| pubmed-article:1716881 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1716881 | lifeskim:mentions | umls-concept:C0005821 | lld:lifeskim |
| pubmed-article:1716881 | lifeskim:mentions | umls-concept:C0031621 | lld:lifeskim |
| pubmed-article:1716881 | lifeskim:mentions | umls-concept:C0033634 | lld:lifeskim |
| pubmed-article:1716881 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
| pubmed-article:1716881 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:1716881 | pubmed:dateCreated | 1991-10-21 | lld:pubmed |
| pubmed-article:1716881 | pubmed:abstractText | We have shown that platelets stimulated with thrombin or guanosine 5'-[gamma-thio]triphosphate (GTP[S]), both of which activate phospholipase C and protein kinase C (PKC), show enhancement of 3-phosphorylated phosphoinositide accumulation (3-PPI). We now report the following. (1) Inhibition of thrombin- or GTP[S]-stimulated PKC by pseudo-substrate peptide (RFARK) added to permeabilized platelets markedly inhibits 3-PPI, whereas the serine/threonine phosphatase inhibitor, okadaic acid, promotes 3-PPI. PKC activity, insufficient in itself for fully activating 3-PPI, appears crucial to receptor and post-receptor stimulation of 3-PPI, even when tyrosine phosphorylation is unimpaired. (2) Alteration of Gi by ADP-ribosylation only slightly affects the stimulation of 3-PPI by thrombin, and activation of the G-protein Gi by adrenaline has no effect on 3-PPI. (3) Inhibition of PKC blocks activated secretion of platelet-derived growth factor (PDGF). However, PDGF cannot promote platelet 3-PPI, and thus cannot account for the inhibitory effects of RFARK on 3-PPI. | lld:pubmed |
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| pubmed-article:1716881 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1716881 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1716881 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1716881 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1716881 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:1716881 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:1716881 | pubmed:author | pubmed-author:ZhangJJ | lld:pubmed |
| pubmed-article:1716881 | pubmed:author | pubmed-author:RittenhouseS... | lld:pubmed |
| pubmed-article:1716881 | pubmed:author | pubmed-author:KingW GWG | lld:pubmed |
| pubmed-article:1716881 | pubmed:author | pubmed-author:SoriskyAA | lld:pubmed |
| pubmed-article:1716881 | pubmed:author | pubmed-author:KuceraG LGL | lld:pubmed |
| pubmed-article:1716881 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1716881 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:1716881 | pubmed:volume | 278 ( Pt 2) | lld:pubmed |
| pubmed-article:1716881 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1716881 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1716881 | pubmed:pagination | 475-80 | lld:pubmed |
| pubmed-article:1716881 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:1716881 | pubmed:meshHeading | pubmed-meshheading:1716881-... | lld:pubmed |
| pubmed-article:1716881 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1716881 | pubmed:articleTitle | Protein kinase C regulates the stimulated accumulation of 3-phosphorylated phosphoinositides in platelets. | lld:pubmed |
| pubmed-article:1716881 | pubmed:affiliation | Department of Biochemistry, University of Vermont College of Medicine, Burlington 05405. | lld:pubmed |
| pubmed-article:1716881 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1716881 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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