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anti-Human PKC gamma Antibodies:
anti-Mouse (Murine) PKC gamma Antibodies:
anti-Rat (Rattus) PKC gamma Antibodies:
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Human Polyclonal PKC gamma Primary Antibody for IHC (p), ELISA - ABIN545463
Uchino, Sakai, Kashiwagi, Shirai, Shinohara, Hirose, Iino, Yamamura, Saito: Isoform-specific phosphorylation of metabotropic glutamate receptor 5 by protein kinase C (PKC) blocks Ca2+ oscillation and oscillatory translocation of Ca2+-dependent PKC. in The Journal of biological chemistry 2004
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Polyclonal PKC gamma Primary Antibody for WB - ABIN540606
Saito, Shirai: Protein kinase C gamma (PKC gamma): function of neuron specific isotype. in Journal of biochemistry 2002
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Human Monoclonal PKC gamma Primary Antibody for IF, IP - ABIN533142
Kawakami, Kitaura, Yao, McHenry, Kawakami, Newton, Kang, Kato, Leitges, Rawlings, Kawakami: A Ras activation pathway dependent on Syk phosphorylation of protein kinase C. in Proceedings of the National Academy of Sciences of the United States of America 2003
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This study presented one of the largest SCA14 cohorts of patients reported contributing with novel variants and supporting the distinct phenotype spectrum with specific cellular defects resulting from different types of PRKCG mutations.
This study demonstrated that a combination of both, loss-of-function and gain-of-function mechanisms are likely to underlie the pathogenesis of SCA14, caused by mutations in the C1 domain of PKCgamma
This review showed that the PKC Gamma signaling related genes and calcium signaling related genes then discuss their role for both Purkinje cell dendritic development and cerebellar ataxia.
SUMOylation of EphB1 repressed activation of its downstream signaling molecule PKC-gamma, and consequently inhibited neuroblastoma tumorigenesis.
two out of three known mutations in the catalytic domain of PKCgamma did indeed show increased biological activity.
Lysophosphatidylcholines prime polymorphonuclear neutrophil through Hck-dependent activation of PKCdelta, which stimulates PKCgamma, resulting in translocation of phosphorylated p47(phox).
The gene-environment combination of PRKCG rs3745406 C allele, BDNF rs6265 G allele and high level of negative life events was significantly associated with major depressive disorder.
The results showed that carrier of rs454006*C allele and rs3745406*C might elevate the risk of osteosarcoma
Data suggest that PRKCG (protein kinase C gamma) phosphorylates TA isoforms of p63 (tumor protein p63) at Thr157 to stabilize them and promote cell apoptosis in tumor cells.
PKCgamma,mutated in the neurodegenerative disease spinocerebellar ataxia type 14 is a novel amyloidogenic protein.
The rs454006 polymorphism of the PRKCG gene correlated to osteosarcoma susceptibility and might increase the risk of osteosarcoma.
findings provide evidence for both an increased PKCgamma activity in Purkinje cells in vivo and for pathological changes typical for cerebellar disease thus linking increased and dysregulated activity of PKCgamma to development of cerebellar disease
we show that the mutation V138E of the protein kinase C gamma (PKCgamma) C1B domain, which is implicated in spinocerebellar ataxia type 14, exhibits a partially unfolded C-terminus
PKCgamma plays a critical role in cancer cells, and simultaneous inhibition of PKCgamma and Hsp90alpha synergistically prevents cell migration and promotes apoptosis in cancer cells.
A novel missense mutation, F643L, which maps to a highly conserved amino acid of the catalytic domain of protein kinase C gamma, extends the phenotype associated with the spinocerebellar ataxia type 14 (SCA14) locus.
Spinocerebellar ataxia type 14 mutant PKC-gamma upregulates Hsp70. Hsp70 has a role in degrading mutant PKC-gamma.
Exome sequencing of large, 5-generational British kindred finds a novel p.Arg26Gly mutation in the PRKCG gene causing familial spinocerebellar ataxia 14.
SCA14, a novel mutation in the PRKCG gene, was found in two families in Norway with autosomal dominant cerebellar ataxia.
