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pubmed-article:8645283pubmed:abstractTextCyclic ADP-ribose (cADPR), a well-known stimulator of ca(2+) release from the intracellular Ca(2+) pool, has recently emerged as a potential regulator of insulin secretion in pancreatic beta cells. As recently described, BST-1 is a glycosyl-phosphatidylinositol (GPI)-anchored surface molecule that exhibits homology with CD38 and Aplysia ADP-ribosyl cyclase. Like CD38, BST-1 has both ADP-ribosyl cyclase and cADPR hydrolase activities. As a step toward elucidating the physiological role of cADPR in insulin secretion we examined whether BST-1 is expressed in pancreatic islet cells. Sensitive reverse transcription-polymerase chain reaction detected almost as abundant expression of BST-1 mRNA in pancreatic islets as CD38 mRNA. Immunohistochemical analyses utilizing mirror image sections revealed that BST-1 protein is expressed in a majority of the cells in pancreatic islets and that at least beta cells and, to an even greater extent, alpha cells express BST-1. These observations suggest the involvement of multiple enzymes in the regulation of cADPR concentrations in pancreatic islet cells.lld:pubmed
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pubmed-article:8645283pubmed:articleTitlePancreatic islet cells express BST-1, a CD38-like surface molecule having ADP-ribosyl cyclase activity.lld:pubmed
pubmed-article:8645283pubmed:affiliationFirst Department of Medicine, Osaka University School of Medicine, Japan.lld:pubmed
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pubmed-article:8645283pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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