Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.11.13 (protein kinase C)
 49,245 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The long-term renal epithelial cell line LLC-PK1 expresses at confluence several differentiated characteristics of renal proximal tubule including Na/glucose cotransport and several brush border membrane hydrolases. The differentiation-inducing chemical hexamethylene bisacetamide (HMBA) triggers a dramatic induction of Na+/glucose symport, trehalase and maltase, expressed as an increase in the number of cells in the culture that express the differentiated phenotype. Characteristics of the induction response are reviewed in terms of proposed mechanisms of inducer action. New evidence suggests that in addition to elevation of intracellular Na levels mediated by partial inhibition of the sodium pump, HMBA treatment also alters polyamine levels via effects on ornithine decarboxylase. These responses may be mediated by HMBA effects on protein kinase C activity. The possible role of polyamine fluctuations and DNA demethylation in mediating HMBA effects on differentiated gene expression is currently being investigated.
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PMID:Chemical inducers of differentiation in a long-term renal cell line. 264 78

Addition of glucose to cells of the yeast Saccharomyces cerevisiae causes rapid activation of plasma membrane H(+)-ATPase and a stimulation of cellular H+ extrusion. We show that addition of diacylglycerol and other activators of protein kinase C to intact cells also activates the H(+)-ATPase and causes at the same time a stimulation of H+ extrusion from the cells. Both effects are reversed by addition of staurosporine, a protein kinase C inhibitor. Addition of staurosporine or calmidazolium, an inhibitor of Ca2+/calmodulin-dependent protein kinases, separately, causes a partial inhibition of glucose-induced H(+)-ATPase activation and stimulation of cellular H+ extrusion; together they cause a more potent inhibition. Addition of neomycin, which complexes with phosphatidylinositol 4,5-bisphosphate, or addition of compound 48/80, a phospholipase C inhibitor, also causes near complete inhibition. Diacylglycerol and other protein kinase C activators had no effect on the activity of the K(+)-uptake system and the activity of trehalase and glucose-induced activation of the K(+)-uptake system and trehalase was not inhibited by neomycin, supporting the specificity of the effects observed on the H(+)-ATPase. The results support a model in which glucose-induced activation of H(+)-ATPase is mediated by a phosphatidylinositol-type signaling pathway triggering phosphorylation of the enzyme both by protein kinase C and one or more Ca2+/calmodulin-dependent protein kinases.
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PMID:Possible involvement of a phosphatidylinositol-type signaling pathway in glucose-induced activation of plasma membrane H(+)-ATPase and cellular proton extrusion in the yeast Saccharomyces cerevisiae. 806 Oct 44