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PRKCA  -  protein kinase C, alpha

Sus scrofa

 
 
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High impact information on PRKCA

 

Biological context of PRKCA

 

Anatomical context of PRKCA

 

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

References

  1. High glucose concentrations increase endothelial cell permeability via activation of protein kinase C alpha. Hempel, A., Maasch, C., Heintze, U., Lindschau, C., Dietz, R., Luft, F.C., Haller, H. Circ. Res. (1997) [Pubmed]
  2. Histamine-induced vasoconstriction involves phosphorylation of a specific inhibitor protein for myosin phosphatase by protein kinase C alpha and delta isoforms. Eto, M., Kitazawa, T., Yazawa, M., Mukai, H., Ono, Y., Brautigan, D.L. J. Biol. Chem. (2001) [Pubmed]
  3. Protein kinase C-alpha activity modulates transepithelial permeability and cell junctions in the LLC-PK1 epithelial cell line. Rosson, D., O'Brien, T.G., Kampherstein, J.A., Szallasi, Z., Bogi, K., Blumberg, P.M., Mullin, J.M. J. Biol. Chem. (1997) [Pubmed]
  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. Mullin, J.M., Soler, A.P., Laughlin, K.V., Kampherstein, J.A., Russo, L.M., Saladik, D.T., George, K., Shurina, R.D., O'Brien, T.G. Exp. Cell Res. (1996) [Pubmed]
  5. Replacement of Ser657 of protein kinase C-alpha by alanine leads to premature down regulation after phorbol-ester-induced translocation to the membrane. Gysin, S., Imber, R. Eur. J. Biochem. (1996) [Pubmed]
  6. Phorbol-ester-activated protein kinase C-alpha lacking phosphorylation at Ser657 is down-regulated by a mechanism involving dephosphorylation. Gysin, S., Imber, R. Eur. J. Biochem. (1997) [Pubmed]
  7. Is protein kinase C alpha (PKC alpha) involved in vasopressin-induced effects on LLC-PK1 pig kidney cells? Dibas, A., Mia, A.J., Yorio, T. Biochem. Mol. Biol. Int. (1996) [Pubmed]
  8. Enhanced oxidative stress in neutrophils from hyperlipidemic guinea pig. Maeda, K., Yasunari, K., Sato, E.F., Inoue, M. Atherosclerosis (2005) [Pubmed]
  9. Protein kinase C-alpha attenuates cholinergically stimulated gastric acid secretion of rabbit parietal cells. Fährmann, M., Kaufhold, M., Pfeiffer, A.F., Seidler, U. Br. J. Pharmacol. (2003) [Pubmed]
  10. Selective and transient activation of protein kinase C alpha by fumonisin B1, a ceramide synthase inhibitor mycotoxin, in cultured porcine renal cells. Gopee, N.V., Sharma, R.P. Life Sci. (2004) [Pubmed]
  11. Correlation between protein kinase C alpha activity and membrane phase behavior. Micol, V., Sánchez-Piñera, P., Villalaín, J., de Godos, A., Gómez-Fernández, J.C. Biophys. J. (1999) [Pubmed]
  12. An infrared spectroscopic study of the secondary structure of protein kinase C alpha and its thermal denaturation. Torrecillas, A., Corbalán-García, S., Gómez-Fernández, J.C. Biochemistry (2004) [Pubmed]
 
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