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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
27
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pubmed:dateCreated |
2000-8-16
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pubmed:abstractText |
CD38 is a bifunctional ectoenzyme predominantly expressed on hematopoietic cells where its expression correlates with differentiation and proliferation. The two enzyme activities displayed by CD38 are an ADP-ribosyl cyclase and a cyclic adenosine diphosphate ribose (cADPR) hydrolase that catalyzes the synthesis and hydrolysis of cADPR. T lymphocytes can be induced to express CD38 when activated with antibodies against specific antigen receptors. If the activated T cells are then exposed with NAD, cell death by apoptosis occurs. During the exposure of activated T cells to NAD, the CD38 is modified by ecto-mono-ADP-ribosyltransferases (ecto-mono-ADPRTs) specific for cysteine and arginine residues. Arginine-ADP-ribosylation results in inactivation of both cyclase and hydrolase activities of CD38, whereas cysteine-ADP-ribosylation results only in the inhibition of the hydrolase activity. The arginine-ADP-ribosylation causes a decrease in intracellular cADPR and a subsequent decrease in Ca(2+) influx, resulting in apoptosis of the activated T cells. Our results suggest that the interaction of two classes of ecto-ADP-ribose transfer enzymes plays an important role in immune regulation by the selective induction of apoptosis in activated T cells and that cADPR mediated signaling is essential for the survival of activated T cells.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ADP-ribosyl Cyclase,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate Ribose,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD38,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation,
http://linkedlifedata.com/resource/pubmed/chemical/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/CD38 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Cd38 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic ADP-Ribose,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/NAD,
http://linkedlifedata.com/resource/pubmed/chemical/NAD Nucleosidase,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol...,
http://linkedlifedata.com/resource/pubmed/chemical/Poly(ADP-ribose) Polymerases,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
275
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
20799-805
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:10777496-ADP-ribosyl Cyclase,
pubmed-meshheading:10777496-Adenosine Diphosphate Ribose,
pubmed-meshheading:10777496-Animals,
pubmed-meshheading:10777496-Antigens, CD,
pubmed-meshheading:10777496-Antigens, CD38,
pubmed-meshheading:10777496-Antigens, Differentiation,
pubmed-meshheading:10777496-Apoptosis,
pubmed-meshheading:10777496-Arginine,
pubmed-meshheading:10777496-Calcium,
pubmed-meshheading:10777496-Cell Line,
pubmed-meshheading:10777496-Cyclic ADP-Ribose,
pubmed-meshheading:10777496-Cysteine,
pubmed-meshheading:10777496-Flow Cytometry,
pubmed-meshheading:10777496-Humans,
pubmed-meshheading:10777496-Lymphocyte Activation,
pubmed-meshheading:10777496-Membrane Glycoproteins,
pubmed-meshheading:10777496-Mice,
pubmed-meshheading:10777496-Mice, Inbred BALB C,
pubmed-meshheading:10777496-NAD,
pubmed-meshheading:10777496-NAD+ Nucleosidase,
pubmed-meshheading:10777496-Phosphatidylinositol Diacylglycerol-Lyase,
pubmed-meshheading:10777496-Poly(ADP-ribose) Polymerases,
pubmed-meshheading:10777496-Signal Transduction,
pubmed-meshheading:10777496-T-Lymphocytes,
pubmed-meshheading:10777496-Transfection,
pubmed-meshheading:10777496-Type C Phospholipases
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pubmed:year |
2000
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pubmed:articleTitle |
Interaction of two classes of ADP-ribose transfer reactions in immune signaling.
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pubmed:affiliation |
Department of Biochemistry and Department of Internal Medicine, Institute for Medical Sciences, Chonbuk National University Medical School, Chonju, Chonbuk 561-182, Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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