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Protein kinase c activity restricts dendritic arborization during embryonic brain circuit development through synaptotropic stabilization of dynamic processes.
Our findings demonstrate the mechanism of PKCzeta as a new phosphorylase of SIRT6 on maintaining tumor fatty acid beta-oxidation and define the new role of PKCzeta in lipid homeostasis.
Protein kinase C acts as a tumor suppressor.Cancer-associated mutations in protein kinase C are generally loss-of-function mutations.[review]
We also carried out PKC-iota and PKC-zeta directed siRNA treatments to prove the above observations. Immunoprecipitation data suggested an association between PKC-iota and vimentin and PKC-iota siRNA treatments confirmed that PKC-iota activates vimentin by phosphorylation. These results further suggested that PKC-iota is involved in signaling pathways which upregulate EMT and which can be effectively suppressed using A...
PKCzeta promoted lung adenocarcinoma invasion and metastasis, and its expression was associated with MMP2 and MMP9 expression.
PKC-zeta may be responsible for the abnormal growth, proliferation, and migration of metastatic LOVO colon cancer cells via PKC-zeta/Rac1/Pak1/beta-Catenin pathway.
reduced expression of PKCzeta/Pard3/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 remarkably attenuated gut injury by suppressing apoptosis. H/R induced PKCzeta to combine with TRAF2, which was phosphorylated by PKCzeta at Ser(55), but not at Ser(11), under intestinal I/R or H/R conditions
these results conclude that miR-25 targets PKCzeta and protects osteoblastic cells from Dex via activating AMPK signaling.
PKCzeta was specifically involved in ACOT7 depletion-mediated cell cycle arrest as an upstream molecule of the p53-p21 signaling pathway in MCF7 human breast carcinoma and A549 human lung carcinoma cells.
we found that Wnt3a treatment rapidly induces hyperphosphorylation and stabilization of Dvl2 and Dvl3. Our findings suggest a model of positive regulation of PKCzeta-mediated Dvl signaling activity, to produce a strong and sustained response to Wnt3a treatment by stabilizing Dvl 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.
Drug discovery efforts have been hindered due to the non-availability of the protein structure and hence in the present study we attempted to build the open and closed models of the protein PKMzeta using homology modeling.
This study demonstrated that zinc upregulates PKCzeta by activating GPR39 to enhance the abundance of ZO-1, 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 and interleukin-10
Here we provide the first evidence that PKC-zeta is a potential target for the treatment of COPD by selective small molecules
Study provides evidence for a novel PKC-zeta to p47phox interaction that is required for cell transformation from blebbishields and ROS production in cancer cells.
FRET-based translocation assays reveal that insulin promotes the association of both p62 and aPKC with the insulin-regulated scaffold IRS-1.
data suggest that the interaction between this novel region in Galphaq and the effector PKCzeta is a key event in Galphaq signaling.
The PKC-zeta - induced phosphorylation of GSK-3 beta stimulates GSK-3 beta activity.
Over-expression of PRKCZ results in gene and/or protein expression alterations of insulin-like growth factor 1 receptor (IGF1R) and integrin beta 3 (ITGB3) in SKOV3 and OVCAR3 cells.
protein kinase M zeta expression in the anterior cingulate cortex is enhanced by peripheral nerve injury in a transcription-independent manner.
this study elucidates the role of the aPKC-CBP pathway in modulating neurovascular remodeling and functional recovery following focal ischemic stroke.
HIF regulation of HOIL-1L targets the phosphorylated PKC-zeta for degradation and serves as an hypoxia-adaptive mechanism to stabilize the Na,K-ATPase, avoiding significant lung injury.
Under physiological conditions, PKMzeta is the principal PKC isoform that maintains LTP 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(-/-) mice, suggesting that these molecules were major downstream effectors of Angptl4.
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 phosphorylation and recruitment to the mCRAMP promoter, leading to enhanced transcription
APPL1 enhances glucose uptake by modulating the activation and localization of PKCzeta, as well as its functional interaction with both PP2A and myosin IIa.
Findings indicate PDZRN3 regulates vascular permeability through a PKCzeta-containing complex.
Thus, whereas PKMzeta is essential for wild-type long-term potentiation and long-term memory, persistent PKCiota/lambda activation compensates for PKMzeta loss in PKMzeta-null mice.
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 resistance (overweight and diabetes type 2) by regulating downstream signal transduction components mTOR (mammalian target of rapamycin protein) and Ccnd2 (cyclin-D2).
androstenedione administration increased Akt1 and PKC zeta phosphorylation in the muscle tissue of C57BL6 mice.
studies support a model wherein an alternative mechanism regulates PKCzeta-mediated insulin signalling that does not utilize conventional activation via agonist-evoked phosphorylation at the activation loop
PKCzeta/p62 activation stimulated inflammatory cytokine production and enhanced IGF-I-stimulated VSMC proliferation
Neuronal NF1/RAS regulation of cyclic AMP requires atypical PKC zeta activation, which is perturbed in neurofibromatosis type 1.
Asymmetric division and CD8+ T lymphocyte fate specification is regulated by protein kinase Czeta and protein kinase Clambda.
Data indicate that pseudosubstrate arginine residues are key regulators of atypical protein kinase C-lambda and atypical protein kinase C-zeta.
Lgl1 forms two distinct complexes in vivo, Lgl1-NMIIA and Lgl1-Par6alpha-aPKCzeta, and that the formation of these complexes is affected by the phosphorylation state of Lgl1.
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, via phosphorylation of eNOS on Thr(497) by PKC zeta, is responsible, at least in part, for inhibition of VEGF-stimulated endothelial permeability by Ang-1.
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