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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
1997-1-23
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pubmed:abstractText |
CD26 and ecto-adenosine deaminase (ADA) are found associated on the plasma membrane of T lymphocytes and each possess distinct catalytic activities. CD26 has a proteolytic activity identical to dipeptidylpeptidase IV (DPPIV; E.C. 3.4.14.5), and ecto-ADA (E.C. 3.5.4.4) degrades extracellular adenosine. The cell surface expression of CD26 and ecto-adenosine deaminase (ecto-ADA) is regulated on stimulated T lymphocytes, and ADA binding to CD26 produces a synergistic costimulatory response with T cell receptor activation. This study addresses the potential regulation by allosteric interactions of the catalytic activities of CD26 associated with ecto-ADA, which could define the mechanism of the synergism observed in T cell signaling. Cell lines genetically deficient in ADA, ligands for ADA such as adenosine, and a specific inhibitor of ADA, deoxycoformycin, were used to define the effect of ADA activity on CD26 DPPIV activity and affinity for dipeptide substrate. Conversely, a recombinant Chinese hamster ovary cell line expressing human CD26 with or without a mutation in the DPPIV catalytic domain, and the boronic acid inhibitor Val-boroPro, were used to determine the effect of DPPIV activity on ecto-ADA activity and association with CD26. These studies found no significant allosteric interaction between the catalytic activities of CD26 and ecto-ADA when associated. Therefore, signaling events in T cells involving costimulation with CD26 and ecto-ADA and the synergism observed upon ADA binding to CD26 occur independently of the catalytic activities of these cell surface molecules.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Deaminase,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Deaminase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Boronic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Dipeptidyl Peptidase 4,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Pentostatin
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-2952
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
52
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1757-65
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:8986139-Adenosine Deaminase,
pubmed-meshheading:8986139-Adenosine Deaminase Inhibitors,
pubmed-meshheading:8986139-Allosteric Regulation,
pubmed-meshheading:8986139-Animals,
pubmed-meshheading:8986139-Boronic Acids,
pubmed-meshheading:8986139-CHO Cells,
pubmed-meshheading:8986139-Cell Line,
pubmed-meshheading:8986139-Cricetinae,
pubmed-meshheading:8986139-Dipeptidyl Peptidase 4,
pubmed-meshheading:8986139-Enzyme Inhibitors,
pubmed-meshheading:8986139-Humans,
pubmed-meshheading:8986139-Lymphocytes,
pubmed-meshheading:8986139-Pentostatin
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pubmed:year |
1996
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pubmed:articleTitle |
Effect of deoxycoformycin and Val-boroPro on the associated catalytic activities of lymphocyte CD26 and ecto-adenosine deaminase.
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pubmed:affiliation |
Department of Immunological Diseases, Inflammatory Diseases, and Pharmaceutics, Boehringer Ingelheim Pharmaceuticals, Inc. Ridgefield, CT 06877, USA.
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pubmed:publicationType |
Journal Article
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