High impact information on PRKCA

• High glucose concentrations increase endothelial cell permeability via activation of protein kinase C alpha [1].
• Histamine-induced vasoconstriction involves phosphorylation of a specific inhibitor protein for myosin phosphatase by protein kinase C alpha and delta isoforms [2].
• Protein kinase C-alpha activity modulates transepithelial permeability and cell junctions in the LLC-PK1 epithelial cell line [3].
• Acute exposure of control cell sheets to TPA induces activation, translocation, and down-regulation of protein kinase C-alpha (PKC-alpha) [4].
• Chronic exposure of LLC-PK1 epithelia to the phorbol ester TPA produces polyp-like foci with leaky tight junctions and altered protein kinase C-alpha expression and localization [4].

Biological context of PRKCA

• Replacement of Ser657 of protein kinase C-alpha by alanine leads to premature down regulation after phorbol-ester-induced translocation to the membrane [5].
• Phorbol-ester-activated protein kinase C-alpha lacking phosphorylation at Ser657 is down-regulated by a mechanism involving dephosphorylation [6].
• These results suggest that the signal transduction pathway of vasopressin in LLC-PK1 cells does not involve PKC alpha activation and translocation [7].
• Recovery of barrier function in portions of chronically TPA-treated cultures does not correlate with up-regulation of PKC-alpha nor translocation back to the cytosolic compartment [4].
• These results indicate that PMN from hyperlipidemic animals is associated with an accelerated respiratory burst of ROS by increasing the expression of PKC alpha, betaI and gp91phox, and pitavastatin inhibits this by suppressing the expression of those proteins [8].

Anatomical context of PRKCA

• Protein kinase C-alpha attenuates cholinergically stimulated gastric acid secretion of rabbit parietal cells [9].

Associations of PRKCA with chemical compounds

• Selective and transient activation of protein kinase C alpha by fumonisin B1, a ceramide synthase inhibitor mycotoxin, in cultured porcine renal cells [10].
• Vasopressin (100 mU/ml) failed to induce a translocation of PKC alpha from the C to the PM [7].
• In chronically TPA-treated and clone PLF-A cells, total PKC-alpha levels are reduced even further and almost all remaining PKC-alpha is found in the membrane-associated and Triton-insoluble fractions [4].
• When the phase diagram was elaborated in the presence of Ca2+ and Mg2+, at concentrations similar to those used in the PKC alpha activity assay, the boundaries between the regions changed slightly and C1 had 35 mol% 1,2-DMG [11].
• PKC alpha was better preserved from thermal denaturation in the presence of Ca(2+), the aggregated beta-sheet at 1618 cm(-1) decreasing from 19% in the absence of this ligand to 13% in its presence [12].

Other interactions of PRKCA

• By contrast, phorbol myristate acetate (PMA, 200 nM), a potent activator of PKC, induced a relocalization of PKC alpha from the C to the PM [7].
• In the presence of Ca2+ and Mg2+, maximum PKC alpha activity occurred at concentrations of 1,2-DMG that were close to the boundary in the phase diagram between region 1, where compound C1 and the pure phospholipid coexisted in the gel phase, and region 2, where compounds C1 and C2 coexisted [11].

Analytical, diagnostic and therapeutic context of PRKCA

• In LLC-PK1 cells, the redistribution of PKC alpha, a predominant isoform of PKC detected, was studied utilizing western blotting after stimulation with vasopressin [7].
• Immunofluorescence shows that PKC-alpha expression is restricted to the PLFs in chronically TPA-treated cells and is more homogeneously distributed in clone PLF-A cultures [4].

References