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INS — PRKCA

Text-mined interactions from Literome

Formisano et al., Mol Cell Biol 2000 (MAP Kinase Signaling System) : In L6 muscle cells expressing wild-type human insulin receptors ( L6hIR ), insulin induced protein kinase Calpha (PKCalpha) and beta activities ... In L6hIR cells, inhibition of insulin receptor substrate 1 (IRS-1) expression caused a 90 % decrease in insulin induced PKCalpha and -beta activation and blocked insulin stimulation of mitogen activated protein kinase ( MAPK ) and DNA synthesis ... ( i ) The tyrosine kinase activity of the IR is necessary for insulin activation of PKCalpha and -beta
Bihlmayer et al., Neuroendocrinology 2001 (Insulinoma...) : It is suggested that PKC alpha , beta and/or zeta may play a role in the modulation of insulin secretion by GRP
Lin et al., Am J Physiol Endocrinol Metab 2001 : Muscles preincubated for 1 h with 1 microM phorbol 12,13-dibutyrate ( PDBu ) showed an impaired ability of insulin to stimulate glucose incorporation into glycogen and a translocation of PKC-alpha , -betaI, -theta, and -epsilon, and probably -betaII, from the cytosol to membranes
Motley et al., Hypertension 2002 : PKC-alpha , but not PKC-beta, is expressed in vascular smooth muscle cells, and overexpression of PKC-alpha, but not PKC-beta or PKC-delta, inhibited insulin induced Akt activation
Leitges et al., Mol Endocrinol 2002 : We conclude that 1 ) PKC alpha is not required for insulin stimulated glucose transport, and 2 ) PKC alpha is activated by insulin at least partly independently of PI3K, and largely serves as a physiological feedback inhibitor of insulin signaling to the insulin receptor substrate 1/PI3K/PKB/PKC lambda/zeta/iota complex and dependent metabolic processes
Tsuru et al., Am J Physiol Endocrinol Metab 2002 : Insulin also activated the overexpressed PKC-delta but not PKC-alpha
Lesage et al., Hepatology 2002 : Insulin induced activation of PKC alpha , which decreased secretin stimulated cAMP and PKA activity
Vigliotta et al., Mol Cell Biol 2004 (Diabetes Mellitus) : In vivo, insulin stimulated glucose uptake was decreased by almost 50 % in fat and muscle tissues of the ped/pea-15 transgenic mice, accompanied by protein kinase Calpha activation and block of insulin induction of protein kinase Czeta
Warwar et al., Diabetes 2006 (Diabetes Mellitus, Type 2) : Data from this and related studies support a role for PKCalpha in glucose induced insulin granule recruitment for exocytosis ; a role for PKCepsilon in activation of insulin granules for exocytosis and/or in the glucose generated time dependent potentiation signal for insulin release ; and a dual function for PKCzeta in initiating insulin release and in a regulatory role in the transcriptional machinery
Cipok et al., Biochem Biophys Res Commun 2006 : PKCalpha may regulate IRS activity in response to insulin ... PKCalpha is constitutively associated with IRS-1, and insulin stimulation of PKCalpha causes disassociation of the two proteins within 5 min. Blockade of PKCalpha inhibited insulin induced disassociation of PKCalpha from IRS1 ... Insulin stimulation activates PKB and increases the association of PKCalpha with PKB ... We suggest that PKCalpha regulates insulin signaling in skeletal muscle through its disassociation from IRS-1 and association with PKB
Horovitz-Fried et al., Biochem Biophys Res Commun 2007 : In contrast, in the nucleus insulin induced an increase in association between PKCalpha and SP-1 ... PKCalpha inhibition blocked insulin induced serine phosphorylation of SP-1 and its association with PKCalpha in the nucleus ... Thus, PKCalpha regulates insulin induced PKCdelta expression levels and this regulation involves activation of SP-1 and NFkappaB
Kotova et al., Cell Mol Biol Incl Cyto Enzymol 2006 : Ouabain reduced basal and insulin stimulated phosphorylation of PKC alpha/beta and delta isoforms, whereas phosphorylation of PKCzeta was unchanged
Nakamura et al., Biochim Biophys Acta 2007 : Western blot analysis revealed that insulin slightly increases membrane bound PKCalpha , betaI, and delta, and wortmannin decreases PKCbetaI, betaII, and delta in the membrane fraction
Avignon et al., Biochem J 1995 : Insulin increases mRNA levels of protein kinase C-alpha and -beta in rat adipocytes and protein kinase C-alpha, -beta and -theta in rat skeletal muscle ... Insulin also stimulated the apparent translocation of PKC-alpha , -beta, -epsilon and -theta, to the membrane fractions of adipocytes, adipose tissue and gastrocnemius muscles, and, in some instances, total PKC levels were diminished, e.g. PKC-alpha and PKC-beta in cultured adipocytes in vitro and/or whole adipose tissue in vivo, and PKC-alpha and PKC-theta in the gastrocnemius muscle ... We conclude that insulin induced translocation and degradation of PKC-alpha , PKC-beta and PKC-theta are attended by selective increases in their mRNAs
Standaert et al., Biochem J 1996 (Diabetes Mellitus, Type 2) : Our findings suggest that insulin acts through PI 3-kinase to activate a PC-specific phospholipase D and causes the translocative activation of PKC-alpha and PKC-beta in plasma membranes of rat adipocytes
Formisano et al., J Biol Chem 1998 : Selective depletion of cellular PKC-alpha and -delta, by 24 h of 12-O-tetradecanoylphorbol-13-acetate ( TPA ) exposure, reduced insulin degradation by 3-fold and similarly increased insulin retroendocytosis, with no change in PKC-zeta
Antoine et al., Endocrinology 1998 : Insulin induction of protein kinase C alpha expression is independent of insulin receptor Tyr1162/1163 residues and involves mitogen activated protein kinase kinase 1 and sustained activation of nuclear p44MAPK ... We examined the effect of insulin on protein kinase C alpha (PKCalpha) expression and the implication of the mitogen activated protein kinase kinase 1 mitogen activated protein kinase ( MAPK ) pathway in this effect ... Insulin induction of PKCalpha expression involved the MEK1MAPK pathway, as it was 1 ) almost completely suppressed by the potent MEK1 inhibitor PD98059, 2 ) mimicked by the dominant-active MEK1 ( S218D/S222D ) mutant, and 3 ) associated with sustained MAPK activation ... These results indicate that induction of PKCalpha gene expression by insulin is independent of Tyr1162/1163 autophosphorylation sites and correlates with sustained activation of p44MAPK at the nuclear level
Miura et al., Biochem Mol Biol Int 1998 (Insulinoma) : These results suggest that TPA independently provokes insulin secretion via PKC activation and that PKC alpha and beta activation may be involved in insulin secretion in human insulinoma cells