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کاربرد نوع شرط:
- جایگاه : پژوهشی
- مجله: Iranian Journal of Immunology
- نوع مقاله: Journal Article
- کلمات کلیدی: Immunization,ELISA,Diphtheria-Tetanus-Pertussis Vaccine
- چکیده:
- چکیده انگلیسی: Background: Immunization against diphtheria, tetanus and pertussis has been applied in Iran since 1950. WHO suggests periodical evaluation of effectiveness of the triple diphtheria-tetanus-whole cell pertussis (DTwP) vaccine, worldwide.
Objectives: To determine the immunogenicity of locally manufactured DTwP vaccine administered to preschool children in a number of health centers of Tehran in 2006.
Methods: In this prospective study, 350 children aged 4-6 years were injected with DTwP vaccine manu-factured by Razi Institute of Iran. Blood samples were collected before and 2-4 weeks after the vaccination. The immunogenicity of the vaccine was assayed by measurement of specific antibodies using enzyme-linked immunosorbent assay (ELISA) technique.
Results: Of the 337 children who were vaccinated, 99.4% and 100% had protective anti-diphtheria and anti-tetanus antibody titers, respectively. The vaccine response and seroconversion for pertussis was achieved in 70.3% of the subjects. The geometric mean titers (GMT) of the antibodies produced against diphtheria, tetanus and pertussis by DTwP vaccine were 7.76, 9.37 IU/ml and 30.20 EU/ml after booster vaccine dose, respectively.
Conclusions: Comparison of the results obtained from this study with those of previous studies performed in other countries reveals that immunogenicity of diphtheria and tetanus components is similar to other vaccines, but the immunogenicity of pertussis vaccine was less efficient. The lower immunogenicity of DTwP against pertussis may be related to the bacterial strain used or the formulation protocol adopted for the vaccine preparation.- انتشار مقاله: 17-05-1395
- نویسندگان: Saeed Zarei,Mahmood Jeddi-Tehrani,Mohammad Mehdi Akhondi,Hojjat Zeraati,Tahere Kheirkhah,Morteza Ghazanfari,Fazel Shokri
- مشاهده
- جایگاه : پژوهشی
- مجله: Iranian Journal of Immunology
- نوع مقاله: Journal Article
- کلمات کلیدی: Flow cytometry,ALL,Immunophenotyping,Pro-B,Pre-B
- چکیده:
- چکیده انگلیسی: Background: Immunophenotypic characterization of the leukemic cells has been widely used as a tool for diagnosis, classification, stratification and prognosis of leukaemia.
Objective: To investigate the immunophenotypic subtype profiles of Iranian patients with acute lymphoblastic leukemia (ALL) and its association to disease outcome.
Methods: In this study, a total of 60 Iranian patients with ALL were immunophenotyped by flow cytometry using a panel of monoclonal antibodies specific for CD2, CD3, CD5, CD10, CD13, CD14, CD19, CD20, CD33, CD34, CD45, HLA-DR and TdT molecules.
Results: The samples were initially categorized into T-ALL (n=9), B-ALL (n=50) and mixed lineage (n=1) based on the expression patterns of CD3 and CD19 molecules. B-ALL patients could further be classified into four subtypes, including Pro-B (n=7, 11.7%), Pre-B I (n=28, 46.7%), Pre-B II (n=13, 21.7%) and immature/mature B cells (n=2, 3.3%) on the basis of expression of CD10, CD19, CD20, HLA-DR and TdT. Clinical manifestations and laboratory findings of the patients did not reveal association with immunophenotypic sub-types of ALL, with the exception of mediastinal mass and WBC count at the time of diag-nosis which were found to be significantly higher in patients with T-ALL compared with B-ALL (p=0.001 and 0.014), respectively.
Conclusion: Our results indicate that overall the immunophenotypic profile of Iranian ALL patients is similar to previous reports and it might be used for monitoring of minimal residual disease and prognosis.- انتشار مقاله: 17-05-1395
- نویسندگان: Hossein Asgarian Omran,Mahdi Shabani,Tahereh Shahrestani,Abdolfattah Sarafnejad,Jalal Khoshnoodi,Parvaneh Vossough,Mohammad Faranoush,Ramzan A. Sharifian,Mahmood Jeddi-Tehrani,Hodjatallah Rabbani,Fazel Shokri
- مشاهده
- جایگاه : پژوهشی
- مجله: Iranian Journal of Immunology
- نوع مقاله: Journal Article
- کلمات کلیدی: Pregnancy,Indoleamine 2,3-dioxygenase,Tolerance,Immunology
- چکیده:
- چکیده انگلیسی: Indoleamine 2,3-dioxygenase (IDO), an enzyme involved in the catabolism of tryptophan, is expressed by a variety of cells and tissues such as macrophages, dendritic cells, cells of the endocrine system and by the placenta. IFN- γ is the main inducer of this enzyme. IDO acts as an important defense mechanism of innate immunity against pathogens. It also has tumor suppressive activity and prolongs the survival of allograft. One of the interesting functions of IDO is prevention of the allogenic fetus rejection during pregnancy by inhibiting alloreactive T cells. It was shown that inhibition of IDO activity by IDO inhibitor, 1-methyl tryptophan, during mouse pregnancy causes fetal rejection. The main mechanism by which IDO protects fetus is through reducing the tryptophan level and suppressing the T cell activity in the feto-maternal interface. In this review the biological functions of IDO with emphasis on its role in allogeneic fetus protection have been discussed.
