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Prkcd  -  protein kinase C, delta

Rattus norvegicus

Synonyms: Pkcd, Protein kinase C delta type, nPKC-delta
 
 
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Disease relevance of Prkcd

  • The expression and subcellular distribution of liver cPKC alpha and beta, nPKC delta and aPKC zeta isoenzymes and the plasma levels of fibrinogen were measured in young, 2- and 6-month-old, and aged, 24-month-old, normal and turpentine-treated rats, to induce an aseptic inflammatory condition and the acute-phase response [1].
 

High impact information on Prkcd

 

Biological context of Prkcd

  • Furthermore, we demonstrated that overproduction of an exogenous cPKC beta I isoform in these cells (R6-PKC3) altered the TPA-induced down-regulation of nPKC delta and nPKC epsilon [4].
  • In contrast to TPA response element (TRE), where overexpression of a variety of PKC isozymes results in enhanced activation by TPA, activation of NF-kappa B by TPA is not enhanced by overexpression of PKC isozymes such as cPKC alpha, nPKC delta, or nPKC theta [5].
 

Associations of Prkcd with chemical compounds

  • By contrast, the activity of cPKC-gamma was unaffected by Ca(2+), as were the activities of nPKC-delta and -epsilon and aPKC-zeta, as expected [6].
 

Regulatory relationships of Prkcd

 

Other interactions of Prkcd

  • EC50 values for the translocation of nPKC-delta and nPKC-epsilon by BK(1-8) were more than 5 microM [7].
  • BK or kallidin stimulated the rapid (less than 30 s) translocation of more than 80% of the novel protein kinase C (PKC) isoforms nPKC-delta and nPKC-epsilon from the soluble to the particulate fraction [7].
 

Analytical, diagnostic and therapeutic context of Prkcd

  • Western blot analysis indicated that growth to confluent density significantly increased the protein levels of cPKC-alpha (11.6-fold), nPKC-delta (5.3-fold), and nPKC-epsilon (22.0-fold) but not aPKC-zeta [8].
  • The activity of this enzyme was specifically reduced by immunoprecipitation, depending on the concentration of the polyclonal antibody, PC-delta, which was raised against a peptide synthesized according to a sequence of rat brain nPKC delta [9].

References

  1. c-PKC-dependent modulation of plasma fibrinogen levels during the acute-phase response in young and old rats. La Porta, C.A., Franchi, C., Comolli, R. Mech. Ageing Dev. (1998) [Pubmed]
  2. Activation of novel protein kinases C delta and C epsilon upon mitogenic stimulation of quiescent rat 3Y1 fibroblasts. Ohno, S., Mizuno, K., Adachi, Y., Hata, A., Akita, Y., Akimoto, K., Osada, S., Hirai, S., Suzuki, K. J. Biol. Chem. (1994) [Pubmed]
  3. Expression of four protein kinase C isoforms in rat fibroblasts. Distinct subcellular distribution and regulation by calcium and phorbol esters. Borner, C., Guadagno, S.N., Fabbro, D., Weinstein, I.B. J. Biol. Chem. (1992) [Pubmed]
  4. Expression of four protein kinase C isoforms in rat fibroblasts. Differential alterations in ras-, src-, and fos-transformed cells. Borner, C., Guadagno, S.N., Hsiao, W.W., Fabbro, D., Barr, M., Weinstein, I.B. J. Biol. Chem. (1992) [Pubmed]
  5. A protein kinase C isozyme, nPKC epsilon, is involved in the activation of NF-kappa B by 12-O-tetradecanoylphorbol-13-acetate (TPA) in rat 3Y1 fibroblasts. Hirano, M., Hirai, S., Mizuno, K., Osada, S., Hosaka, M., Ohno, S. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
  6. Interaction of protein kinase C with filamentous actin: isozyme specificity resulting from divergent phorbol ester and calcium dependencies. Slater, S.J., Milano, S.K., Stagliano, B.A., Gergich, K.J., Curry, J.P., Taddeo, F.J., Stubbs, C.D. Biochemistry (2000) [Pubmed]
  7. Stimulation of phosphatidylinositol hydrolysis, protein kinase C translocation, and mitogen-activated protein kinase activity by bradykinin in rat ventricular myocytes: dissociation from the hypertrophic response. Clerk, A., Gillespie-Brown, J., Fuller, S.J., Sugden, P.H. Biochem. J. (1996) [Pubmed]
  8. Regulation of expression and activity of four PKC isozymes in confluent and mechanically stimulated UMR-108 osteoblastic cells. Geng, W.D., Boskovic, G., Fultz, M.E., Li, C., Niles, R.M., Ohno, S., Wright, G.L. J. Cell. Physiol. (2001) [Pubmed]
  9. Ca(2+)-independent, phospholipid-activated protein kinase in 3Y1 cells. Uchida, C., Hagiwara, M., Hidaka, H. Arch. Biochem. Biophys. (1991) [Pubmed]
 
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