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Direct Association of Adenosine Deaminase with a T Cell Activation Antigen, CD26

Junichi Kameoka, Toshiaki Tanaka, Yoshihisa Nojima, Stuart F. Schlossman and Chikao Morimoto
Science
New Series, Vol. 261, No. 5120 (Jul. 23, 1993), pp. 466-469
Stable URL: http://www.jstor.org/stable/2881934
Page Count: 4
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Direct Association of Adenosine Deaminase with a T Cell Activation Antigen, CD26
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Abstract

CD26, the T cell activation molecule dipeptidyl peptidase IV (DPPIV), associates with a 43-kilodalton protein. Amino acid sequence analysis and immunoprecipitation studies demonstrated that this 43-kilodalton protein was adenosine deaminase (ADA). ADA was coexpressed with CD26 on the Jurkat T cell lines, and an in vitro binding assay showed that the binding was through the extracellular domain of CD26. ADA deficiency causes severe combined immunodeficiency disease (SCID) in humans. Thus, ADA and CD26 (DPPIV) interact on the T cell surface, and this interaction may provide a clue to the pathophysiology of SCID caused by ADA deficiency.

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