FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1988556835> ?p ?o ?g. }

• W1988556835 endingPage "393" @default.
• W1988556835 startingPage "380" @default.
• W1988556835 abstract "Prior studies have shown that vitamin D regulation of protein kinase C activity (PKC) in the cell layer of chondrocyte cultures is cell maturation-dependent. In the present study, we examined the membrane distribution of PKC and whether 1α,25-(OH)2D3 and 24R,25-(OH)2D3 can directly regulate enzyme activity in isolated plasma membranes and extracellular matrix vesicles. Matrix vesicle PKC was activated by bryostatin-1 and inhibited by a PKC-specific pseudosubstrate inhibitor peptide. Depletion of membrane PKC activity using isoform-specific anti-PKC antibodies suggested that PKCα is the major isoform in cell layer lysates as well as in plasma membranes isolated from both cell types; PKCζ is the predominant form in matrix vesicles. This was confirmed in Western blots of immunoprecipitates as well as in studies using control peptides to block binding of the isoform specific antibody to the enzyme and using a PKCζ-specific pseudosubstrate inhibitor peptide. The presence of PKCζ in matrix vesicles was further verified by immunoelectron microscopy. Enzyme activity in the matrix vesicle was insensitive to exogenous lipid, whereas that in the plasma membrane required lipid for full activity. 1,25-(OH)2D3 and 24,25-(OH)2D3 inhibited matrix vesicle PKC, but stimulated plasma membrane PKC when added directly to the isolated membrane fractions. PKC activity in the matrix vesicle was calcium-independent, whereas that in the plasma membrane required calcium. Moreover, the vitamin D-sensitive PKC in matrix vesicles was not dependent on calcium, whereas the vitamin D-sensitive enzyme in plasma membranes was calcium-dependent. It is concluded that PKC isoforms are differentially distributed between matrix vesicles and plasma membranes and that enzyme activity is regulated in a membrane-specific manner. This suggests the existence of a nongenomic mechanism whereby the effects of 1,25-(OH)2D3 and 24,25-(OH)2D3 may be mediated via PKC. Further, PKCζ may be important in nongenomic, autocrine signal transduction at sites distal from the cell. © 1996 Wiley-Liss, Inc." @default.
• W1988556835 created "2016-06-24" @default.
• W1988556835 creator A5029880479 @default.
• W1988556835 creator A5046003294 @default.
• W1988556835 creator A5052368052 @default.
• W1988556835 creator A5066597811 @default.
• W1988556835 creator A5067715356 @default.
• W1988556835 creator A5072899732 @default.
• W1988556835 creator A5073060614 @default.
• W1988556835 date "1996-06-01" @default.
• W1988556835 modified "2023-10-17" @default.
• W1988556835 title "Nongenomic regulation of protein kinase C isoforms by the vitamin D metabolites 1α,25-(OH)2D3 and 24R,25-(OH)2D3" @default.
• W1988556835 cites W148785554 @default.
• W1988556835 cites W1491958169 @default.
• W1988556835 cites W1550946273 @default.
• W1988556835 cites W1553713007 @default.
• W1988556835 cites W1571844404 @default.
• W1988556835 cites W1573258139 @default.
• W1988556835 cites W1576708287 @default.
• W1988556835 cites W1587135257 @default.
• W1988556835 cites W1965979895 @default.
• W1988556835 cites W1974955088 @default.
• W1988556835 cites W1976404758 @default.
• W1988556835 cites W1990938161 @default.
• W1988556835 cites W1992176184 @default.
• W1988556835 cites W1997442781 @default.
• W1988556835 cites W1999566158 @default.
• W1988556835 cites W2004624711 @default.
• W1988556835 cites W2008407614 @default.
• W1988556835 cites W2016068011 @default.
• W1988556835 cites W2030464593 @default.
• W1988556835 cites W2031430407 @default.
• W1988556835 cites W2032691911 @default.
• W1988556835 cites W2042187005 @default.
• W1988556835 cites W2043525438 @default.
• W1988556835 cites W2064689399 @default.
• W1988556835 cites W2070194131 @default.
• W1988556835 cites W2071502893 @default.
• W1988556835 cites W2072487937 @default.
• W1988556835 cites W2073882699 @default.
• W1988556835 cites W2085536935 @default.
• W1988556835 cites W2090464853 @default.
• W1988556835 cites W2117227310 @default.
• W1988556835 cites W2127010550 @default.
• W1988556835 cites W2138011807 @default.
• W1988556835 cites W2153465154 @default.
• W1988556835 cites W2160176627 @default.
• W1988556835 cites W2166259149 @default.
• W1988556835 cites W2228774691 @default.
• W1988556835 cites W2414175907 @default.
• W1988556835 cites W4232534952 @default.
• W1988556835 cites W4256011908 @default.
• W1988556835 cites W4299669929 @default.
• W1988556835 doi "https://doi.org/10.1002/(sici)1097-4652(199606)167:3<380::aid-jcp2>3.0.co;2-l" @default.
• W1988556835 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8655592" @default.
• W1988556835 hasPublicationYear "1996" @default.
• W1988556835 type Work @default.
• W1988556835 sameAs 1988556835 @default.
• W1988556835 citedByCount "103" @default.
• W1988556835 countsByYear W19885568352012 @default.
• W1988556835 countsByYear W19885568352013 @default.
• W1988556835 countsByYear W19885568352014 @default.
• W1988556835 countsByYear W19885568352015 @default.
• W1988556835 countsByYear W19885568352016 @default.
• W1988556835 countsByYear W19885568352018 @default.
• W1988556835 countsByYear W19885568352022 @default.
• W1988556835 crossrefType "journal-article" @default.
• W1988556835 hasAuthorship W1988556835A5029880479 @default.
• W1988556835 hasAuthorship W1988556835A5046003294 @default.
• W1988556835 hasAuthorship W1988556835A5052368052 @default.
• W1988556835 hasAuthorship W1988556835A5066597811 @default.
• W1988556835 hasAuthorship W1988556835A5067715356 @default.
• W1988556835 hasAuthorship W1988556835A5072899732 @default.
• W1988556835 hasAuthorship W1988556835A5073060614 @default.
• W1988556835 hasConcept C130316041 @default.
• W1988556835 hasConcept C184235292 @default.
• W1988556835 hasConcept C185592680 @default.
• W1988556835 hasConcept C195794163 @default.
• W1988556835 hasConcept C41625074 @default.
• W1988556835 hasConcept C55493867 @default.
• W1988556835 hasConcept C86803240 @default.
• W1988556835 hasConcept C95444343 @default.
• W1988556835 hasConceptScore W1988556835C130316041 @default.
• W1988556835 hasConceptScore W1988556835C184235292 @default.
• W1988556835 hasConceptScore W1988556835C185592680 @default.
• W1988556835 hasConceptScore W1988556835C195794163 @default.
• W1988556835 hasConceptScore W1988556835C41625074 @default.
• W1988556835 hasConceptScore W1988556835C55493867 @default.
• W1988556835 hasConceptScore W1988556835C86803240 @default.
• W1988556835 hasConceptScore W1988556835C95444343 @default.
• W1988556835 hasIssue "3" @default.
• W1988556835 hasLocation W19885568351 @default.
• W1988556835 hasLocation W19885568352 @default.
• W1988556835 hasOpenAccess W1988556835 @default.
• W1988556835 hasPrimaryLocation W19885568351 @default.
• W1988556835 hasRelatedWork W1638339816 @default.
• W1988556835 hasRelatedWork W1926803380 @default.
• W1988556835 hasRelatedWork W1979156653 @default.

• next