Down-regulation of protein kinase C and of an endogenous 80-kDa substrate in transformed fibroblasts.
about
Expression of a protein tyrosine phosphatase in normal and v-src-transformed mouse 3T3 fibroblasts.Brain protein kinase C phosphorylating poly(arginine,serine) or lamin B is stimulated by anions and by an activator purified from bovine serum albumin preparations.Decreased susceptibility of a 70-kDa protein to cathepsin L after phosphorylation by protein kinase C.Evidence that v-src and v-fps gene products use a protein kinase C-mediated pathway to induce expression of a transformation-related geneTransformation stimulates glucose transporter gene expression in the absence of protein kinase CActivation of YRP kinase by v-Src and protein kinase C-mediated signal transduction pathwaysProtein kinase C activation potently down-regulates the expression of its major substrate, 80K, in Swiss 3T3 cells.Dissociation of inositol trisphosphate from diacylglycerol production in Rous sarcoma virus-transformed fibroblastsThe mitogenic signaling pathway but not the plasminogen activator-inducing pathway of basic fibroblast growth factor is mediated through protein kinase C in fetal bovine aortic endothelial cells.Evidence that v-Src-induced phospholipase D activity is mediated by a G protein.Abnormal protein kinase C down regulation and reduced substrate levels in non-phorbol ester-responsive 3T3-TNR9 cells.v-Src increases diacylglycerol levels via a type D phospholipase-mediated hydrolysis of phosphatidylcholine.Elevated phosphocholine concentration in ras-transformed NIH 3T3 cells arises from increased choline kinase activity, not from phosphatidylcholine breakdownThe v-src inducible gene 9E3/pCEF4 is regulated by both its promoter upstream sequence and its 3' untranslated region.Loss of responsiveness of an AP1-related factor, PEBP1, to 12-O-tetradecanoylphorbol-13-acetate after transformation of NIH 3T3 cells by the Ha-ras oncogene.Evidence for a role of phosphatidylcholine-hydrolysing phospholipase C in the regulation of protein kinase C by ras and src oncogenes.p21ras and protein kinase C function in distinct and interdependent signaling pathways in C3H 10T1/2 fibroblasts.Protein turnover in 3T3 cells transformed with the oncogene c-H-ras1.Phorbol ester and bryostatin differentially regulate the hydrolysis of phosphatidylethanolamine in Ha-ras- and raf-oncogene-transformed NIH 3T3 cells.Transformation-specific decrease of phosphorylation of 80K protein, a substrate of protein kinase C, in NIH3T3 cells.Transfection of insulin-producing cells with a transforming c-Ha-ras oncogene stimulates phospholipase C activity.Scrape-loaded p21ras down-regulates agonist-stimulated inositol phosphate production by a mechanism involving protein kinase C.v-Src activates a unique phospholipase D activity that can be distinguished from the phospholipase D activity activated by phorbol esters
P2860
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P2860
Down-regulation of protein kinase C and of an endogenous 80-kDa substrate in transformed fibroblasts.
description
1987 nî lūn-bûn
@nan
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
1987年论文
@zh
1987年论文
@zh-cn
name
Down-regulation of protein kin ...... te in transformed fibroblasts.
@en
Down-regulation of protein kin ...... te in transformed fibroblasts.
@nl
type
label
Down-regulation of protein kin ...... te in transformed fibroblasts.
@en
Down-regulation of protein kin ...... te in transformed fibroblasts.
@nl
prefLabel
Down-regulation of protein kin ...... te in transformed fibroblasts.
@en
Down-regulation of protein kin ...... te in transformed fibroblasts.
@nl
P2093
P1476
Down-regulation of protein kin ...... ate in transformed fibroblasts
@en
P2093
Blackshear PJ
Wingrove TG
P304
16546-16552
P407
P577
1987-12-01T00:00:00Z