| pubmed-article:2026625 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2026625 | lifeskim:mentions | umls-concept:C0027950 | lld:lifeskim |
| pubmed-article:2026625 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:2026625 | lifeskim:mentions | umls-concept:C0001374 | lld:lifeskim |
| pubmed-article:2026625 | lifeskim:mentions | umls-concept:C0021017 | lld:lifeskim |
| pubmed-article:2026625 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
| pubmed-article:2026625 | lifeskim:mentions | umls-concept:C0033634 | lld:lifeskim |
| pubmed-article:2026625 | lifeskim:mentions | umls-concept:C0033640 | lld:lifeskim |
| pubmed-article:2026625 | lifeskim:mentions | umls-concept:C0038592 | lld:lifeskim |
| pubmed-article:2026625 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:2026625 | lifeskim:mentions | umls-concept:C1524075 | lld:lifeskim |
| pubmed-article:2026625 | lifeskim:mentions | umls-concept:C0443199 | lld:lifeskim |
| pubmed-article:2026625 | lifeskim:mentions | umls-concept:C0337112 | lld:lifeskim |
| pubmed-article:2026625 | pubmed:issue | 14 | lld:pubmed |
| pubmed-article:2026625 | pubmed:dateCreated | 1991-6-10 | lld:pubmed |
| pubmed-article:2026625 | pubmed:abstractText | Neutrophils possess a classical Ca2+, phosphatidyl serine (PS) and diglyceride (DG)-dependent protein kinase C (beta-PKC) which was translocatable from cytosol to membrane in response to elevated Ca2+ in the physiologic range or to pretreatment with phorbol myristate acetate (PMA). The translocatable beta-PKC was purified from neutrophil membranes prepared in the presence of Ca2+, eluted with EGTA and subjected to hydroxyapatite chromatography. An 80-kDa protein possessing Ca/DG/PS-dependent histone phosphorylating activity was recognized by a monoclonal antibody to beta-PKC but not to alpha-PKC or gamma-PKC. A cytosolic kinase activity remaining after Ca(2+)-induced translocation of beta-PKC was dependent on PS and DG but did not require Ca2+. This novel Ca(2+)-independent, PS/DG-dependent kinase, termed nPKC, eluted from hydroxyapatite between alpha-PKC and beta-PKC, ran as a 76-kDa band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and was reactive to a polyclonal consensus antibody but not to monoclonal antibodies to alpha-PKC, beta-PKC, or gamma-PKC. Long chain fatty acyl-CoA, but not the corresponding free fatty acids, inhibited nPKC in the 1-10 microM range. The chemotactic peptide fMet-Leu-Phe triggered prompt but transient increases in neutrophil long chain fatty acid acyl-CoA, suggesting that nPKC is regulated by fatty acyl-CoA as well as DG during neutrophil activation. Purified beta-PKC phosphorylated a number of cytosolic proteins in a Ca(2+)-dependent manner, including a major 47-kDa cytosolic protein, which may be implicated in superoxide anion generation. In contrast, nPKC did not phosphorylate the 47-kDa protein, but phosphorylated numerous cytosolic proteins in a Ca(2+)-independent manner, including a 66-kDa protein which was not phosphorylated by beta-PKC. Differences in location, substrate specificity, and cofactor dependence between nPKC and beta-PKC suggest these kinases may play selective roles in the activation sequence of the neutrophil. | lld:pubmed |
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| pubmed-article:2026625 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2026625 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2026625 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2026625 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2026625 | pubmed:month | May | lld:pubmed |
| pubmed-article:2026625 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:2026625 | pubmed:author | pubmed-author:JohnstonR... | lld:pubmed |
| pubmed-article:2026625 | pubmed:author | pubmed-author:RosenO MOM | lld:pubmed |
| pubmed-article:2026625 | pubmed:author | pubmed-author:PhillipsW AWA | lld:pubmed |
| pubmed-article:2026625 | pubmed:author | pubmed-author:KorchakH MHM | lld:pubmed |
| pubmed-article:2026625 | pubmed:author | pubmed-author:CorkeyB EBE | lld:pubmed |
| pubmed-article:2026625 | pubmed:author | pubmed-author:MajumdarSS | lld:pubmed |
| pubmed-article:2026625 | pubmed:author | pubmed-author:FujikiTT | lld:pubmed |
| pubmed-article:2026625 | pubmed:author | pubmed-author:DirrEE | lld:pubmed |
| pubmed-article:2026625 | pubmed:author | pubmed-author:RossiM WMW | lld:pubmed |
| pubmed-article:2026625 | pubmed:author | pubmed-author:QueenC FCF | lld:pubmed |
| pubmed-article:2026625 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2026625 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:2026625 | pubmed:volume | 266 | lld:pubmed |
| pubmed-article:2026625 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2026625 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2026625 | pubmed:pagination | 9285-94 | lld:pubmed |
| pubmed-article:2026625 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:2026625 | pubmed:meshHeading | pubmed-meshheading:2026625-... | lld:pubmed |
| pubmed-article:2026625 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:2026625 | pubmed:articleTitle | Protein kinase C isotypes and signaling in neutrophils. Differential substrate specificities of a translocatable calcium- and phospholipid-dependent beta-protein kinase C and a phospholipid-dependent protein kinase which is inhibited by long chain fatty acyl coenzyme A. | lld:pubmed |
| pubmed-article:2026625 | pubmed:affiliation | Department of Pediatrics, University of Pennsylvania School of Medicine, Philadelphia 19104. | lld:pubmed |
| pubmed-article:2026625 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2026625 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:2026625 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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