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

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Cellular Peptidases in Immune Functions and Diseases

Part of the book series: Advances in Experimental Medicine and Biology ((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.

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© 1997 Springer Science+Business Media New York

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Hegen, M., Kameoka, J., Dong, RP., Morimoto, C., Schlossman, S.F. (1997). Structure of CD26 (Dipeptidyl Peptidase IV) and Function in Human T Cell Activation. In: Ansorge, S., Langner, J. (eds) Cellular Peptidases in Immune Functions and Diseases. Advances in Experimental Medicine and Biology, vol 421. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9613-1_15

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  • DOI: https://doi.org/10.1007/978-1-4757-9613-1_15

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4757-9615-5

  • Online ISBN: 978-1-4757-9613-1

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