ANTIBODY-BINDING PROFILE OF PURIFIED AND CELL-BOUND CD26 - DESIGNATION OF BT5/9 AND TA5.9 TO THE CD26 CLUSTER

被引:24
作者
DEMEESTER, I
SCHARPE, S
VANHAM, G
BOSMANS, E
HEYLIGEN, H
VANHOOF, G
CORTE, G
机构
[1] INST TROP MED PRINCE LEOPOLD,PATHOL & IMMUNOL LAB,B-2000 ANTWERP,BELGIUM
[2] DR WILLEMS INST,DIEPENBEEK,BELGIUM
[3] EUROGENET,TESSENDERLO,BELGIUM
[4] UNIV GENOA,IST TUMORI,I-16126 GENOA,ITALY
关键词
D O I
10.1016/S0171-2985(11)80494-8
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
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.
引用
收藏
页码:145 / 158
页数:14
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