Tumor necrosis factor alpha modifies agonist-dependent responses in human neutrophils by inducing the synthesis and myristoylation of a specific protein kinase C substrate.
Thelen M, Rosen A, Nairn A, Aderem A. Tumor necrosis factor alpha modifies agonist-dependent responses in human neutrophils by inducing the synthesis and myristoylation of a specific protein kinase C substrate. Proceedings Of The National Academy Of Sciences Of The United States Of America 1990, 87: 5603-5607. PMID: 2116001, PMCID: PMC54375, DOI: 10.1073/pnas.87.15.5603.Peer-Reviewed Original ResearchMeSH KeywordsColony-Stimulating FactorsGranulocyte-Macrophage Colony-Stimulating FactorGrowth SubstancesHumansIn Vitro TechniquesInterferon-gammaIntracellular Signaling Peptides and ProteinsKineticsLipopolysaccharidesLysineMembrane ProteinsMyristic AcidMyristic AcidsMyristoylated Alanine-Rich C Kinase SubstrateNeutrophilsPhosphatesPhosphopeptidesPhosphorylationProtein BiosynthesisProtein Kinase CProteinsRecombinant ProteinsTumor Necrosis Factor-alphaConceptsSpecific protein kinase C substrateProtein kinase C substrateProtein kinase CC substrateKinase C.Kinase CAlanine-rich C kinase substratePhosphorylation of MARCKSN-terminal glycineC kinase substrateProtein kinase C.Agonist-dependent responsesIdentical phosphopeptidesKinase substrateTransduction pathwaysMARCKS phosphorylationMARCKSEnhanced phosphorylationHuman neutrophilsMurine fibroblastsEffector moleculesProteinPhosphorylationMyristoylationBovine brain