Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1993 Apr 15;291(Pt 2):329–343. doi: 10.1042/bj2910329

Protein kinase C isoenzymes: divergence in signal transduction?

H Hug 1, T F Sarre 1
PMCID: PMC1132529  PMID: 8484714

Full text

PDF

Images in this article

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ahmed S., Kozma R., Monfries C., Hall C., Lim H. H., Smith P., Lim L. Human brain n-chimaerin cDNA encodes a novel phorbol ester receptor. Biochem J. 1990 Dec 15;272(3):767–773. doi: 10.1042/bj2720767. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Aihara H., Asaoka Y., Yoshida K., Nishizuka Y. Sustained activation of protein kinase C is essential to HL-60 cell differentiation to macrophage. Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11062–11066. doi: 10.1073/pnas.88.24.11062. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Akita Y., Ohno S., Yajima Y., Suzuki K. Possible role of Ca2(+)-independent protein kinase C isozyme, nPKC epsilon, in thyrotropin-releasing hormone-stimulated signal transduction: differential down-regulation of nPKC epsilon in GH4C1 cells. Biochem Biophys Res Commun. 1990 Oct 15;172(1):184–189. doi: 10.1016/s0006-291x(05)80191-3. [DOI] [PubMed] [Google Scholar]
  4. Azzi A., Boscoboinik D., Hensey C. The protein kinase C family. Eur J Biochem. 1992 Sep 15;208(3):547–557. doi: 10.1111/j.1432-1033.1992.tb17219.x. [DOI] [PubMed] [Google Scholar]
  5. Bacher N., Zisman Y., Berent E., Livneh E. Isolation and characterization of PKC-L, a new member of the protein kinase C-related gene family specifically expressed in lung, skin, and heart. Mol Cell Biol. 1991 Jan;11(1):126–133. doi: 10.1128/mcb.11.1.126. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Bacher N., Zisman Y., Berent E., Livneh E. Isolation and characterization of PKC-L, a new member of the protein kinase C-related gene family specifically expressed in lung, skin, and heart. Mol Cell Biol. 1992 Mar;12(3):1404–1404. doi: 10.1128/mcb.12.3.1404-a. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Bader M., Sarre T. F. A (re)initiation-dependent cell-free protein-synthesis system from mouse erythroleukemia cells. Eur J Biochem. 1986 Nov 17;161(1):103–109. doi: 10.1111/j.1432-1033.1986.tb10129.x. [DOI] [PubMed] [Google Scholar]
  8. Bazzi M. D., Nelsestuen G. L. Constitutive activity of membrane-inserted protein kinase C. Biochem Biophys Res Commun. 1988 Apr 15;152(1):336–343. doi: 10.1016/s0006-291x(88)80719-8. [DOI] [PubMed] [Google Scholar]
  9. Bazzi M. D., Nelsestuen G. L. Role of substrate in imparting calcium and phospholipid requirements to protein kinase C activation. Biochemistry. 1987 Apr 7;26(7):1974–1982. doi: 10.1021/bi00381a029. [DOI] [PubMed] [Google Scholar]
  10. Bell R. M., Burns D. J. Lipid activation of protein kinase C. J Biol Chem. 1991 Mar 15;266(8):4661–4664. [PubMed] [Google Scholar]
  11. Bellacosa A., Testa J. R., Staal S. P., Tsichlis P. N. A retroviral oncogene, akt, encoding a serine-threonine kinase containing an SH2-like region. Science. 1991 Oct 11;254(5029):274–277. doi: 10.1126/science.254.5029.274. [DOI] [PubMed] [Google Scholar]
