Purified and cell-bound CD26: enzymatic inhibition, antibody binding profile, and expression on T cells in relation to other surface markers

Verh K Acad Geneeskd Belg. 1994;56(6):537-59.

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). We investigated some molecular and inhibition characteristics as well as the monoclonal antibody (mAb)-binding profile of this molecule purified from human lymphocytes. Among the antibodies we explored, two, anti-BT5/9 and anti-TA5.9, exhibited a high affinity for both purified and cell-bound CD26 Ag. Their significance in the study of immunologic memory and lymphocyte activation is discussed in relation to other markers of lymphocyte activation. Among 4 types of inhibitors studied, Pro-boroPro proved to be the most promising substance for further research on the physiological role of dipeptidyl peptidase IV (CD26).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies, Monoclonal / immunology
  • Binding Sites, Antibody
  • Boron Compounds / pharmacology
  • Dipeptidyl Peptidase 4 / immunology*
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / antagonists & inhibitors*
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / isolation & purification
  • Enzymes, Immobilized
  • Glycosylation
  • Humans
  • Isoelectric Focusing
  • Leukocytes, Mononuclear / immunology
  • Lymphocyte Activation
  • Pyrrolidines / pharmacology
  • T-Lymphocytes / enzymology*
  • T-Lymphocytes / immunology*

Substances

  • Antibodies, Monoclonal
  • Boron Compounds
  • Enzymes, Immobilized
  • Pyrrolidines
  • 1-(2-pyrrolidinylcarbonyl)-2-pyrrolidinylboronic acid
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
  • Dipeptidyl Peptidase 4