Phosphorylation of human serum amyloid A protein by protein kinase C

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dc.contributor.authorNel A.E.
dc.contributor.authorDe Beer M.C.
dc.contributor.authorShephard E.G.
dc.contributor.authorStrachan A.F.
dc.contributor.authorVandenplas M.L.
dc.contributor.authorDe Beer F.C.
dc.date.accessioned2011-05-15T16:03:24Z
dc.date.available2011-05-15T16:03:24Z
dc.date.issued1988
dc.description.abstractMonokine-induced hepatic secretion of serum amyloid A protein (apo-SAA), an acute-phase reactant, is followed by rapid association with high-density lipoprotein (HDL) in plasma. Plasma clearance of apo-SAA is more rapid than any of the other HDL apolipoproteins. It has been shown that, of the acute-phase HDL3 apolipoproteins, apo-SAA preferentially associated with neutrophil membranes. HDL apolipoproteins have been shown to activate protein kinase C in endothelial cells. We therefore investigated potential phosphorylation of HDL3 apolipoproteins by protein kinase C. Apo-SAA was the only apolipoprotein phosphorylated (K(m) = 12 mM). Phosphorylation of the apo-SAA-containing HDL3 particle was selective for the more basic isoforms of apo-SAA (pI 7.0, 7.4, 7.5 and 8.0), with more acidic isoforms being phosphorylated when delipidated acute-phase apolipoproteins were used as substrate. However, phosphorylation was not in itself responsible for the establishment of the apo-SAA isoforms.
dc.description.versionArticle
dc.identifier.citationBiochemical Journal
dc.identifier.citation255
dc.identifier.citation1
dc.identifier.issn2646021
dc.identifier.urihttp://hdl.handle.net/10019.1/12608
dc.subjectacute phase protein
dc.subjectamyloid protein
dc.subjectapolipoprotein
dc.subjecthigh density lipoprotein
dc.subjectmonokine
dc.subjectprotein kinase c
dc.subjecthuman
dc.subjectpriority journal
dc.subjectprotein phosphorylation
dc.subjectAmino Acids
dc.subjectAmyloid Protein SAA
dc.subjectApolipoproteins
dc.subjectCell Line
dc.subjectElectrophoresis, Polyacrylamide Gel
dc.subjectHuman
dc.subjectIsoelectric Focusing
dc.subjectPeptide Mapping
dc.subjectPhosphorylation
dc.subjectProtein Kinase C
dc.subjectSupport, Non-U.S. Gov't
dc.titlePhosphorylation of human serum amyloid A protein by protein kinase C
dc.typeArticle
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