  12. Bernards R. N-myc disrupts protein kinase C-mediated signal transduction in neuroblastoma. EMBO J. 1991 May;10(5):1119–1125. doi: 10.1002/j.1460-2075.1991.tb08052.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Berridge M. J. Inositol trisphosphate and diacylglycerol: two interacting second messengers. Annu Rev Biochem. 1987;56:159–193. doi: 10.1146/annurev.bi.56.070187.001111. [DOI] [PubMed] [Google Scholar]
  14. Berridge M. J., Irvine R. F. Inositol phosphates and cell signalling. Nature. 1989 Sep 21;341(6239):197–205. doi: 10.1038/341197a0. [DOI] [PubMed] [Google Scholar]
  15. Berry N., Ase K., Kishimoto A., Nishizuka Y. Activation of resting human T cells requires prolonged stimulation of protein kinase C. Proc Natl Acad Sci U S A. 1990 Mar;87(6):2294–2298. doi: 10.1073/pnas.87.6.2294. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Berry N., Nishizuka Y. Protein kinase C and T cell activation. Eur J Biochem. 1990 Apr 30;189(2):205–214. doi: 10.1111/j.1432-1033.1990.tb15478.x. [DOI] [PubMed] [Google Scholar]
  17. Borner C., Filipuzzi I., Wartmann M., Eppenberger U., Fabbro D. Biosynthesis and posttranslational modifications of protein kinase C in human breast cancer cells. J Biol Chem. 1989 Aug 15;264(23):13902–13909. [PubMed] [Google Scholar]
  18. Borner C., Filipuzzi I., Weinstein I. B., Imber R. Failure of wild-type or a mutant form of protein kinase C-alpha to transform fibroblasts. Nature. 1991 Sep 5;353(6339):78–80. doi: 10.1038/353078a0. [DOI] [PubMed] [Google Scholar]
  19. Borner C., Guadagno S. N., Fabbro D., Weinstein I. B. Expression of four protein kinase C isoforms in rat fibroblasts. Distinct subcellular distribution and regulation by calcium and phorbol esters. J Biol Chem. 1992 Jun 25;267(18):12892–12899. [PubMed] [Google Scholar]
  20. Bruder J. T., Heidecker G., Rapp U. R. Serum-, TPA-, and Ras-induced expression from Ap-1/Ets-driven promoters requires Raf-1 kinase. Genes Dev. 1992 Apr;6(4):545–556. doi: 10.1101/gad.6.4.545. [DOI] [PubMed] [Google Scholar]
  21. Burns D. J., Bell R. M. Protein kinase C contains two phorbol ester binding domains. J Biol Chem. 1991 Sep 25;266(27):18330–18338. [PubMed] [Google Scholar]
  22. Burns D. J., Bloomenthal J., Lee M. H., Bell R. M. Expression of the alpha, beta II, and gamma protein kinase C isozymes in the baculovirus-insect cell expression system. Purification and characterization of the individual isoforms. J Biol Chem. 1990 Jul 15;265(20):12044–12051. [PubMed] [Google Scholar]
  23. Castagna M., Takai Y., Kaibuchi K., Sano K., Kikkawa U., Nishizuka Y. Direct activation of calcium-activated, phospholipid-dependent protein kinase by tumor-promoting phorbol esters. J Biol Chem. 1982 Jul 10;257(13):7847–7851. [PubMed] [Google Scholar]
  24. Cataldi A., Miscia S., Lisio R., Rana R., Cocco L. Transient shift of diacylglycerol and inositol lipids induced by interferon in Daudi cells. Evidence for a different pattern between nuclei and intact cells. FEBS Lett. 1990 Sep 3;269(2):465–468. doi: 10.1016/0014-5793(90)81216-b. [DOI] [PubMed] [Google Scholar]
