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23409220
Editorial
In this first editorial for the “first issue” of Avicenna Journal of Medical Biotechnology (AJMB), I thought I should provide our dear readers a little background as well as the reasons used in making decision to publish an English journal in the field of Medical Biotechnology in Iran.
Although the field of Medical Biotechnology is still at its infancy in many ways, it has travelled a long journey since its inception in early 1980s, a period parallel to the emergence of DNA recombinant technology and genetic engineering. At that time, the impact of genetic engineering in medicine was predicted to be great and this proved to be correct since the science of Medical Biotechnology expanded later on to include a variety of fields such as molecular medicine, cellular and molecular therapies, applied immunology, nanomedicine, genomics and proteomics, bioinformatics, tissue engineering, biosensors and pharmaceuticals. As a consequence of the great impacts that Medical Biotechnology has had in commercial, legal, ethical and social areas, AJMB is intending to provide a venue for articles discussing these issues in specific areas pertaining to the application of technologies in medicine in general.
Since the establishment of biotechnology research centers in Iran, including National Center for Biotechnology and Genetic Engineering more than 15 years ago as well as Avicenna Research Institute, several English language journals have been published in the field of Biotechnology in Iran. AJMB is another English journal in this field but what makes it distinguishable from other journals is its scope of coverage and the comprehensiveness of the fields in medical biotechnology.
Regarding the journal’s name, after many hours of deliberations, the scientific staff at Avicenna Research Institute voted for the selection of the name “Avicenna” because of three reasons: 1. Avicenna simply best represents the Iranian-Islamic scientific culture and medicine in history 2. Avicenna is a name that is well recognized and respected in science and medicine throughout the world. 3. Avicenna is a name that has been chosen for a research institute that is focused on the application of biotechnologies in the areas of reproductive biology and cancer. Therefore, it is most appropriate to have Avicenna as the name for a Journal that publishes articles in Medical Biotechnology.
As we all know, Avicenna is a Latinized name of Ibn-e-Sina and his contributions to almost all fields of medical sciences and philosophy in the world is well known. Recently, Avicenna’s contributions to science and medicine have been recognized by major international organizations. For example, the United Nations Educational, Scientific and Cultural Organization (UNESCO) has established a virtual campus dedicated to open distance learning in eleven Mediterranean countries under the name of The Avicenna Virtual Campus Project. Also another project with the name of Avicenna Directories of Educational Institutions for the Health Professionals has been initiated under the auspices of the World Health Organization (WHO).
I hope the name of “Avicenna” at both Avicenna Research Institute and Avicenna Journal of Medical Biotechnology provides the inspiration for conducting good science and become a place where high quality articles are published. I look forward to receiving your articles in the future and hope the readers of AJMB make this journal, the journal of their choice to publish the results of their research work in the field of Medical Biotechnology.
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https://www.ajmb.org/En/Article.aspx?id=156
https://www.ajmb.org/PDF/En/FullText/156.pdf
AliM. ArdekaniReproductive Biotechnology Research Center, Avicenna Research Institute, ACECR, Tehran, Iran2
en
23407771
The Place of Avicenna in the History of Medicine
Avicenna, a Muslim scientist of the tenth and eleventh centuries has an important place in the history of medicine in Iran and the world. Furthermore, the modern medicine is laid upon the infrastructure of his medicine. In this article, the position of Avicenna in the medical history and the scientific influence of his medical works in particular Al-Canon in the development of medical literature and medical educational programs have been studied in a historical approach. In reviewing the position of Avicenna in the history of medicine in the Islamic world and the Europe, it was concluded that during 11th to 17th centuries, the scientific and educational activities of medicine in the world were moving on the pivot of Avicenna medicine or was under its intensive influence.
Avicenna, Avicenna Medicine, Islamic Medicine, Medical History, Medical Literature, Traditional Medicine
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https://www.ajmb.org/En/Article.aspx?id=1
https://www.ajmb.org/PDF/En/FullText/1.pdf
JamalMoosaviDepartment of History and Civilization of Islamic Nations, University of Tehran , Tehran, Iran1
en
23407612
Nutrigenomics and Cancer
Cancer incidence is projected to increase in the future and an effectual preventive strategy is required to face this challenge. Alteration of dietary habits is potentially an effective approach for reducing cancer risk. Assessment of biological effects of a specific food or bioactive component that is linked to cancer and prediction of individual susceptibility as a function of nutrient-nutrient interactions and genetics is an essential element to evaluate the beneficiaries of dietary interventions. In general, the use of biomarkers to evaluate individuals susceptibilities to cancer must be easily accessible and reliable. However, the response of individuals to bioactive food components depends not only on the effective concentration of the bioactive food components, but also on the target tissues. This fact makes the response of individuals to food components vary from one individual to another. Nutrigenomics focuses on the understanding of interactions between genes and diet in an individual and how the response to bioactive food components is influenced by an individual’s genes. Nutrients have shown to affect gene expression and to induce changes in DNA and protein molecules. Nutrigenomic approaches provide an opportunity to study how gene expression is regulated by nutrients and how nutrition affects gene variations and epigenetic events. Finding the components involved in interactions between genes and diet in an individual can potentially help identify target molecules important in preventing and/or reducing the symptoms of cancer.
