| pubmed-article:8288587 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8288587 | lifeskim:mentions | umls-concept:C1706586 | lld:lifeskim |
| pubmed-article:8288587 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:8288587 | lifeskim:mentions | umls-concept:C2323499 | lld:lifeskim |
| pubmed-article:8288587 | lifeskim:mentions | umls-concept:C0033640 | lld:lifeskim |
| pubmed-article:8288587 | lifeskim:mentions | umls-concept:C0036720 | lld:lifeskim |
| pubmed-article:8288587 | lifeskim:mentions | umls-concept:C0812215 | lld:lifeskim |
| pubmed-article:8288587 | lifeskim:mentions | umls-concept:C2746015 | lld:lifeskim |
| pubmed-article:8288587 | lifeskim:mentions | umls-concept:C1515877 | lld:lifeskim |
| pubmed-article:8288587 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:8288587 | lifeskim:mentions | umls-concept:C0591833 | lld:lifeskim |
| pubmed-article:8288587 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:8288587 | pubmed:dateCreated | 1994-2-22 | lld:pubmed |
| pubmed-article:8288587 | pubmed:abstractText | We have previously found that Raf-1, which is activated by hematopoietic growth factors in association with phosphorylation, is required for hematopoietic cell proliferation. Recently, 12-O-tetradecanoylphorbol 13-acetate has been found to mediate Raf-1 phosphorylation, suggesting that protein kinase C (PKC) may be involved in the Raf-1 activation mechanism(s). Since PKC can be activated by hematopoietic growth factors, it was investigated as a potential "Raf-1 kinase-kinase." Results demonstrate that bryostatin 1, a pharmacologic activator of PKC, induces activation of Raf-1 in FDC-P1 cells. PKC inhibitors H7 and staurosporine block both bryostatin 1- and interleukin-3-mediated Raf-1 phosphorylation and FDC-P1 cell proliferation. Additionally, an antisense c-raf oligodeoxyribonucleotide specifically inhibits bryostatin 1-mediated proliferation, indicating a necessary role for Raf-1 in PKC signaling. Purified PKC can phosphorylate Raf-1 serine residues to high stoichiometry in vitro. Comparative phosphopeptide maps localize two PKC phosphorylation sites to Raf-1 phosphopeptides isolated from hematopoietic growth factor- or bryostatin 1-stimulated cells. The sites of PKC-mediated Raf-1 phosphorylation are deduced to be Ser497 and Ser619. Furthermore, PKC-mediated serine phosphorylation is sufficient to activate the enzymatic function of Raf-1 in vitro. These findings demonstrate that activated PKC can promote hematopoietic cell growth by regulating the enzymatic activity of Raf-1 through direct serine phosphorylation. | lld:pubmed |
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| pubmed-article:8288587 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8288587 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8288587 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8288587 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:8288587 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8288587 | pubmed:author | pubmed-author:CarrollM PMP | lld:pubmed |
| pubmed-article:8288587 | pubmed:author | pubmed-author:MauW WWW | lld:pubmed |
| pubmed-article:8288587 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8288587 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:8288587 | pubmed:volume | 269 | lld:pubmed |
| pubmed-article:8288587 | pubmed:geneSymbol | c-raf-1 | lld:pubmed |
| pubmed-article:8288587 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8288587 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8288587 | pubmed:pagination | 1249-56 | lld:pubmed |
| pubmed-article:8288587 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:8288587 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8288587 | pubmed:articleTitle | Protein kinase C-mediated serine phosphorylation directly activates Raf-1 in murine hematopoietic cells. | lld:pubmed |
| pubmed-article:8288587 | pubmed:affiliation | Johns Hopkins Oncology Center, Baltimore, Maryland 21287. | lld:pubmed |
| pubmed-article:8288587 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8288587 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:8288587 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8288587 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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