  25. Chauhan A., Chauhan V. P., Brockerhoff H. Activation of protein kinase C by phosphatidylinositol 4,5-bisphosphate: possible involvement in Na+/H+ antiport down-regulation and cell proliferation. Biochem Biophys Res Commun. 1991 Mar 29;175(3):852–857. doi: 10.1016/0006-291x(91)91643-q. [DOI] [PubMed] [Google Scholar]
  26. Chen K. H., Widen S. G., Wilson S. H., Huang K. P. Characterization of the 5'-flanking region of the rat protein kinase C gamma gene. J Biol Chem. 1990 Nov 15;265(32):19961–19965. [PubMed] [Google Scholar]
  27. Choi P. M., Tchou-Wong K. M., Weinstein I. B. Overexpression of protein kinase C in HT29 colon cancer cells causes growth inhibition and tumor suppression. Mol Cell Biol. 1990 Sep;10(9):4650–4657. doi: 10.1128/mcb.10.9.4650. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Clark J. D., Lin L. L., Kriz R. W., Ramesha C. S., Sultzman L. A., Lin A. Y., Milona N., Knopf J. L. A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-dependent translocation domain with homology to PKC and GAP. Cell. 1991 Jun 14;65(6):1043–1051. doi: 10.1016/0092-8674(91)90556-e. [DOI] [PubMed] [Google Scholar]
  29. Clemens M. J., Trayner I., Menaya J. The role of protein kinase C isoenzymes in the regulation of cell proliferation and differentiation. J Cell Sci. 1992 Dec;103(Pt 4):881–887. doi: 10.1242/jcs.103.4.881. [DOI] [PubMed] [Google Scholar]
  30. Cook P. P., Chen J., Ways D. K. Interleukin-3 induces translocation and down-regulation of protein kinase C in human platelets. Biochem Biophys Res Commun. 1992 Jun 15;185(2):670–675. doi: 10.1016/0006-291x(92)91677-i. [DOI] [PubMed] [Google Scholar]
  31. Coussens L., Parker P. J., Rhee L., Yang-Feng T. L., Chen E., Waterfield M. D., Francke U., Ullrich A. Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signaling pathways. Science. 1986 Aug 22;233(4766):859–866. doi: 10.1126/science.3755548. [DOI] [PubMed] [Google Scholar]
  32. Coussens L., Rhee L., Parker P. J., Ullrich A. Alternative splicing increases the diversity of the human protein kinase C family. DNA. 1987 Oct;6(5):389–394. doi: 10.1089/dna.1987.6.389. [DOI] [PubMed] [Google Scholar]
  33. Crabos M., Imber R., Woodtli T., Fabbro D., Erne P. Different translocation of three distinct PKC isoforms with tumor-promoting phorbol ester in human platelets. Biochem Biophys Res Commun. 1991 Aug 15;178(3):878–883. doi: 10.1016/0006-291x(91)90973-b. [DOI] [PubMed] [Google Scholar]
  34. Cuadrado A., Molloy C. J., Pech M. Expression of protein kinase CI in NIH 3T3 cells increases its growth response to specific activators. FEBS Lett. 1990 Jan 29;260(2):281–284. doi: 10.1016/0014-5793(90)80123-z. [DOI] [PubMed] [Google Scholar]
  35. Danish R., el-Awar O., Weber B. L., Langmore J., Turka L. A., Ryan J. J., Clarke M. F. c-myb effects on kinetic events during MEL cell differentiation. Oncogene. 1992 May;7(5):901–907. [PubMed] [Google Scholar]
