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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1998-12-21
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pubmed:abstractText |
Cyclic ADP-ribose (cADPR) is a natural metabolite of beta-NAD+ with a potent Ca2+-mobilizing activity in different cell types, including T-lymphocytes. We investigated (i) whether stimulation of T-lymphocytes with different agonists affects the intracellular concentration of cADPR, and (ii) whether the lymphocyte antigen CD38, through its ectocellular ADP-ribosyl cyclase and cADPR-hydrolase enzymatic activities, can account for the regulation of the intracellular levels of cADPR and the Ca2+-mobilizing effects of this nucleotide in Jurkat and HPB.ALL T-lymphocytes. The anti-CD3 antibody OKT3, the sphingolipid sphingosine and lysophosphatidic acid induced an increase in intracellular cADPR with concomitant increases in the intracellular Ca2+ concentration ([Ca2+]i). In contrast, activation of an ectocellular ADP-ribosyl cyclase by preincubation of cells with beta-NAD+ led to a dose-dependent increase in cADPR, but no changes in [Ca2+]i were observed. However, extensive washing of the cells following preincubation with NAD+ demonstrated that the increases in cADPR were not intracellular but due to cell surface-associated nucleotide. Accordingly, measurements of ADP-ribosyl cyclase activity in intact T-cells showed ectocellular synthesis of cADPR, but no evidence was obtained for a shift of this activity into the cells which could account for intracellular accumulation of cADPR. Taken together, the results indicate no direct involvement of the ADP-ribosyl cyclase activity of CD38 on the regulation of the cADPR-mediated intracellular Ca2+-signalling in T-lymphocytes.
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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/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/Cyclic ADP-Ribose,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/NAD Nucleosidase,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
439
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
291-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9845340-ADP-ribosyl Cyclase,
pubmed-meshheading:9845340-Adenosine Diphosphate Ribose,
pubmed-meshheading:9845340-Antigens, CD,
pubmed-meshheading:9845340-Antigens, CD38,
pubmed-meshheading:9845340-Antigens, Differentiation,
pubmed-meshheading:9845340-Biological Transport,
pubmed-meshheading:9845340-Blotting, Western,
pubmed-meshheading:9845340-Calcium Signaling,
pubmed-meshheading:9845340-Catalysis,
pubmed-meshheading:9845340-Cyclic ADP-Ribose,
pubmed-meshheading:9845340-Flow Cytometry,
pubmed-meshheading:9845340-Humans,
pubmed-meshheading:9845340-Jurkat Cells,
pubmed-meshheading:9845340-Membrane Glycoproteins,
pubmed-meshheading:9845340-NAD+ Nucleosidase,
pubmed-meshheading:9845340-Receptors, Antigen, T-Cell,
pubmed-meshheading:9845340-T-Lymphocytes
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pubmed:year |
1998
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pubmed:articleTitle |
Ectocellular CD38-catalyzed synthesis and intracellular Ca2+-signalling activity of cyclic ADP-ribose in T-lymphocytes are not functionally related.
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pubmed:affiliation |
University of Hamburg, Institute of Physiological Chemistry, Department of Enzyme Chemistry, Germany. dasilva@uke.uni-hamburg.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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