Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-6-16
pubmed:abstractText
Bradykinin (BK) B2 receptor signaling involves activation of phospholipase C (PLC). PLC activation by other receptors consists of either allosteric activation of PLC beta isoforms by G-proteins or tyrosine phosphorylation of PLC gamma isoforms. Because the B2 receptor is a G-protein-coupled receptor, it has been assumed that the receptor signals through PLC beta. In the present study, however, we have found that BK stimulation of IP3 production and the Ca2+ signal in endothelial cells is dependent on tyrosine phosphorylation. Furthermore, stimulation of B2 receptors in these cells is accompanied by a transient tyrosine phosphorylation of PLC gamma 1. Phosphorylation is correlated with increased IP3 production and association of PLC gamma 1 with the C-terminal intracellular domain of the B2 receptor. The B2 receptor can thus physically associate with intracellular proteins other than G-proteins. Activation of PLC gamma isoforms, rather than PLC beta isoforms, may, therefore, be primarily responsible for BK-stimulated IP3 generation in endothelial cells.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/4-amino-5-(4-methylphenyl)-7-(tert-b..., http://linkedlifedata.com/resource/pubmed/chemical/Bradykinin, http://linkedlifedata.com/resource/pubmed/chemical/Inositol 1,4,5-Trisphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes, http://linkedlifedata.com/resource/pubmed/chemical/Phospholipase C gamma, http://linkedlifedata.com/resource/pubmed/chemical/Pyrazoles, http://linkedlifedata.com/resource/pubmed/chemical/Pyrimidines, http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Angiotensin, Type 1, http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Angiotensin, Type 2, http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Bradykinin B2, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Angiotensin, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Bradykinin, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases, http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine, http://linkedlifedata.com/resource/pubmed/chemical/src-Family Kinases
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
246
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
70-5
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:9600070-Animals, pubmed-meshheading:9600070-Bradykinin, pubmed-meshheading:9600070-Cattle, pubmed-meshheading:9600070-Cells, Cultured, pubmed-meshheading:9600070-Endothelium, Vascular, pubmed-meshheading:9600070-Enzyme Activation, pubmed-meshheading:9600070-Inositol 1,4,5-Trisphosphate, pubmed-meshheading:9600070-Isoenzymes, pubmed-meshheading:9600070-Phospholipase C gamma, pubmed-meshheading:9600070-Phosphorylation, pubmed-meshheading:9600070-Pyrazoles, pubmed-meshheading:9600070-Pyrimidines, pubmed-meshheading:9600070-Receptor, Angiotensin, Type 1, pubmed-meshheading:9600070-Receptor, Angiotensin, Type 2, pubmed-meshheading:9600070-Receptor, Bradykinin B2, pubmed-meshheading:9600070-Receptors, Angiotensin, pubmed-meshheading:9600070-Receptors, Bradykinin, pubmed-meshheading:9600070-Recombinant Fusion Proteins, pubmed-meshheading:9600070-Signal Transduction, pubmed-meshheading:9600070-Type C Phospholipases, pubmed-meshheading:9600070-Tyrosine, pubmed-meshheading:9600070-src-Family Kinases
pubmed:year
1998
pubmed:articleTitle
Bradykinin stimulates the tyrosine phosphorylation and bradykinin B2 receptor association of phospholipase C gamma 1 in vascular endothelial cells.
pubmed:affiliation
Department of Pediatrics, Medical College of Georgia, Augusta 30912, USA. rvenema@mail.mcg.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't