Biochemical characterization of CD26 (dipeptidyl peptidase IV): Functional comparison of distinct epitopes recognized by various anti-CD26 monoclonal antibodies

التفاصيل البيبلوغرافية
العنوان: Biochemical characterization of CD26 (dipeptidyl peptidase IV): Functional comparison of distinct epitopes recognized by various anti-CD26 monoclonal antibodies
المؤلفون: Chikao Morimoto, Toshiaki Tanaka, Nam H. Dang, Stuart F. Schlossman, Catherine M. Prado, Y Torimoto
المصدر: Molecular Immunology. 29:183-192
بيانات النشر: Elsevier BV, 1992.
سنة النشر: 1992
مصطلحات موضوعية: Antigens, Differentiation, T-Lymphocyte, medicine.drug_class, Dipeptidyl Peptidase 4, T-Lymphocytes, CD3, T cell, Immunology, Cross Reactions, Lymphocyte Activation, Monoclonal antibody, Peptide Mapping, Epitope, Dipeptidyl peptidase, Epitopes, Antigen, medicine, Humans, Dipeptidyl-Peptidases and Tripeptidyl-Peptidases, Molecular Biology, biology, Antibodies, Monoclonal, Precipitin, Precipitin Tests, Molecular biology, medicine.anatomical_structure, Biochemistry, Leukocytes, Mononuclear, biology.protein, Antibody
الوصف: In this paper, we performed further biochemical characterization of the CD26 antigen, as defined by the mAbs in anti-1F7 and anti-Ta1, in order to clarify the observed functional differences among these mAbs. For this purpose, we developed a mAb, anti-5F8, which recognizes yet another epitope on the CD26 antigen different from that recognized by anti-1F7 and anti-Ta1 and compared their respective effect on T cell activation as well as the structures recognized by these mAbs. Functionally, anti-5F8 did not exhibit a comitogenic effect on T cell activation via the CD3 and CD2 pathways. Peptide mapping studies suggested that the 110 kDa molecules precipitated by these mAbs are identical. We showed that the 110 kDa CD26 structure on human T cells is composed of a family of heterogeneous molecules, as determined by isoelectric focusing studies. In addition, we demonstrated that the CD26 antigen has a DPPIV enzyme activity and this enzyme activity is found only on the principal basic structure of CD26 but not on the additional acidic structures. Biochemical studies also revealed that these mAbs recognized distinct epitopes on the CD26 antigen. Pulse-chase studies showed the the 1F7 epitope was found on both the immature (100 kDa) and mature (110 kDa) forms of the CD26 antigen. On the other hand, the Ta1 and 5F8 epitopes were expressed mainly on the mature form of the CD26 antigen. Moreover, anti-IF7 consistently precipitated an additional 43 kDa molecule in association with the principal 110 kDa molecule. Taken together, these data suggested that the additional 43 kDa structure or the distinct epitope recognized by anti-IF7 may play a role in human T cell activation via the CD3 and CD2 pathways.
تدمد: 0161-5890
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be50df6f7e9714de6d2b10f9d44e9dbb
https://doi.org/10.1016/0161-5890(92)90099-j
حقوق: CLOSED
رقم الأكسشن: edsair.doi.dedup.....be50df6f7e9714de6d2b10f9d44e9dbb
قاعدة البيانات: OpenAIRE