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Protein kinase c activity restricts dendritic arborization during embryonic brain circuit development through synaptotropic stabilization of dynamic processes.
PKCzeta promoted lung adenocarcinoma invasion and metastasis, and its expression was associated with MMP2 (show MMP2 Proteins) and MMP9 (show MMP9 Proteins) expression.
PKC-zeta may be responsible for the abnormal growth, proliferation, and migration of metastatic LOVO colon cancer cells via PKC-zeta/Rac1/Pak1 (show PAK1 Proteins)/beta-Catenin (show CTNNB1 Proteins) pathway.
reduced expression of PKCzeta/Pard3 (show PARD3 Proteins)/Pard6 contributes to non-small-cell lung cancer epithelial-mesenchymal transition, invasion, and chemoresistance.
Intestinal I/R induced the membrane translocation and phosphorylation of PKCzeta. Pretreatment with the PKCzeta activator phosphatidylcholine (show SGMS2 Proteins) remarkably attenuated gut (show GUSB Proteins) injury by suppressing apoptosis. H/R induced PKCzeta to combine with TRAF2 (show TRAF2 Proteins), which was phosphorylated by PKCzeta at Ser (show SIGLEC1 Proteins)(55), but not at Ser (show SIGLEC1 Proteins)(11), under intestinal I/R or H/R conditions
these results conclude that miR (show MLXIP Proteins)-25 targets PKCzeta and protects osteoblastic cells from Dex via activating AMPK (show PRKAA1 Proteins) signaling.
PKCzeta was specifically involved in ACOT7 (show ACOT7 Proteins) depletion-mediated cell cycle arrest as an upstream molecule of the p53 (show TP53 Proteins)-p21 (show CDKN1A Proteins) signaling pathway in MCF7 human breast carcinoma and A549 human lung carcinoma cells.
we found that Wnt3a (show WNT3A Proteins) treatment rapidly induces hyperphosphorylation and stabilization of Dvl2 (show DVL2 Proteins) and Dvl3 (show DVL3 Proteins). Our findings suggest a model of positive regulation of PKCzeta-mediated Dvl (show DVL2 Proteins) signaling activity, to produce a strong and sustained response to Wnt3a (show WNT3A Proteins) treatment by stabilizing Dvl (show DVL2 Proteins) protein levels.
The data demonstrate that PKCzeta expression regulates the maturation of neonatal T-cells into specific functional phenotypes and that environmental influences may work via PKCzeta to regulate these phenotypes and disease susceptibility.
This study demonstrated that zinc upregulates PKCzeta by activating GPR39 (show GPR39 Proteins) to enhance the abundance of ZO-1 (show TJP1 Proteins), thereby improving epithelial integrity in S. typhimurium-infected Caco-2 cells.
Inhibition of protein kinase C zeta expression in prostate cancer cells promoted chemotaxis of peripheral macrophages and acquisition of M2 phenotypic features. These results were further supported by the finding that silencing of endogenous protein kinase C zeta promoted the expression of prostate cancer cell-derived interleukin-4 (show IL4 Proteins) and interleukin-10 (show IL10 Proteins)
HIF regulation of HOIL-1L (show RBCK1 Proteins) targets the phosphorylated PKC-zeta for degradation and serves as an hypoxia-adaptive mechanism to stabilize the Na,K-ATPase (show ATP1A1 Proteins), avoiding significant lung injury.
Under physiological conditions, PKMzeta is the principal PKC isoform that maintains LTP (show SCP2 Proteins) and long-term memory. PKCiota/lambda can compensate for PKMzeta, and because other isoforms could also maintain synaptic facilitation, there may be a hierarchy of compensatory mechanisms maintaining memory if PKMzeta malfunctions. [Review]
aPKCzeta is required for the cellular organization of acto-non-muscle myosin II (NMII) cytoskeleton, for proper cell adhesion and directed cell migration.
This study demonstrates that the combination therapy of PKCzeta and COX-2 inhibitors can significantly inhibit melanoma metastasis in vitro and in vivo, which will be an efficient strategy for treatment of melanoma metastasis in clinics
the inhibition of PKCzeta or ceramide synthesis did not further improve glucose tolerance in Angptl4 (show ANGPTL4 Proteins)(-/-) mice, suggesting that these molecules were major downstream effectors of Angptl4 (show ANGPTL4 Proteins).
Immunoblotting, qPCR, ChIP and siRNA-mediated gene knockdown studies revealed that the activation of phosphatidylinositol 3-kinase/protein kinase C zeta pathways in poly(I:C)-stimulated cells underlies Sp1 (show SP1 Proteins) phosphorylation and recruitment to the mCRAMP promoter, leading to enhanced transcription
APPL1 (show APPL1 Proteins) enhances glucose uptake by modulating the activation and localization of PKCzeta, as well as its functional interaction with both PP2A (show PPP2R2B Proteins) and myosin IIa.
Findings indicate PDZRN3 (show PDZRN3 Proteins) regulates vascular permeability through a PKCzeta-containing complex.
Data (including data from studies in transgenic and knockout mice) suggest that Pkcz (protein kinase C zeta) activation is key for early compensatory pancreatic beta-cell proliferation in insulin (show INS Proteins) resistance (overweight and diabetes type 2) by regulating downstream signal transduction components mTOR (mammalian target of rapamycin (show FRAP1 Proteins) protein) and Ccnd2 (cyclin-D2 (show CCND2 Proteins)).
These data identify atypical PKC isozymes as STAT and ERK activators that mediate c-fos and collagenase expression.
chronic exposure to hypoxia leads to the emergence of cells lacking anti-replication activity of PKCzeta in the pulmonary artery adventitia.
inhibition of NO production by Ang-1 (show ANGPT1 Proteins), via phosphorylation of eNOS (show NOS3 Proteins) on Thr (show TRH Proteins)(497) by PKC zeta, is responsible, at least in part, for inhibition of VEGF (show VEGFA Proteins)-stimulated endothelial permeability by Ang-1 (show ANGPT1 Proteins).
ceramide as a potent physiological modulator of the Na(+)-ATPase, participating in a regulatory network in kidney cells and counteracting the stimulatory effect of PKA via PKCzeta.
Zebrafish pronephros tubulogenesis and epithelial identity maintenance are reliant on the polarity proteins Prkc iota and zeta.
Protein kinase C (PKC) zeta is a member of the PKC family of serine/threonine kinases which are involved in a variety of cellular processes such as proliferation, differentiation and secretion. Unlike the classical PKC isoenzymes which are calcium-dependent, PKC zeta exhibits a kinase activity which is independent of calcium and diacylglycerol but not of phosphatidylserine. Furthermore, it is insensitive to typical PKC inhibitors and cannot be activated by phorbol ester. Unlike the classical PKC isoenzymes, it has only a single zinc finger module. These structural and biochemical properties indicate that the zeta subspecies is related to, but distinct from other isoenzymes of PKC. Alternative splicing results in multiple transcript variants encoding different isoforms.
protein kinase C, zeta
, protein kinase c type Z
, protein kinase C zeta type
, protein kinase C zeta type-like
, atypical protein kinase C
, protein kinase C zeta subspecies
, 14 - 3 - 3 - zeta isoform
, atypical protein kinase C zeta