity chromatography is the purification method of choice that is currently applied in the development of coagulation factor VIIa products. Aptamers as nucleic acid based affinity ligands are more promising than monoclonal antibodies. In addition, DNA aptamers are more acceptable than RNA ones in this regard.&lt;br /&gt;
Methods: In this study, two of the aptameric DNA oligonucleotides that showed acceptable affinities for purification of coagulation factor VIIa from plasma, were selected to evaluate their affinity against Aryoseven. A serial dilution of fluorescence labeled aptamers was incubated against the concentration of 1 &lt;em&gt;nM&lt;/em&gt; from Aryoseven. Then, a fluorescence index was calculated according to the fluorescence intensity data measured from test and control samples. The dissociation constant of aptamers was calculated using according to the fluorescence index Prism5 software.&lt;br /&gt;
Results: Results showed that the binding affinity of the 44 nucleotide aptamer was more than 81 nucleotide aptamer sequence. As a result, this aptamer could be optimized in order to develop aptamer based affinity chromatography process for this form of recombinant coagulation factor VIIa.&lt;br /&gt;
Discussion: Aptamers with shorter length of sequence could show higher affinity in target binding, as they could adapt more easily to suitable conformation according to target interaction. However, it should be considered that the selectivity of affinity ligands is also important for target purification and analytical applications.&lt;/p&gt;
</CONTENT>
        </ABSTRACT>
    </ABSTRACTS>
    <PAGES>
        <PAGE>
            <FPAGE>109</FPAGE>
            <TPAGE>112</TPAGE>
        </PAGE>
    </PAGES>
    <AUTHORS>
        <AUTHOR>
<Name>Maryam</Name>
<MidName></MidName>
<Family>Tabarzad</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Protein Technology Research Center, Shahid Beheshti University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Protein Technology Research Center, Shahid Beheshti University of Medical Sciences</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Marzieh</Name>
<MidName></MidName>
<Family>Jafari</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Department of Pharmacology and Toxicology, Faculty of Pharmacy, Ahvaz Jundishapur University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Department of Pharmacology and Toxicology, Faculty of Pharmacy, Ahvaz Jundishapur University of Medical Sciences</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR><AUTHOR>
<Name>Nastaran</Name>
<MidName></MidName>
<Family>Nafissi-varcheh</Family>
<NameE></NameE>
<MidNameE></MidNameE>
<FamilyE></FamilyE>
<Organizations>
<Organization>Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Shahid Beheshti University of Medical Sciences</Organization>
</Organizations>
<Universities>
<University>Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Shahid Beheshti University of Medical Sciences</University>
</Universities>
<Countries>
<Country>Iran</Country>
</Countries>
<EMAILS>
<Email></Email>
</EMAILS>
</AUTHOR>
    </AUTHORS>
    <KEYWORDS>
        <KEYWORD><KeyText>Affinity</KeyText></KEYWORD><KEYWORD><KeyText>Aptamer</KeyText></KEYWORD><KEYWORD><KeyText>Factor VIIa</KeyText></KEYWORD><KEYWORD><KeyText>Fluorescence</KeyText></KEYWORD>
    </KEYWORDS>
    <PDFFileName>275.pdf</PDFFileName>
    <REFRENCES>
        <REFRENCE>
