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In human ovarian cancers, high PRKCI expression correlates with high expression (show TNF ELISA Kits) of TNFalpha and YAP1 and low infiltration of cytotoxic T cells
promotes epithelial-mesenchymal transition and induces immunosuppression through the aPKC-iota/P-Sp1 (show PSG1 ELISA Kits)/Snail (show SNAI1 ELISA Kits) signaling pathway in cholangiocarcinoma
Polarity signaling via CDC42 (show CDC42 ELISA Kits)/atypical protein kinase C (show PRKCZ ELISA Kits) can affect the dynamic turnover of the intermediate filament network to promote the polarization of the network itself.
a PI3K (show PIK3CA ELISA Kits)/PKCiota/cyclin E (show CCNE1 ELISA Kits) signaling pathway as a therapeutic target during ovarian tumorigenesis
results identify a novel role of PHLPP (show PHLPP1 ELISA Kits) in regulating aPKC and cell polarity.
the polarity function of PRKCI during cavitation
14-3-3zeta (show YWHAZ ELISA Kits)-mediated invasion of cancer cells was found to upregulate Snail (show SNAI1 ELISA Kits) through the activation of atypical protein kinase C (show PRKCZ ELISA Kits) (aPKC).
Upregulated expression of PRKCI and interaction with CDK7 (show CDK7 ELISA Kits) is associated with esophageal squamous cell carcinoma.
the results revealed that PRKCI rs546950 variant decreased the risk of prostate cancer in an Iranian population
effects. Further studies indicated that PRKCI knockdown-mediated autophagy was associated with the inactivation of phosphatidylinositol 3-kinase alpha/AKT (show AKT1 ELISA Kits)-mammalian target of rapamycin (show FRAP1 ELISA Kits) (PIK3CA (show PIK3CA ELISA Kits)/AKT (show AKT1 ELISA Kits)-MTOR (show FRAP1 ELISA Kits)) signaling.
he oncogenic activity of PRKCI relates in part to the up-regulation of TNFalpha (show TNF ELISA Kits) to promote an immune-suppressive tumor microenvironment characterized by an abundance of myeloid-derived suppressor cells and inhibition of cytotoxic T-cell infiltration
Selective deletion of the aPKC isoform Pkc (show PKC ELISA Kits)-lambda in proopiomelanocortin (POMC (show POMC ELISA Kits)) neurons disrupts leptin (show LEP ELISA Kits) action, reduces melanocortin content in the paraventricular nucleus, and markedly increases susceptibility to obesity, glucose intolerance, and insulin (show INS ELISA Kits) resistance specifically in HFD-fed male mice.
Prkci and its downstream partners direct polarized cell division of luminal myocardial cells to drive trabeculation in the nascent heart.
Prkci regulates expansion of various stem cells via Notch (show NOTCH1 ELISA Kits)-dependent pathway.
PKClambda/iota could be a crucial regulator of mitochondrial function and energy metabolism in stem cells and other cellular contexts
Asymmetric division and CD8+ T lymphocyte fate specification is regulated by protein kinase Czeta and protein kinase Clambda.
adenoviral-mediated supplementation of hepatic PKC-lambda induced a diabetic state in heterozygous PKC-lambda knockout mice.
Data indicate that pseudosubstrate arginine residues are key regulators of atypical protein kinase C (show PRKCZ ELISA Kits)-lambda and atypical protein kinase C-zeta (show PRKCZ ELISA Kits).
Loss of aPKClambda in differentiated neurons disrupts the polarity complex but does not induce obvious neuronal loss or disorientation in mouse brains.
Zebrafish pronephros tubulogenesis and epithelial identity maintenance are reliant on the polarity proteins Prkc iota and zeta.
a loss of zBves affects the proteins involved in the pathway of the PAR (show AFG3L2 ELISA Kits) junctional complex, especially aPKC, and both aPKC and Bves (show BVES ELISA Kits) are indispensable to claudin expression.
Heart and soul/PRKCi and nagie oko/Mpp5 (show MPP5 ELISA Kits) regulate myocardial coherence and remodeling during cardiac morphogenesis (show XIRP1 ELISA Kits).
PrkCi function and planar divisions are necessary for asymmetric, self-renewing division of spinal cord precursors.
These data identify atypical PKC isozymes as STAT and ERK activators that mediate c-fos and collagenase expression.
This gene encodes a member of the protein kinase C (PKC) family of serine/threonine protein kinases. The PKC family comprises at least eight members, which are differentially expressed and are involved in a wide variety of cellular processes. This protein kinase is calcium-independent and phospholipid-dependent. It is not activated by phorbolesters or diacylglycerol. This kinase can be recruited to vesicle tubular clusters (VTCs) by direct interaction with the small GTPase RAB2, where this kinase phosphorylates glyceraldehyde-3-phosphate dehydrogenase (GAPD/GAPDH) and plays a role in microtubule dynamics in the early secretory pathway. This kinase is found to be necessary for BCL-ABL-mediated resistance to drug-induced apoptosis and therefore protects leukemia cells against drug-induced apoptosis. There is a single exon pseudogene mapped on chromosome X.
protein kinase C, iota
, protein kinase C iota
, protein kinase C iota type
, 17 kDa inhibitor of protein kinase C
, adenosine 5'-monophosphoramidase
, histidine triad nucleotide-binding protein 1
, protein kinase C inhibitor 1
, protein kinase C-interacting protein 1
, atypical protein kinase C-lambda/iota
, protein kinase C, lambda
, heart and soul protein