Structure of CD26 (Dipeptidyl Peptidase IV) and Function in Human T Cell Activation

  • Martin Hegen
  • Junichi Kameoka
  • Rui-Ping Dong
  • Chikao Morimoto
  • Stuart F. Schlossman
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 421)

Abstract

1996 was the 10th anniversary of the establishment of the cluster of differentiation antigen, CD26 by the Second Workshop and Conference on Human Leukocyte Differentiation Antigens1. First described as a T cell activation antigen, CD26 was found to he strongly expressed on subsets of both activated CD4 and CD8 T cells2. Subsequent work showed the expression of CD26 on activated Nk cells, B cells and B cell lines and demonstrated CD26 expression on a variety of different cell types, most abundantly on epithelia of the intestine, prostate and the proximal tubuli of the kidneys3,4,5. Furthermore, it was demonstrated that CD26 possesses enzymatic activity, dipeptidyl peptidase IV (DPP IV; EC 3.4.14.5), in its extracellular domain4 and is identical to the previously described adenosine deaminase (ADA, EC 3.5.4.4) binding protein6,7. Recent studies indicate that CD26 plays a seminal role in T cell costimulation and may be involved in severe combined immunodeficiency and HIV infection 8,9.

Keywords

Tyrosine Phosphorylation Adenosine Deaminase Dipeptidyl Peptidase Severe Combine Immunodeficiency Disease Induce Tyrosine Phosphorylation 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1997

Authors and Affiliations

  • Martin Hegen
    • 1
  • Junichi Kameoka
    • 1
  • Rui-Ping Dong
    • 1
  • Chikao Morimoto
    • 1
  • Stuart F. Schlossman
    • 1
  1. 1.Division of Tumor Immunology Dana-Farber Cancer Institute and Department of MedicineHarvard Medical SchoolBostonUSA

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