- انتشار مقاله: 15-05-1395
- نویسندگان: Amir Hassan Zarnani,Pouneh Dokouhaki,Mahmood Jeddi-Tehrani
- مشاهده
- جایگاه : پژوهشی
- مجله: Iranian Journal of Immunology
- نوع مقاله: Journal Article
- کلمات کلیدی: Pregnancy,Indoleamine 2,3-dioxygenase,Tolerance,Immunology
- چکیده:
- چکیده انگلیسی: Indoleamine 2,3-dioxygenase (IDO), an enzyme involved in the catabolism of tryptophan, is expressed by a variety of cells and tissues such as macrophages, dendritic cells, cells of the endocrine system and by the placenta. IFN- γ is the main inducer of this enzyme. IDO acts as an important defense mechanism of innate immunity against pathogens. It also has tumor suppressive activity and prolongs the survival of allograft. One of the interesting functions of IDO is prevention of the allogenic fetus rejection during pregnancy by inhibiting alloreactive T cells. It was shown that inhibition of IDO activity by IDO inhibitor, 1-methyl tryptophan, during mouse pregnancy causes fetal rejection. The main mechanism by which IDO protects fetus is through reducing the tryptophan level and suppressing the T cell activity in the feto-maternal interface. In this review the biological functions of IDO with emphasis on its role in allogeneic fetus protection have been discussed.
- انتشار مقاله: 15-05-1395
- نویسندگان: Amir Hassan Zarnani,Pouneh Dokouhaki,Mahmood Jeddi-Tehrani
- مشاهده
- جایگاه : پژوهشی
- مجله: Iranian Journal of Immunology
- نوع مقاله: Journal Article
- کلمات کلیدی: Pregnancy,Indoleamine 2,3-dioxygenase,Tolerance,Immunology
- چکیده:
- چکیده انگلیسی: Indoleamine 2,3-dioxygenase (IDO), an enzyme involved in the catabolism of tryptophan, is expressed by a variety of cells and tissues such as macrophages, dendritic cells, cells of the endocrine system and by the placenta. IFN- γ is the main inducer of this enzyme. IDO acts as an important defense mechanism of innate immunity against pathogens. It also has tumor suppressive activity and prolongs the survival of allograft. One of the interesting functions of IDO is prevention of the allogenic fetus rejection during pregnancy by inhibiting alloreactive T cells. It was shown that inhibition of IDO activity by IDO inhibitor, 1-methyl tryptophan, during mouse pregnancy causes fetal rejection. The main mechanism by which IDO protects fetus is through reducing the tryptophan level and suppressing the T cell activity in the feto-maternal interface. In this review the biological functions of IDO with emphasis on its role in allogeneic fetus protection have been discussed.
- انتشار مقاله: 15-05-1395
- نویسندگان: Amir Hassan Zarnani,Pouneh Dokouhaki,Mahmood Jeddi-Tehrani
- مشاهده
- جایگاه : پژوهشی
- مجله: Iranian Journal of Basic Medical Sciences
- نوع مقاله: Journal Article
- کلمات کلیدی: Antibody,western blot,β-actin Immunocytochemistry,Immunohistochemistry Peptide
- چکیده:
- چکیده انگلیسی: Objective(s):Antibodies against actin, as one of the most widely studied structural and multifunctional housekeeping proteins in eukaryotic cells, are used as internal loading controls in western blot analyses. The aim of this study was to produce polyclonal antibody against a synthetic peptide derived from N-terminal region of β-actin protein to be used as a protein loading control in western blot and other assay systems.
Materials and Methods: A synthetic peptide derived from β-actin protein was designed and conjugated to Keyhole limpet hemocyanin (KLH (and used to immunize a white New Zealand rabbit. The antibody was purified from serum by affinity chromatography column. The purity of the antibody was determined by SDS-PAGE and its ability to recognize the immunizing peptide was measured by ELISA. The reactivity of the antibody with β-actin protein in a panel of different cell lysates was then evaluated by western blot. In addition, the reactivity of the antibody with the corresponding protein was also evaluated by Immunocytochemistry and Immunohistochemistry in different samples.