Bioactive food components, Biomarker, Cancer prevention, Nutrigenetics, Nutrigenomics
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https://www.ajmb.org/En/Article.aspx?id=2
https://www.ajmb.org/PDF/En/FullText/2.pdf
AliM. ArdekaniReproductive Biotechnology Research Center, Avicenna Research Institute, ACECR , Tehran, Iran2
SepidehJabbariReproductive Biotechnology Research Center, Avicenna Research Institute, ACECR , Tehran, Iran3
en
23407435
Generation and Characterization of Mouse Hybridomas Secreting Monoclonal Antibodies Specific for Human IgG3
Mammalians express several subclasses of the IgG molecule. In human being there are four homologous IgG subclasses, each of which is structurally unique and has different functions. Quantification of IgG subclasses is fundamental to clinical assessment and diagnosis of many diseases as such assessments depends on the availability of subclassspecific antibodies (Abs), particularly monoclonal antibodies (MAbs). In the present study, we produced and characterized two murine MAbs specific for human IgG3 molecule. These MAbs were obtained by the fusion of myeloma cells with splenocytes from Balb/c mice immunized with heavy chain of a human IgG3 myeloma protein. Fused cells were selected in hypoxanthine, aminopterine and thymidine (HAT) medium and cloned by limiting dilution assay. Ab-secreting cells were screened by enzyme-linked immunosorbent assay (ELISA) and the specificity of secreted MAbs was further analyzed, using a panel of purified myeloma proteins by ELISA and immunoblotting. Two stable hybridomas designated 1F18G7 and 1F18A11 were obtained secreting MAbs specific for Fc fragment of human IgG3. None of these MAbs showed cross-reactivity with other immunoglobulin isotypes derived from human and nine other animals, except 1F18A11 which displayed a weak cross-reactivity with only dog serum. Immunoblotting results indicate that these MAbs react with linear epitope(s) located in the heavy chain of human IgG3 molecules. The affinity constant of 1F18G7 and 1F18A11 MAbs was found to be 0.81×109 Mol –1 and 0.71×109 Mol –1, respectively, as measured by ELISA. These two MAbs with relatively high affinity can be useful tools for quantification of IgG3 subclass levels in human serum.
Heavy chain, Human IgG3, Immunoglobulin, Isotype, Light chain, Monoclonal antibody
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https://www.ajmb.org/En/Article.aspx?id=3
https://www.ajmb.org/PDF/En/FullText/3.pdf
FatemehHajighasemiDepartment of Immunology, School of Medicine, Shahed University , Tehran, Iran4
FazelShokriMonoclonal Antibody Research Center, Avecinna Research Center ACECR , Tehran, Iran5
en
23407330
Conjugation of Monoclonal Antibodies to Super Paramagnetic Iron Oxide Nanoparticles for Detection of her2/neu Antigen on Breast Cancer Cell Lines
Conjugation of monoclonal antibodies to super paramagnetic nanoparticles is an effective method for cancer diagnosis and treatment. In this study the humanized anti her2/neu monoclonal antibody- Herceptin- was conjugated to super paramagnetic iron oxide (SPIO) nanoparticles using EDC method. The concentration of the conjugated antibodies was measured by Bradford assay. The antibody-nanoparticle conjugates were incubated with SKBR-3 and T47D human breast carcinoma cell lines and the presence of the conjugates on cell surface was confirmed by Prussian blue iron staining method. Conjugation of Herceptin to SPIO resulted in a precipitate-free conjugate containing 20µg antibody/mg SPIO. Prussian blue iron-staining of cells showed successful binding of the conjugates to the cell surfaces. Conjugation of monoclonal antibodies to SPIO may be a useful method for detection of tumor cells, especially by MRI techniques.
