Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1996-7-15
pubmed:abstractText
Cyclic 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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/ADP-ribosyl Cyclase, http://linkedlifedata.com/resource/pubmed/chemical/ADP-ribosyl cyclase 2, 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/Antigens, Surface, http://linkedlifedata.com/resource/pubmed/chemical/CD38 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Cd38 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/GPI-Linked Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Glycosylphosphatidylinositols, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/N-Glycosyl Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
219
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
941-6
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:8645283-ADP-ribosyl Cyclase, pubmed-meshheading:8645283-Animals, pubmed-meshheading:8645283-Antigens, CD, pubmed-meshheading:8645283-Antigens, CD38, pubmed-meshheading:8645283-Antigens, Differentiation, pubmed-meshheading:8645283-Antigens, Surface, pubmed-meshheading:8645283-Aplysia, pubmed-meshheading:8645283-Flow Cytometry, pubmed-meshheading:8645283-GPI-Linked Proteins, pubmed-meshheading:8645283-Gene Expression, pubmed-meshheading:8645283-Glycosylphosphatidylinositols, pubmed-meshheading:8645283-Humans, pubmed-meshheading:8645283-Immunohistochemistry, pubmed-meshheading:8645283-Islets of Langerhans, pubmed-meshheading:8645283-Membrane Glycoproteins, pubmed-meshheading:8645283-Mice, pubmed-meshheading:8645283-Mice, Inbred BALB C, pubmed-meshheading:8645283-N-Glycosyl Hydrolases, pubmed-meshheading:8645283-Point Mutation, pubmed-meshheading:8645283-Polymerase Chain Reaction, pubmed-meshheading:8645283-RNA, Messenger, pubmed-meshheading:8645283-Recombinant Proteins, pubmed-meshheading:8645283-Sequence Homology, Amino Acid, pubmed-meshheading:8645283-Transfection
pubmed:year
1996
pubmed:articleTitle
Pancreatic islet cells express BST-1, a CD38-like surface molecule having ADP-ribosyl cyclase activity.
pubmed:affiliation
First Department of Medicine, Osaka University School of Medicine, Japan.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't