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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