  36. De Benedetti A., Joshi-Barve S., Rinker-Schaeffer C., Rhoads R. E. Expression of antisense RNA against initiation factor eIF-4E mRNA in HeLa cells results in lengthened cell division times, diminished translation rates, and reduced levels of both eIF-4E and the p220 component of eIF-4F. Mol Cell Biol. 1991 Nov;11(11):5435–5445. doi: 10.1128/mcb.11.11.5435. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Dekker L. V., Parker P. J., McIntyre P. Biochemical properties of rat protein kinase C-eta expressed in COS cells. FEBS Lett. 1992 Nov 9;312(2-3):195–199. doi: 10.1016/0014-5793(92)80934-9. [DOI] [PubMed] [Google Scholar]
  38. Dietrich A., Rose-John S., Marks F. Expression of the kinase domain of mouse protein kinase C in E. coli. Biochem Int. 1989 Jul;19(1):163–172. [PubMed] [Google Scholar]
  39. Divecha N., Banfić H., Irvine R. F. The polyphosphoinositide cycle exists in the nuclei of Swiss 3T3 cells under the control of a receptor (for IGF-I) in the plasma membrane, and stimulation of the cycle increases nuclear diacylglycerol and apparently induces translocation of protein kinase C to the nucleus. EMBO J. 1991 Nov;10(11):3207–3214. doi: 10.1002/j.1460-2075.1991.tb04883.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Downward J., Graves J. D., Warne P. H., Rayter S., Cantrell D. A. Stimulation of p21ras upon T-cell activation. Nature. 1990 Aug 23;346(6286):719–723. doi: 10.1038/346719a0. [DOI] [PubMed] [Google Scholar]
  41. Duronio V., Nip L., Pelech S. L. Interleukin 3 stimulates phosphatidylcholine turnover in a mast/megakaryocyte cell line. Biochem Biophys Res Commun. 1989 Oct 31;164(2):804–808. doi: 10.1016/0006-291x(89)91530-1. [DOI] [PubMed] [Google Scholar]
  42. Duyster J., Hidaka H., Decker K., Dieter P. Proteinkinase C beta-isoform triggers the formation of prostanoids and superoxide in liver macrophages. Biochem Biophys Res Commun. 1992 Mar 31;183(3):1247–1253. doi: 10.1016/s0006-291x(05)80324-9. [DOI] [PubMed] [Google Scholar]
  43. Eichholtz T., Alblas J., van Overveld M., Moolenaar W., Ploegh H. A pseudosubstrate peptide inhibits protein kinase C-mediated phosphorylation in permeabilized Rat-1 cells. FEBS Lett. 1990 Feb 12;261(1):147–150. doi: 10.1016/0014-5793(90)80657-5. [DOI] [PubMed] [Google Scholar]
  44. Eldar H., Zisman Y., Ullrich A., Livneh E. Overexpression of protein kinase C alpha-subtype in Swiss/3T3 fibroblasts causes loss of both high and low affinity receptor numbers for epidermal growth factor. J Biol Chem. 1990 Aug 5;265(22):13290–13296. [PubMed] [Google Scholar]
  45. Farese R. V., Standaert M. L., Cooper D. R. Protein kinase C downregulation? Nature. 1992 Nov 26;360(6402):305–305. doi: 10.1038/360305c0. [DOI] [PubMed] [Google Scholar]
  46. Fiebich B., Hug H., Marmé D. High-efficiency expression of rat protein kinase C-gamma in baculovirus-infected insect cells. FEBS Lett. 1990 Dec 17;277(1-2):15–18. doi: 10.1016/0014-5793(90)80798-n. [DOI] [PubMed] [Google Scholar]
  47. Fields A. P., Pettit G. R., May W. S. Phosphorylation of lamin B at the nuclear membrane by activated protein kinase C. J Biol Chem. 1988 Jun 15;263(17):8253–8260. [PubMed] [Google Scholar]
  48. Finkenzeller G., Marmé D., Hug H. Inducible overexpression of human protein kinase C alpha in NIH 3T3 fibroblasts results in growth abnormalities. Cell Signal. 1992 Mar;4(2):163–177. doi: 10.1016/0898-6568(92)90080-r. [DOI] [PubMed] [Google Scholar]