            <REF>Wandtke T, Woźniak J, Kopiński P. Aptamers in diagnostics and treatment of viral infections. Viruses 2015;7(2):751-780.##Li F, Zhang H, Wang Z, Newbigging AM, Reid MS, Li XF, et al. Aptamers facilitating amplified detection of biomolecules. Anal Chem 2015;87(1):274-292.##Ku TH, Zhang T, Luo H, Yen TM, Chen PW, Han Y, et al. Nucleic acid aptamers: an emerging tool for biotechnology and biomedical sensing. Sensors (Basel) 2015;15(7):16281-16313.##Zhao Q, Wu M, Chris Le X, Li XF. Applications of aptamer affinity chromatography. Trends Analyt Chem 2012;41:46-57.##Jing M, Bowser MT. Methods for measuring aptamer-protein equilibria: a review. Anal Chim Acta 2011;686(1-2):9-18.##Wang G, Zhu Y, Chen L, Zhang X. Photoinduced electron transfer (PET) based label-free aptasensor for platelet-derived growth factor-BB and its logic gate application. Biosens Bioelectron 2015;63:552-557.##Deng Q, German I, Buchanan D, Kennedy RT. Retention and separation of adenosine and analogues by affinity chromatography with an aptamer stationary phase. Anal Chem 2001;73(22):5415-5421.##Lim HK, Kim IH, Nam HY, Shin S, Hah SS. Aptamer-based alternatives to the conventional immobilized metal affinity chromatography for purification of His-tagged proteins. Anal Lett 2013;46(3):407-415.##Brothier F, Pichon V. Miniaturized DNA aptamer-based monolithic sorbent for selective extraction of a target analyte coupled on-line to nanoLC. Anal Bioanal chem 2014;406(30):7875-7886.##Bock LC, Griffin LC, Latham JA, Vermaas EH, Toole JJ. Selection of single-stranded DNA molecules that bind and inhibit human thrombin. Nature 1992;355(6360):564-566.##Tiede A, Amano K, Ma A, Arkhammar P, El Fegoun SB, Rosholm A, et al. The use of recombinant activated factor VII in patients with acquired haemophilia. Blood Rev 2015;29 Suppl 1:S19-25.##Lin Y, Stanworth S, Birchall J, Doree C, Hyde C. Recombinant factor VIIa for the prevention and treatment of bleeding in patients without haemophilia. Cochrane Database Syst Rev 2011;(2):CD005011.##Neufeld EJ, N&#233;grier C, Arkhammar P, Benchikh el Fegoun S, Simonsen MD, Rosholm A, et al. Safety update on the use of recombinant activated factor VII in approved indications. Blood Rev 2015;29:S34-S41.##Rusconi CP, Yeh A, Lyerly HK, Lawson JH, Sullenger BA. Blocking the initiation of coagulation by RNA aptamers to factor VIIa. Thromb Haemost 2000;84(5):841-848.##Layzer JM, Sullenger BA. Simultaneous generation of aptamers to multiple gamma-carboxyglutamic acid proteins from a focused aptamer library using DeSELEX and convergent selection. Oligonucleotides 2007;17(1):1-11.##Perret G, Nogre M. Means for purifying a protein of blood plasma and methods for implementing same. U.S. Patent Application No. 13/201,690;2012.##Hage DS, Anguizola JA, Bi C, Li R, Matsuda R, Papastavros E, et al. Pharmaceutical and biomedical applications of affinity chromatography: recent trends and developments. J Pharm Biomed Anal 2012;69:93-105.##Romig TS, Bell C, Drolet DW. Aptamer affinity chromatography: combinatorial chemistry applied to protein purification. J Chromatogr B Biomed Sci Appl  1999;731(2):275-284.##Ramezani M, Danesh NM, Lavaee P, Abnous Kh, Taghdisi SM. A selective and sensitive fluorescent aptasensor for detection of kanamycin based on catalytic recycling activity of exonuclease III and gold nanoparticles. Sens Actuators B Chem. 2016;222:1-7.##Dassie JP, Liu XY, Thomas GS, Whitaker RM, Thiel KW, Stockdale KR, et al. Systemic administration of optimized aptamer-siRNA chimeras promotes regression of PSMA-expressing tumors. Nat Biotechnol 2009;27(9):839-849.##Stoltenburg R, Schubert T, Strehlitz B. In vitro selection and interaction studies of a DNA aptamer targeting protein A. PloS One 2015;10(7):e0134403.##Biesecker G, Dihel L, Enney K, Bendele R. Derivation of RNA aptamer inhibitors of human complement C5. Immunopharmacology 1999;42(1-3):219-230.##Kiani Z, Shafiei M, Ebrahimi A. Selection of DNA aptamers for digoxin and assaying of their binding profile and inhibitory effects. Res Pharm Sci 2012;7(5):S490.##</REF>
        </REFRENCE>
    </REFRENCES>
</ARTICLE>

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