Biochemical and Biophysical Research Communications
Regular ArticleN-Protein Kinase C Isoenzymes May Be Involved in the Regulation of Various Neutrophil Functions
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Incomplete activation of human eosinophils via the histamine H <inf>4</inf>-receptor: Evidence for ligand-specific receptor conformations
2012, Biochemical PharmacologyCitation Excerpt :However, a mechanism solely driven by elevation of [Ca2+]i is contradicted by the finding that histamine and UR-PI376, although they effectively elevated [Ca2+]i, did not induce EPO release. Thus, additional signaling mechanisms to elevated [Ca2+]i, e.g. activation of a calcium-independent isoforms of protein kinase C, are necessary to effectively induce degranulation of eosinophils [71,72]. In humans, the concentration of histamine in peripheral blood is about 1 nM in normal and 10 nM in allergic conditions [73].
PKC-δ controls the fMLF-induced overproduction of superoxide by neutrophils
2010, Free Radical Biology and MedicineProtein kinase Cζ is up-regulated in osteoarthritic cartilage and is required for activation of NF-κB by tumor necrosis factor and interleukin-1 in articular chondrocytes
2006, Journal of Biological ChemistryCitation Excerpt :Gö 6976 reportedly is also most potent against the Ca2+-requiring (conventional) PKC isoforms and is less potent against the nPKCs and aPKCs, with an IC50 for PKCζ of >10 μm (21, 59). Gö 6976 showed some inhibition of both IL-1 and TNF induction of NF-κB-luciferase activity, but it was no more potent in this assay than BIS, despite the fact that Gö 6976 has an IC50 ∼4-fold lower than BIS on cPKCs (21). Calphostin C is a compound that competes for the diacylglycerol/phorbol ester-binding site in the regulatory domain of the conventional and novel PKCs and competitively inhibits their activity (17).
Protein kinase Cα regulates insulin receptor signaling in skeletal muscle
2006, Biochemical and Biophysical Research CommunicationsCitation Excerpt :Assuming that the constitutive association of PKCα with IRS1 exerts a down-regulatory influence on IRS1, as suggested [18], the insulin-induced disassociation of PKCα from IRS1 could be an important component of the insulin signaling cascade. In support of this notion, we also found that inhibition of PKCα, by treatment with a selective inhibitor GO6976 [21,25], blocked insulin-induced disassociation of PKCα from IRS1 and increased the effect of insulin to lower blood glucose levels. The results of this study, in which PKCα was inhibited pharmacologically by administration of GO6976, are compatible with those recently reported from studies on animals in which the PKCα gene was selectively eliminated by homologous recombination [18].
Modulation of Kv3.1b potassium channel phosphorylation in auditory neurons by conventional and novel protein kinase C isozymes
2006, Journal of Biological ChemistryCitation Excerpt :Group I inhibitors were those that are known only to inhibit the conventional family of PKCs (cPKC), whereas the group II inhibitors act on both cPKC and nPKC. Gö6976 is a specific inhibitor of cPKCs and has no effect on the activity of nPKC or aPKC isozymes even at micromolar levels (25, 26). GF109203X is, at a concentration of 50 nm, a specific inhibitor of cPKCs.