  49. Finkenzeller G., Marmé D., Hug H. Sequence of human protein kinase C alpha. Nucleic Acids Res. 1990 Apr 25;18(8):2183–2183. doi: 10.1093/nar/18.8.2183. [DOI] [PMC free article] [PubMed] [Google Scholar]
  50. Flint A. J., Paladini R. D., Koshland D. E., Jr Autophosphorylation of protein kinase C at three separated regions of its primary sequence. Science. 1990 Jul 27;249(4967):408–411. doi: 10.1126/science.2377895. [DOI] [PubMed] [Google Scholar]
  51. Freisewinkel I., Riethmacher D., Stabel S. Downregulation of protein kinase C-gamma is independent of a functional kinase domain. FEBS Lett. 1991 Mar 25;280(2):262–266. doi: 10.1016/0014-5793(91)80307-o. [DOI] [PubMed] [Google Scholar]
  52. Galabru J., Hovanessian A. Autophosphorylation of the protein kinase dependent on double-stranded RNA. J Biol Chem. 1987 Nov 15;262(32):15538–15544. [PubMed] [Google Scholar]
  53. Geppert M., Archer B. T., 3rd, Südhof T. C. Synaptotagmin II. A novel differentially distributed form of synaptotagmin. J Biol Chem. 1991 Jul 25;266(21):13548–13552. [PubMed] [Google Scholar]
  54. Ghosh S., Baltimore D. Activation in vitro of NF-kappa B by phosphorylation of its inhibitor I kappa B. Nature. 1990 Apr 12;344(6267):678–682. doi: 10.1038/344678a0. [DOI] [PubMed] [Google Scholar]
  55. Grabarek J., Raychowdhury M., Ravid K., Kent K. C., Newman P. J., Ware J. A. Identification and functional characterization of protein kinase C isozymes in platelets and HEL cells. J Biol Chem. 1992 May 15;267(14):10011–10017. [PubMed] [Google Scholar]
  56. Graff J. M., Stumpo D. J., Blackshear P. J. Characterization of the phosphorylation sites in the chicken and bovine myristoylated alanine-rich C kinase substrate protein, a prominent cellular substrate for protein kinase C. J Biol Chem. 1989 Jul 15;264(20):11912–11919. [PubMed] [Google Scholar]
  57. Greif H., Ben-Chaim J., Shimon T., Bechor E., Eldar H., Livneh E. The protein kinase C-related PKC-L(eta) gene product is localized in the cell nucleus. Mol Cell Biol. 1992 Mar;12(3):1304–1311. doi: 10.1128/mcb.12.3.1304. [DOI] [PMC free article] [PubMed] [Google Scholar]
  58. Gschwendt M., Kittstein W., Marks F. Protein kinase C activation by phorbol esters: do cysteine-rich regions and pseudosubstrate motifs play a role? Trends Biochem Sci. 1991 May;16(5):167–169. doi: 10.1016/0968-0004(91)90064-3. [DOI] [PubMed] [Google Scholar]
  59. Hannun Y. A., Loomis C. R., Bell R. M. Activation of protein kinase C by Triton X-100 mixed micelles containing diacylglycerol and phosphatidylserine. J Biol Chem. 1985 Aug 25;260(18):10039–10043. [PubMed] [Google Scholar]
  60. Hartwig J. H., Thelen M., Rosen A., Janmey P. A., Nairn A. C., Aderem A. MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin. Nature. 1992 Apr 16;356(6370):618–622. doi: 10.1038/356618a0. [DOI] [PubMed] [Google Scholar]
  61. Hashimoto K., Kishimoto A., Aihara H., Yasuda I., Mikawa K., Nishizuka Y. Protein kinase C during differentiation of human promyelocytic leukemia cell line, HL-60. FEBS Lett. 1990 Apr 9;263(1):31–34. doi: 10.1016/0014-5793(90)80698-i. [DOI] [PubMed] [Google Scholar]