Breast cancer, Conjugation, Herceptin, Nanomagnetic particles
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https://www.ajmb.org/En/Article.aspx?id=4
https://www.ajmb.org/PDF/En/FullText/4.pdf
FereshtehShamsipourMonoclonal Antibody Research Center, Avicenna Research Institute, ACECR , Tehran, Iran6
Amir-HassanZarnaniDepartment of Immunology, Reproductive Biotechnology Research Center, Avicenna Research Institute, ACECR , Tehran, Iran7
RoyaGhodsMonoclonal Antibody Research Center, Avicenna Research Institute, ACECR , Tehran, Iran8
MahmoodChamankhahNanobiotechnology Research Center, Avicenna Research Institute, ACECR , Tehran, Iran9
FloraForouzeshNanobiotechnology Research Center, Avicenna Research Institute, ACECR , Tehran, Iran10
SedighehVafaeiMonoclonal Antibody Research Center, Avicenna Research Institute, ACECR , Tehran, Iran11
Ali AhmadBayatMonoclonal Antibody Research Center, Avicenna Research Institute, ACECR , Tehran, Iran12
Mohammad MehdiAkhondiDepartment of Immunology, Reproductive Biotechnology Research Center, Avicenna Research Institute, ACECR , Tehran, Iran13
Mohammad AliOghabianResearch Centre for Science and Technology in Medicine, Tehran University of Medical Sciences , Tehran, Iran14
MahmoodJeddi-TehraniMonoclonal Antibody Research Center, Avicenna Research Institute, ACECR , Tehran, Iran15
en
23407141
Producing a Mammalian GFP Expression Vector Containing Neomycin Resistance Gene
The green fluorescent protein (GFP) was originally isolated from the Jellyfish Aequorea Victoria that fluoresces green when exposed to blue light. GFP protein is composed of 238 amino acids with the molecular mass of 26.9 kD. The GFP gene is frequently used in cellular and molecular biology as a reporter gene. To date, many bacterial, yeast , fungal, plants, fly and mammalian cells, including human, have been created which express GFP. Martin Chalfie, Osamu Shimomura, and Roger Tsien were awarded the 2008 noble prize in chemistry for their discovery and development of GFP. In many studies on mammalian cells, GFP gene is introduced into cells using vector-based systems or a recombinant virus to track the location of a target protein or to study the expression level of the gene of interest, but in these studies there is no selection marker to normalize transfection. According to the importance of neomycin gene as a selection marker in mammalian cells, we aimed to produce a GFP expression vector that contains neomycin gene. GFP gene was separated from pEGFP-N1 vector and was inserted in the back-bone of pCDNA3.1/His/LacZ vector that contained the neomycin gene. The resulted vector contained GFP beside neomycin gene.
Expression, Green Flourescent Protein, Neomycin, Resistance gene, Vector
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https://www.ajmb.org/En/Article.aspx?id=5
https://www.ajmb.org/PDF/En/FullText/5.pdf
ManizhehIzadiDepartment of Medical Genetics, Faculty of Medicine, Tehran University of Medical Science , Tehran, Iran16
MaryamAbiriDepartment of Medical Genetics, Faculty of Medicine, Tehran University of Medical Science , Tehran, Iran17
MohammadKeramatipourDepartment of Medical Genetics, Faculty of Medicine, Tehran University of Medical Science , Tehran, Iran18
en
23407719
Construction of a High Efficiency PCR Products Cloning T Vector Using pGEM-5zf (+)
A highly efficient cloning vector was constructed for cloning PCR products by inserting an 80 bp DNA fragment into pGEM-5zf (+) vector. The Xcm I digestion of this vector gave rise to a 3’ overhanging deoxythymidine offering the possibility of cloning PCR products with 3' adenosine overhang created by Taq DNA polymerase. Furthermore, two EcoR I sites were added to the construct for identification of recombinant plasmids using a single restriction enzyme. Taken together, the more efficient cloning performance and the lower cost of this vector as compared to the commercial T vector, suggests that it may be one of the best T vectors for cloning of PCR products.
