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PKC beta would sensitize cervical cancer cells to chemotherapy via reducing the chemotherapy induced autophagy in cancer cells.
Loss of PRKCB2 expression is associated with colorectal cancer.
significantly different gene expressions of BECN1 and PRKCB between the control and the Alzheimer's disease (AD) groups and of CDKN2A between the control and the preclinical AD groups, are reported.
a primary functional variant of PRKCB (rs35015313) was identified by genotype imputation using a phased panel of 1,070 Japanese individuals from a prospective, general population cohort study and subsequent in vitro functional analyses. These results may lead to improved understanding of the disease pathways involved in primary biliary cholangitis.
our findings identify PRKCB gene as a novel candidate gene for familial Meniere's Disease (MD )and its expression gradient in supporting cells of the organ of Corti deserves attention, given the role of supporting cells in K(+ )recycling within the endolymph, and its apical turn location may explain the onset of hearing loss at low frequencies in MD
Activation of the Pro-Oxidant PKCbetaII-p66Shc (show SHC1 Proteins) Signaling Pathway Contributes to Pericyte Dysfunction in Skeletal Muscles of Patients With Diabetes With Critical Limb Ischemia
Taken together, these data argue for a complex mechanism of PKC-beta-dependent regulation of SH (show POLD3 Proteins)CA (p66) activation invol (show SIGLEC1 Proteins)ving Ser(139) and a motif surroun (show SIGLEC1 Proteins)ding Ser(213).
The study aimed to identify a small set of genetic signatures that may reliably predict the individuals with a high genetic propensity to heroin addiction. A set of 4 genes (JUN (show JUN Proteins), CEBPB (show CEBPB Proteins), PRKCB, ENO2 (show ENO2 Proteins), or CEBPG (show CEBPG Proteins)) could predict the diagnosis of heroin addiction with the accuracy rate around 85% in our dataset.
Our results provide compelling evidence that glucose-induced PKCalpha (show PKCa Proteins)/PKCbeta-mediated inhibition of Kv current in vascular smooth muscle causes an enhanced constrictor response. Inhibition of Kv current causes a significant depolarization of vascular myocytes leading to marked vasoconstriction
Data suggest that targeted manipulation of protein kinase C isoforms PKCalpha (show PKCa Proteins), PKCbeta, and PKCeta might be beneficial in certain proteinuric kidney diseases with altered transient receptor potential cation channel subfamily C member 6 (show TRPC6 Proteins) protein (TRPC6 (show TRPC6 Proteins)) functions.
propose that PKCbeta acts to suppress the degradation of FTO (show FTO Proteins) protein and reveals the associated role of PKCbeta and FTO (show FTO Proteins) in adipogenesis, suggesting a new pathway that affects the development of obesity and metabolic diseases
Cytosolic NELL2 specifically interacts with PKC beta isotypes and inhibits PKC beta1 through direct binding to the N-terminal pseudosubstrate domain of PKC beta1.
Taken together, these data argue for a complex mechanism of PKCbeta-dependent regulation of p66 (show POLD3 Proteins) activation involving Ser (show SIGLEC1 Proteins)(139) and a motif surrounding Ser (show SIGLEC1 Proteins)(213).
Translocation of PKC-betaII from the cytoplasm to membranes is required for phagocytosis of apoptotic cells and is inhibited by soluble beta-glucan
repressor of myogenesis; opposes calcineurin function
at the functionally mature calyx of Held synapse the Ca(2+)-dependent protein kinase C isoforms alpha and beta are necessary for post-tetanic potentiation, a form of plasticity thought to underlie short-term memory
a new mechanism by which PKC-beta activation promotes EC dysfunction caused by the de-regulation of the IL-18 (show IL18 Proteins)/IL-18BP (show IL18BP Proteins) pathway, leading to increased VCAM-1 (show VCAM1 Proteins) expression, monocyte/macrophage adhesion, and accelerated atherosclerotic plaque formation in diabetes
These results demonstrate the importance of PKCbetaII in chronic lymphocytic leukemia-like disease progression and suggest a role for PKCalpha (show PKCa Proteins) subversion in creating permissive conditions for leukemogenesis.
PKCbeta2 inhibition protects mice from gut (show GUSB Proteins) ischemia-reperfusion injury by suppressing the adaptor p66(Shc)-mediated oxidative stress and subsequent apoptosis.
PKC-alpha (show PKCa Proteins) and -betaIotaIota are the predominant isoforms in the developing optic pathway, whereas PKC-epsilon (show PRKCE Proteins) is the major form in the chiasmatic neurons.
The study identified the serine phosphorylation (p-Ser (show SIGLEC1 Proteins)) sites induced by PKC-Beta activation or AGT (show AGT Proteins), which inhibits insulin (show INS Proteins)-induced p-Tyr (show TYR Proteins) sites on IRS2 (show IRS2 Proteins) and its signals in endothelial cells.
ET-1 (show EDN1 Proteins)-mediated myocardial contractile dysfunction during cardioplegia involves activation of protein kinase C beta II.
The PKCalpha (show PKCa Proteins), PKCbeta1, and PKCbeta2 mRNA levels tended to be lower in ischemia-reperfused than in sham-operated eyes in both the retinal arteries and the neuroretina.
Increases in epicardial perivascular adipose tissue leptin (show LEP Proteins) exacerbate coronary endothelial dysfunction in MetS via a PKC-beta-dependent pathway.
first study to show the expression and cellular localization of PKC beta I in the retina of pigs with development, and these results suggest that PKC beta I, in accordance with PKC alpha (show PKCa Proteins), plays important roles in signal transduction pathways in the pig retina with development
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 family members 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 a distinct role in cells. The protein encoded by this gene is one of the PKC family members. This protein kinase has been reported to be involved in many different cellular functions, such as B cell activation, apoptosis induction, endothelial cell proliferation, and intestinal sugar absorption. Studies in mice also suggest that this kinase may also regulate neuronal functions and correlate fear-induced conflict behavior after stress. Alternatively spliced transcript variants encoding distinct isoforms have been reported.
, protein kinase C beta type
, protein kinase C, beta 1 polypeptide
, protein kinase C beta-II
, protein kinase C, beta 1
, protein kinase C beta I
, protein kinase C beta II
, protein kinase C beta 1
, protein kinase C, beta
, protein kinase C beta 2