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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1995-3-13
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pubmed:abstractText |
The transmembrane glycoprotein CD38 is a bifunctional enzyme that catalyzes at its ectocellular domain both the synthesis and the hydrolysis of cyclic ADP-ribose (cADPR). The complete reaction, converting NAD+ to nicotinamide and ADP-ribose, reproduces an NAD+glycohydrolase (NADase) reaction. CD38 purified from human erythrocyte membranes has been recently shown to undergo stable oligomerization induced by either NAD+ or beta-mercaptoethanol. We demonstrate that oligomerization is also triggered by reduced glutathione (GSH) and that the GSH-induced self-aggregation of purified CD38 is accompanied by extensive and comparable decrease of its ADP-ribosyl cyclase and NADase activities. GSH-induced oligomerization of CD38 and strong enzyme inactivation take place also in situ on erythrocyte membranes.
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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/CD38 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mercaptoethanol,
http://linkedlifedata.com/resource/pubmed/chemical/N-Glycosyl Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/NAD
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
359
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
35-40
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7851527-ADP-ribosyl Cyclase,
pubmed-meshheading:7851527-Adenosine Diphosphate Ribose,
pubmed-meshheading:7851527-Antigens, CD,
pubmed-meshheading:7851527-Antigens, CD38,
pubmed-meshheading:7851527-Antigens, Differentiation,
pubmed-meshheading:7851527-Erythrocyte Membrane,
pubmed-meshheading:7851527-Glutathione,
pubmed-meshheading:7851527-Humans,
pubmed-meshheading:7851527-Macromolecular Substances,
pubmed-meshheading:7851527-Membrane Glycoproteins,
pubmed-meshheading:7851527-Mercaptoethanol,
pubmed-meshheading:7851527-N-Glycosyl Hydrolases,
pubmed-meshheading:7851527-NAD
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pubmed:year |
1995
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pubmed:articleTitle |
Self-aggregation of purified and membrane-bound erythrocyte CD38 induces extensive decrease of its ADP-ribosyl cyclase activity.
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pubmed:affiliation |
Institute of Biochemistry, University of Genoa, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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