We propose that variety of mutant gammaPKC characters integrally and complicatedly participate in the pathophysiology of SCA 14.
The Spinocerebellar ataxia type 14 is caused by mutations in the protein kinase C gamma (PKCgamma, PRKCG) gene with a hotspot for mutations in exon 4. Genetic testing for SCA14 is clinically available.
cPKCgamma knockout significantly increased the infarct volume of mice after experimental ischemic stroke. cPKCgamma knockout also aggravated the oxygen-glucose deprivation-induced cell death and morphological damage of neurites in culture, while cPKCgamma restoration could alleviate the ischemic injury. Phosphorylation levels of synapsin Ia/b Ser549 and 553 could be modulated by cPKCgamma following ischemia.
PRKCG is a protective modifier of Purkinje neuron degeneration in cerebellar ataxia mouse models.
our results suggest that the decrease in the activity of cPKCbetaII and cPKCgamma, especially cPKCgamma, may play key roles in the pathogenesis of diabetic encephalopathy.
cPKC&-gamma modulated sequential reactivation of mTOR inhibited autophagic flux in neurons exposed to OGD/R, which may provide endogenous interventional strategies for stroke, especially ischemia/reperfusion injury
PKCgamma-mediated down-regulation of UCHL1 alleviates ischemic neuronal injuries by decreasing autophagy via ERK-mTOR pathway.
CA8 is a novel important regulator of Purkinje cell dendritic development and that its expression is controlled by PKCgamma activity.
These results suggested that cPKCgamma-modulated neuron-specific autophagy improves the neurological outcome of mice following ischemic stroke through the Akt-mTOR pathway, providing a potential therapeutic target for ischemic stroke.
Immunoblotting and RT-PCR results showed that NIHL increased the expression of PKCgamma but decreased that of GABABR1 and GABABR2 at both protein and mRNA levels in the CNC
PRKCgamma is critical for the localization of slit diaphragm components in the mouse kidney.
Therefore, we propose that PKCgamma positively modulates dopamine release through beta2PIX phosphorylation.
These findings indicate that the identity of the calcium-dependent PKCgamma that mediates PTP controls the mechanism and functional consequences of Posttetanic potentiation.
This study provided new evidence to support the possibility of the involvement of PKC-gamma in the actions of volatile anesthetics in mice brain.
demonstrate a role for the gamma isotype of protein kinase C (PKCgamma) in food-mediated entrainment of behavior and the molecular clock
transient receptor potential 3 which is also needed for mGluR1-dependent slow excitatory postsynaptic potentials and motor coordination and associates with PKCgamma
Membrane residence time of PKCalpha after depolarization-induced translocation is significantly decreased when it is present with the mutant PKCgamma construct of spinocerebellar ataxia type 14.
cPLA(2)-dependent AA release is required for VEGF-induced Src-PLD1-PKCgamma-mediated pathological retinal angiogenesis
reports multiple cPKCgamma-interacting proteins in HPC mouse brain and suggested that cPKCgamma signaling molecules, especially the cPKCgamma-synapsin pathway, might be responsible for HPC-induced neuroprotection against cerebral ischemic injuries of mice
the expression of transthyretin and protein kinase Cgamma were increased in the prefrontal cortex but not in the hippocampus of naltrexone-treated mice
Here, substitution studies on peptides correlating to the C1B domain in PKC gamma show that a flexible structure and ability to be phosphorylated on serine 109 are critical for this purpose.
Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play distinct roles in cells. The protein encoded by this gene is one of the PKC family members. This protein kinase is expressed solely in the brain and spinal cord and its localization is restricted to neurons. It has been demonstrated that several neuronal functions, including long term potentiation (LTP) and long term depression (LTD), specifically require this kinase. Knockout studies in mice also suggest that this kinase may be involved in neuropathic pain development. Defects in this protein have been associated with neurodegenerative disorder spinocerebellar ataxia-14 (SCA14).
protein kinase C, gamma
, protein kinase C gamma type-like
, protein kinase C gamma type
, protein kinase C type I (gamma type)