pubmed-article:9600070 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9600070 | lifeskim:mentions | umls-concept:C1257792 | lld:lifeskim |
pubmed-article:9600070 | lifeskim:mentions | umls-concept:C0914912 | lld:lifeskim |
pubmed-article:9600070 | lifeskim:mentions | umls-concept:C0006100 | lld:lifeskim |
pubmed-article:9600070 | lifeskim:mentions | umls-concept:C1519726 | lld:lifeskim |
pubmed-article:9600070 | lifeskim:mentions | umls-concept:C0753837 | lld:lifeskim |
pubmed-article:9600070 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
pubmed-article:9600070 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:9600070 | pubmed:dateCreated | 1998-6-16 | lld:pubmed |
pubmed-article:9600070 | 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. | lld:pubmed |
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pubmed-article:9600070 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:9600070 | pubmed:language | eng | lld:pubmed |
pubmed-article:9600070 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9600070 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9600070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:9600070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9600070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9600070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9600070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9600070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9600070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:9600070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9600070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9600070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9600070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9600070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9600070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9600070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9600070 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9600070 | pubmed:month | May | lld:pubmed |
pubmed-article:9600070 | pubmed:issn | 0006-291X | lld:pubmed |
pubmed-article:9600070 | pubmed:author | pubmed-author:EatonD CDC | lld:pubmed |
pubmed-article:9600070 | pubmed:author | pubmed-author:SunJJ | lld:pubmed |
pubmed-article:9600070 | pubmed:author | pubmed-author:VenemaV JVJ | lld:pubmed |
pubmed-article:9600070 | pubmed:author | pubmed-author:JuHH | lld:pubmed |
pubmed-article:9600070 | pubmed:author | pubmed-author:VenemaR CRC | lld:pubmed |
pubmed-article:9600070 | pubmed:author | pubmed-author:MarreroM BMB | lld:pubmed |
pubmed-article:9600070 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9600070 | pubmed:day | 8 | lld:pubmed |
pubmed-article:9600070 | pubmed:volume | 246 | lld:pubmed |
pubmed-article:9600070 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9600070 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9600070 | pubmed:pagination | 70-5 | lld:pubmed |
pubmed-article:9600070 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:9600070 | pubmed:year | 1998 | lld:pubmed |
pubmed-article:9600070 | pubmed:articleTitle | Bradykinin stimulates the tyrosine phosphorylation and bradykinin B2 receptor association of phospholipase C gamma 1 in vascular endothelial cells. | lld:pubmed |
pubmed-article:9600070 | pubmed:affiliation | Department of Pediatrics, Medical College of Georgia, Augusta 30912, USA. rvenema@mail.mcg.edu | lld:pubmed |
pubmed-article:9600070 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9600070 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:9600070 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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