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Antibody binding profile of purified and cell-bound CD26. Designation of BT5/9 and TA5.9 to the CD26 cluster.
- Source :
-
Immunobiology [Immunobiology] 1993 Jun; Vol. 188 (1-2), pp. 145-58. - Publication Year :
- 1993
-
Abstract
- The CD26 activation antigen (Ag) which is expressed on a subpopulation of human T cells has been characterized as dipeptidyl peptidase IV (DPP IV, EC 3.4.14.5). In this paper, we describe the antibody binding profile of CD26/DPP IV, purified from human peripheral blood lymphocytes. The purified molecule binds to the anti-Ta1, anti-1F7 and anti-134-2C2 monoclonal antibodies (mAb), reported to react with cell-bound CD26 Ag. Among unclustered mAb recognizing T cell antigens, two, anti-BT5/9 and anti-TA5.9 were found to react with purified and cell-bound CD26 Ag. The classification of the BT5/9 Ag, the functional properties of the BT5/9+ T cell subset, as well as the in vivo effect of anti-BT5/9 mAb administration, are re-interpreted in the light of its specificity. Applying the anti-TA5.9 mAb in three color FACS analyses, we demonstrated that CD26+bright cells co-express CD45RO but not HLA-DR and CD38.
- Subjects :
- Antibodies, Monoclonal immunology
Antigen-Antibody Reactions
Antigens, CD immunology
Antigens, CD isolation & purification
Antigens, Differentiation, T-Lymphocyte immunology
Antigens, Differentiation, T-Lymphocyte isolation & purification
Binding Sites, Antibody
Chromatography, Affinity
Dipeptidyl Peptidase 4
Dipeptidyl-Peptidases and Tripeptidyl-Peptidases immunology
Dipeptidyl-Peptidases and Tripeptidyl-Peptidases isolation & purification
Humans
Antibodies, Monoclonal metabolism
Antigens, CD metabolism
Antigens, Differentiation, T-Lymphocyte metabolism
Dipeptidyl-Peptidases and Tripeptidyl-Peptidases metabolism
T-Lymphocytes enzymology
T-Lymphocytes immunology
Subjects
Details
- Language :
- English
- ISSN :
- 0171-2985
- Volume :
- 188
- Issue :
- 1-2
- Database :
- MEDLINE
- Journal :
- Immunobiology
- Publication Type :
- Academic Journal
- Accession number :
- 8104877
- Full Text :
- https://doi.org/10.1016/S0171-2985(11)80494-8