Results: The antibody could recognize the immunizing peptide in ELISA. It could also recognize β-actin protein in western blot as well as in immunocytochemistry and immunohistochemistry.
Conclusion: Our data suggest that this antibody may be used as an internal control in western blot analyses as well as in other immunological applications such as ELISA,immunocytochemistry and immunohistochemistry.- انتشار مقاله: 03-04-1393
- نویسندگان: Nazila Amini,Mohadeseh Naghi Vishteh,Omid Zarei,Reza Hadavi,Negah Ahmadvand,Hodjattallah Rabbani,Mahmood Jeddi-Tehrani
- مشاهده
- جایگاه : پژوهشی
- مجله: Iranian Journal of Biotechnology
- نوع مقاله: Journal Article
- کلمات کلیدی: Purification,Protein expression,Polyclonal antibody,FCRL,His-tag
- چکیده:
- چکیده انگلیسی: Background: The Fc receptor like (FCRL) molecules belong to the immunoglobulin (Ig) superfamily with potentially immunoregulatory function. Among the FCRL family FCRL2 and 4 are predominantly expressed on memory B cells and FCRL1 is a pan- B cell marker. To date, no ligand has been identifid for the human FCRL1, 2 and 4 molecules. Objectives: Cloning, expression, purifiation and structural analysis of the extracellular domain of human FCRL1, 2 and 4 proteins. Materials and Methods: In this study, the extracellular part of human FCRL1, 2 and 4 were subcloned into prokaryotic expression vectors pET-28b (+) and transformed into BL21-DE3 E.coli strain. Protein expression was optimized by fie adjustments such as induction time, incubation temperature and expression hosts. Recombinant FCRL proteins were purifid by metal affity chromatography using Ni-NTA resin. Purifid FCRL proteins were further characterized by SDS-PAGE and immunoblotting using His-tag and FCRL specifi polyclonal antibodies. Results: Our results demonstrated that FCRL1, 2 and 4 were successfully expressed in pET-28b (+) vector. Optimization of the expression procedure showed that IPTG induction at OD600 = 0.9 and overnight incubation at 37˚C resulted in the highest expression levels of FCRL proteins ranging from approximately 15% (FCRL1) to 25% (FCRL2 and 4) of the total bacterial lysate proteins. Conclusions: These purifid recombinant proteins are potentially a valuable tool for investigating the immunoregulatory function of FCRL molecules and the production of specifi mAbs for immunotherapeutic interventions.
- انتشار مقاله: 04-10-1391
- نویسندگان: Mahdi Shabani,Azam Hemmati,Mahdi Zandemami,Jalal Khoshnoodi,Mahmood Jeddi-Tehrani,Hodjatallah Rabbani,Zahra Amirghofran,Fazel Shokri
- مشاهده
- جایگاه : پژوهشی
- مجله: Asian Pacific Journal of Cancer Prevention
- نوع مقاله: Journal Article
- کلمات کلیدی: Breast cancer,Fusion protein,HER3,Polyclonal antibody
- چکیده:
- چکیده انگلیسی: Objective: Human epidermal growth factor receptor 3 (HER3) is a unique member of the tyrosine kinase receptors with an inactive kinase domain and is the preferable dimerization partner for HER2 which lead to potent tumorigenic signaling. Methods: In this study, the expression plasmids coding for the human HER3 subdomains were transfected into CHO-K1 cells. Produced proteins were characterized by ELISA and SDS-PAGE. Rabbits were immunized and produced polyclonal antibodies (pAbs) that were characterized by ELISA, Immunoblotting and flowcytometry and their inhibitory effects were assessed by XTT on BT-474 and JIMT-1 breast cancer cell lines. Result: The recombinant subdomains were highly immunogenic in rabbits. The pAbs reacted with the recombinant subdomains as well as commercial HER3 and the native receptor on tumor cell membranes and could significantly inhibit growth of Trastuzumab sensitive (BT-474) and resistant (JIMT-1) breast cancer cell lines in vitro. Conclusion: It seems that HER3 extra cellular domains (ECD) induce a strong anti-tumor antibody response and may prove to be potentially useful for immunotherapeutic applications.
- انتشار مقاله: 21-05-1398
- نویسندگان: Samaneh Mansouri-Fard,Mojgan Ghaedi,Mohammad-Reza Shokri,Tannaz Bahadori,Jalal Khoshnoodi,Forough Golsaz-Shirazi,Mahmood Jeddi-Tehrani,Mohammad Mehdi Amiri,Fazel Shokri
- مشاهده