Cloning, PCR products, pGEM-5zf(+), T vector
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https://www.ajmb.org/En/Article.aspx?id=6
https://www.ajmb.org/PDF/En/FullText/6.pdf
YaofengZhaoDivision of Clinical Immunology, Department of Laboratory Medicine, Karolinska University Hospital Huddinge, SE-141 86 , Stockholm, Sweden19
ZhancaiLiuDepartment of Physics, Chemistry and Biology, Jiaozuo Teachers College, Jiaozuo, 454001 , Henan, P. R. China20
ShuyangYuDivision of Clinical Immunology, Department of Laboratory Medicine, Karolinska University Hospital Huddinge, SE-141 86 , Stockholm, Sweden21
SichengWenDivision of Clinical Immunology, Department of Laboratory Medicine, Karolinska University Hospital Huddinge, SE-141 86 , Stockholm, Sweden22
LennartHammarstromDivision of Clinical Immunology, Department of Laboratory Medicine, Karolinska University Hospital Huddinge, SE-141 86 , Stockholm, Sweden23
HodjattallahRabbaniDepartment of Antigen and Antibody Engineering, Monoclonal Antibody Research Center, Avicenna Research Institute, ACECR , Tehran, Iran24
en
23407674
Assessment of Thyroglobulin Expression in Reproductive Organs at Different Stages of Mouse Estrous Cycle
Prevalence of abortion is higher in women with autoimmune thyroid disease. In the majority of cases, however, no abnormality of thyroid function is detected despite the high levels of antithyroid antibodies. The direct influence of such harmful autoantibodies in female reproductive organs may serve a role in pregnancy loss. In this study, expression of thyroglobulin in the reproductive tissues of cycling mice has been evaluated. Stages of estrous cycle were determined by cellular morphology and ratio of epithelial cells to leukocytes in vaginal smear of Balb/C mice. At each phase, the mice were sacrificed and their uterus, ovary and fallopian tubes were removed. Expression of thyroglobulin-specific transcript in endometrium was investigated by two sets of primers using reverse transcriptase-polymerase chain reaction (RT-PCR). In addition, expression of thyroglobulin in reproductive tissues was assessed by immunohistochemistry and dot blot analysis. The results showed that thyroglobulin mRNA is not expressed in endometrial tissue of Balb/C mice at any stage of estrous cycle. Immunohistochemical analysis also confirmed that thyroglobulin or its cross reactive-antigens are not expressed at the protein level in the female reproductive organs. The results showed that thyroglobulin was not expressed in the reproductive organs of female mice. It is plausible that antithyroglobulin antibodies could interact with newly-generated antigens during placentation and pregnancy.
Antithyroglobulin antibody, Endometrium, Estrous cycle, Placentation, Recurrent abortion, Uterus
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https://www.ajmb.org/En/Article.aspx?id=7
https://www.ajmb.org/PDF/En/FullText/7.pdf
AliMoravvejDepartment of Immunology, Faculty of Medicine, Iran University of Medical Sciences , Tehran, Iran25
MahmoodJeddi-TehraniMonoclonal Antibody Research Center, Avicenna Research Institute, ACECR , Tehran, Iran15
Ali RezaSalek MoghaddamDepartment of Immunology, Faculty of Medicine, Iran University of Medical Sciences , Tehran, Iran26
PounehDokouhakiReproductive Biotechnology Research Center, Avicenna Research Institute, ACECR , Tehran, Iran27
MahdiShekarabiDepartment of Immunology, Faculty of Medicine, Iran University of Medical Sciences , Tehran, Iran28
RoyaGhodsMonoclonal Antibody Research Center, Avicenna Research Institute, ACECR , Tehran, Iran8
MahdiShahbaziDepartment of Immunology, Faculty of Medicine, Iran University of Medical Sciences , Tehran, Iran30
JamilehGhasemiReproductive Biotechnology Research Center, Avicenna Research Institute, ACECR , Tehran, Iran31
ParivashDaneshDepartment of Immunology, Faculty of Medicine, Iran University of Medical Sciences , Tehran, Iran32
Ahmad RezaMahmoudiDepartment of Immunology, Faculty of Medicine, Iran University of Medical Sciences , Tehran, Iran33
Amir-HassanZarnaniImmunology Research Center, Faculty of Medicine, Iran University of Medical Sciences , Tehran, Iran7
en
23407807
Production and Purification of Streptokinase by Protected Affinity Chromatography
Streptokinase is an extracellular protein, extracted from certain strains of beta hemolytic streptococcus. It is a non-protease plasminogen activator that activates plasminogen to plasmin, the enzyme that degrades fibrin cloth through its specific lysine binding site; it is used therefore as a drug in thrombolytic therapy. The rate of bacterial growth and streptokinase production was studied in condition of excess glucose addition to culture media and its pH maintenance. The streptokinase product of the bacterial culture was preliminary extracted by salt precipitation and then purified by affinity chromatography on plasminogen substituted sepharose-4B in a condition that the plasminogen active site was protected from streptokinase-induced activation. The purity of streptokinase was confirmed by SDS-PAGE and its biological activity determined in a specific streptokinase assay. The results showed that in the fed –batch culture, the rate of streptokinase production increased over two times as compared with the batch culture while at the same time, shortening the streptokinase purification to a single step increased the yield over 95 % at the chromatography stage.
Affinity chromatography, Culture, Plasminogen, Purification, Streptokinase
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https://www.ajmb.org/En/Article.aspx?id=8
https://www.ajmb.org/PDF/En/FullText/8.pdf
MohammadBabashamsiDepartment of Medical Diagnostics and Biological Products, Monoclonal Antibody Research Center, Avicenna Research Institute, ACECR , Tehran, Iran34
Mohammad HosseinRazavianIslamic Azad University,Qom branch , Qom, Iran35
Mohammad RezaNejadmoghaddamDepartment of Recombinant Technology, Nanobiotechnology Research Center, Avicenna Research Institute, ACECR , Tehran, Iran36