  62. Hass R., Pfannkuche H. J., Kharbanda S., Gunji H., Meyer G., Hartmann A., Hidaka H., Resch K., Kufe D., Goppelt-Strübe M. Protein kinase C activation and protooncogene expression in differentiation/retrodifferentiation of human U-937 leukemia cells. Cell Growth Differ. 1991 Nov;2(11):541–548. [PubMed] [Google Scholar]
  63. Hershey J. W. Translational control in mammalian cells. Annu Rev Biochem. 1991;60:717–755. doi: 10.1146/annurev.bi.60.070191.003441. [DOI] [PubMed] [Google Scholar]
  64. Hocevar B. A., Fields A. P. Selective translocation of beta II-protein kinase C to the nucleus of human promyelocytic (HL60) leukemia cells. J Biol Chem. 1991 Jan 5;266(1):28–33. [PubMed] [Google Scholar]
  65. Hornbeck P., Huang K. P., Paul W. E. Lamin B is rapidly phosphorylated in lymphocytes after activation of protein kinase C. Proc Natl Acad Sci U S A. 1988 Apr;85(7):2279–2283. doi: 10.1073/pnas.85.7.2279. [DOI] [PMC free article] [PubMed] [Google Scholar]
  66. House C., Kemp B. E. Protein kinase C contains a pseudosubstrate prototope in its regulatory domain. Science. 1987 Dec 18;238(4834):1726–1728. doi: 10.1126/science.3686012. [DOI] [PubMed] [Google Scholar]
  67. House C., Kemp B. E. Protein kinase C pseudosubstrate prototope: structure-function relationships. Cell Signal. 1990;2(2):187–190. doi: 10.1016/0898-6568(90)90022-3. [DOI] [PubMed] [Google Scholar]
  68. House C., Wettenhall R. E., Kemp B. E. The influence of basic residues on the substrate specificity of protein kinase C. J Biol Chem. 1987 Jan 15;262(2):772–777. [PubMed] [Google Scholar]
  69. Housey G. M., Johnson M. D., Hsiao W. L., O'Brian C. A., Murphy J. P., Kirschmeier P., Weinstein I. B. Overproduction of protein kinase C causes disordered growth control in rat fibroblasts. Cell. 1988 Feb 12;52(3):343–354. doi: 10.1016/s0092-8674(88)80027-8. [DOI] [PubMed] [Google Scholar]
  70. Housey G. M., O'Brian C. A., Johnson M. D., Kirschmeier P., Weinstein I. B. Isolation of cDNA clones encoding protein kinase C: evidence for a protein kinase C-related gene family. Proc Natl Acad Sci U S A. 1987 Feb;84(4):1065–1069. doi: 10.1073/pnas.84.4.1065. [DOI] [PMC free article] [PubMed] [Google Scholar]
  71. Hsieh L. L., Hoshina S., Weinstein I. B. Phenotypic effects of overexpression of PKC beta 1 in rat liver epithelial cells. J Cell Biochem. 1989 Dec;41(4):179–188. doi: 10.1002/jcb.240410403. [DOI] [PubMed] [Google Scholar]
  72. Huang C. F., Cabot M. C. Phorbol diesters stimulate the accumulation of phosphatidate, phosphatidylethanol, and diacylglycerol in three cell types. Evidence for the indirect formation of phosphatidylcholine-derived diacylglycerol by a phospholipase D pathway and direct formation of diacylglycerol by a phospholipase C pathway. J Biol Chem. 1990 Sep 5;265(25):14858–14863. [PubMed] [Google Scholar]
  73. Huang F. L., Yoshida Y., Cunha-Melo J. R., Beaven M. A., Huang K. P. Differential down-regulation of protein kinase C isozymes. J Biol Chem. 1989 Mar 5;264(7):4238–4243. [PubMed] [Google Scholar]
  74. Huang K. P., Chan K. F., Singh T. J., Nakabayashi H., Huang F. L. Autophosphorylation of rat brain Ca2+-activated and phospholipid-dependent protein kinase. J Biol Chem. 1986 Sep 15;261(26):12134–12140. [PubMed] [Google Scholar]
