DC Field | Value | Language |
---|---|---|
dc.contributor.author | An, NH | ko |
dc.contributor.author | Han, MK | ko |
dc.contributor.author | Um, C | ko |
dc.contributor.author | Park, BH | ko |
dc.contributor.author | Park, BJ | ko |
dc.contributor.author | Kim, HK | ko |
dc.contributor.author | Kim, UH | ko |
dc.date.accessioned | 2024-03-22T03:02:30Z | - |
dc.date.available | 2024-03-22T03:02:30Z | - |
dc.date.created | 2024-03-21 | - |
dc.date.created | 2024-03-21 | - |
dc.date.issued | 2001-04 | - |
dc.identifier.citation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.282, no.3, pp.781 - 786 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | http://hdl.handle.net/10203/318683 | - |
dc.description.abstract | Cyclic ADP-ribose (cADPR), a product of CD38, has a second messenger role for in intracellular Ca2+ mobilization from microsomes of pancreatic islets as well as from a variety of other cells. ADP-ribosylation of CD38 by ecto-mono ADP-ribosyltransferase in activated T cells results in apoptosis as well as inactivation of its activities. We, therefore, examined the effect of ADP-ribosylation of CD38 in mouse pancreatic islet cells. NAD-dependent inactivation and ADP-ribosylation of CD38, intracellular concentrations of cADPR and Ca2+ and insulin secretion were measured following incubation of mouse pancreatic islet cells with NAD, ADP-ribosylation of CD38 inactivated its ecto-enzyme activities, and abolished glucose-induced increase of cADPR production, intracellular concentration of Ca2+, and insulin secretion. Taken together, ecto-cyclase activity of CD38 to produce intracellular cADPR seems to be indispensable for insulin secretion. (C) 2001 Academic Press. | - |
dc.language | English | - |
dc.publisher | ACADEMIC PRESS INC | - |
dc.title | Significance of ecto-cyclase activity of CD38 in insulin secretion of mouse pancreatic islet cells | - |
dc.type | Article | - |
dc.identifier.wosid | 000168092000021 | - |
dc.identifier.scopusid | 2-s2.0-0034816206 | - |
dc.type.rims | ART | - |
dc.citation.volume | 282 | - |
dc.citation.issue | 3 | - |
dc.citation.beginningpage | 781 | - |
dc.citation.endingpage | 786 | - |
dc.citation.publicationname | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.identifier.doi | 10.1006/bbrc.2001.4654 | - |
dc.contributor.localauthor | Park, BH | - |
dc.contributor.nonIdAuthor | An, NH | - |
dc.contributor.nonIdAuthor | Han, MK | - |
dc.contributor.nonIdAuthor | Um, C | - |
dc.contributor.nonIdAuthor | Park, BJ | - |
dc.contributor.nonIdAuthor | Kim, HK | - |
dc.contributor.nonIdAuthor | Kim, UH | - |
dc.description.isOpenAccess | N | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose | - |
dc.subject.keywordAuthor | hydrolase) | - |
dc.subject.keywordAuthor | cyclic ADP-ribose | - |
dc.subject.keywordAuthor | ADP-ribosylation | - |
dc.subject.keywordAuthor | insulin secretion | - |
dc.subject.keywordAuthor | Ca2+ | - |
dc.subject.keywordAuthor | pancreatic islet cells | - |
dc.subject.keywordPlus | CYCLIC ADP-RIBOSE | - |
dc.subject.keywordPlus | BETA-CELLS | - |
dc.subject.keywordPlus | GLYCOHYDROLASE | - |
dc.subject.keywordPlus | SURFACE | - |
dc.subject.keywordPlus | RIBOSYLTRANSFERASE | - |
dc.subject.keywordPlus | DIFFERENTIATION | - |
dc.subject.keywordPlus | ERYTHROCYTES | - |
dc.subject.keywordPlus | HYDROLASE | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | CA2+ | - |
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