  75. Huang K. P., Huang F. L. Conversion of protein kinase C from a Ca2+-dependent to an independent form of phorbol ester-binding protein by digestion with trypsin. Biochem Biophys Res Commun. 1986 Aug 29;139(1):320–326. doi: 10.1016/s0006-291x(86)80116-4. [DOI] [PubMed] [Google Scholar]
  76. Huang K. P., Nakabayashi H., Huang F. L. Isozymic forms of rat brain Ca2+-activated and phospholipid-dependent protein kinase. Proc Natl Acad Sci U S A. 1986 Nov;83(22):8535–8539. doi: 10.1073/pnas.83.22.8535. [DOI] [PMC free article] [PubMed] [Google Scholar]
  77. Hunter T. Cooperation between oncogenes. Cell. 1991 Jan 25;64(2):249–270. doi: 10.1016/0092-8674(91)90637-e. [DOI] [PubMed] [Google Scholar]
  78. Huwiler A., Fabbro D., Pfeilschifter J. Differential recovery of protein kinase C-alpha and -epsilon isozymes after long-term phorbol ester treatment in rat renal mesangial cells. Biochem Biophys Res Commun. 1991 Nov 14;180(3):1422–1428. doi: 10.1016/s0006-291x(05)81355-5. [DOI] [PubMed] [Google Scholar]
  79. Huwiler A., Fabbro D., Stabel S., Pfeilschifter J. Immunocharacterization of delta- and zeta-isoenzymes of protein kinase C in rat renal mesangial cells. FEBS Lett. 1992 Apr 6;300(3):259–262. doi: 10.1016/0014-5793(92)80858-e. [DOI] [PubMed] [Google Scholar]
  80. Jaken S., Kiley S. C. Purification and characterization of three types of protein kinase C from rabbit brain cytosol. Proc Natl Acad Sci U S A. 1987 Jul;84(13):4418–4422. doi: 10.1073/pnas.84.13.4418. [DOI] [PMC free article] [PubMed] [Google Scholar]
  81. Jakes S., Hastings T. G., Reimann E. M., Schlender K. K. Identification of the phosphoserine residue in histone H1 phosphorylated by protein kinase C. FEBS Lett. 1988 Jul 4;234(1):31–34. doi: 10.1016/0014-5793(88)81296-1. [DOI] [PubMed] [Google Scholar]
  82. James G., Olson E. Deletion of the regulatory domain of protein kinase C alpha exposes regions in the hinge and catalytic domains that mediate nuclear targeting. J Cell Biol. 1992 Feb;116(4):863–874. doi: 10.1083/jcb.116.4.863. [DOI] [PMC free article] [PubMed] [Google Scholar]
  83. Jones P. F., Jakubowicz T., Pitossi F. J., Maurer F., Hemmings B. A. Molecular cloning and identification of a serine/threonine protein kinase of the second-messenger subfamily. Proc Natl Acad Sci U S A. 1991 May 15;88(10):4171–4175. doi: 10.1073/pnas.88.10.4171. [DOI] [PMC free article] [PubMed] [Google Scholar]
  84. Kaibuchi K., Miyajima A., Arai K., Matsumoto K. Possible involvement of RAS-encoded proteins in glucose-induced inositolphospholipid turnover in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8172–8176. doi: 10.1073/pnas.83.21.8172. [DOI] [PMC free article] [PubMed] [Google Scholar]
  85. Karin M. Signal transduction from cell surface to nucleus in development and disease. FASEB J. 1992 May;6(8):2581–2590. doi: 10.1096/fasebj.6.8.1317309. [DOI] [PubMed] [Google Scholar]
  86. Kemp B. E., Pearson R. B. Protein kinase recognition sequence motifs. Trends Biochem Sci. 1990 Sep;15(9):342–346. doi: 10.1016/0968-0004(90)90073-k. [DOI] [PubMed] [Google Scholar]
  87. Kikkawa U., Kishimoto A., Nishizuka Y. The protein kinase C family: heterogeneity and its implications. Annu Rev Biochem. 1989;58:31–44. doi: 10.1146/annurev.bi.58.070189.000335. [DOI] [PubMed] [Google Scholar]
  88. Kikkawa U., Nishizuka Y. The role of protein kinase C in transmembrane signalling. Annu Rev Cell Biol. 1986;2:149–178. doi: 10.1146/annurev.cb.02.110186.001053. [DOI] [PubMed] [Google Scholar]
  89. Kiley S., Schaap D., Parker P., Hsieh L. L., Jaken S. Protein kinase C heterogeneity in GH4C1 rat pituitary cells. Characterization of a Ca2(+)-independent phorbol ester receptor. J Biol Chem. 1990 Sep 15;265(26):15704–15712. [PubMed] [Google Scholar]
  90. Kishimoto A., Kajikawa N., Shiota M., Nishizuka Y. Proteolytic activation of calcium-activated, phospholipid-dependent protein kinase by calcium-dependent neutral protease. J Biol Chem. 1983 Jan 25;258(2):1156–1164. [PubMed] [Google Scholar]
  91. Kishimoto A., Mikawa K., Hashimoto K., Yasuda I., Tanaka S., Tominaga M., Kuroda T., Nishizuka Y. Limited proteolysis of protein kinase C subspecies by calcium-dependent neutral protease (calpain). J Biol Chem. 1989 Mar 5;264(7):4088–4092. [PubMed] [Google Scholar]
  92. Kiss Z., Deli E., Kuo J. F. Temporal changes in intracellular distribution of protein kinase C during differentiation of human leukemia HL60 cells induced by phorbol ester. FEBS Lett. 1988 Apr 11;231(1):41–46. doi: 10.1016/0014-5793(88)80698-7. [DOI] [PubMed] [Google Scholar]
  93. Knopf J. L., Lee M. H., Sultzman L. A., Kriz R. W., Loomis C. R., Hewick R. M., Bell R. M. Cloning and expression of multiple protein kinase C cDNAs. Cell. 1986 Aug 15;46(4):491–502. doi: 10.1016/0092-8674(86)90874-3. [DOI] [PubMed] [Google Scholar]
  94. Kochs G., Hummel R., Fiebich B., Sarre T. F., Marmé D., Hug H. Activation of purified human protein kinase C alpha and beta I isoenzymes in vitro by Ca2+, phosphatidylinositol and phosphatidylinositol 4,5-bisphosphate. Biochem J. 1993 Apr 15;291(Pt 2):627–633. doi: 10.1042/bj2910627. [DOI] [PMC free article] [PubMed] [Google Scholar]
  95. Koide H., Ogita K., Kikkawa U., Nishizuka Y. Isolation and characterization of the epsilon subspecies of protein kinase C from rat brain. Proc Natl Acad Sci U S A. 1992 Feb 15;89(4):1149–1153. doi: 10.1073/pnas.89.4.1149. [DOI] [PMC free article] [PubMed] [Google Scholar]
  96. Kolch W., Heidecker G., Lloyd P., Rapp U. R. Raf-1 protein kinase is required for growth of induced NIH/3T3 cells. Nature. 1991 Jan 31;349(6308):426–428. doi: 10.1038/349426a0. [DOI] [PubMed] [Google Scholar]
  97. Krauss R. S., Housey G. M., Johnson M. D., Weinstein I. B. Disturbances in growth control and gene expression in a C3H/10T1/2 cell line that stably overproduces protein kinase C. Oncogene. 1989 Aug;4(8):991–998. [PubMed] [Google Scholar]
  98. Kubo K., Ohno S., Suzuki K. Nucleotide sequence of the 3' portion of a human gene for protein kinase C beta I/beta II. Nucleic Acids Res. 1987 Sep 11;15(17):7179–7180. doi: 10.1093/nar/15.17.7179. [DOI] [PMC free article] [PubMed] [Google Scholar]
  99. Kubo K., Ohno S., Suzuki K. Primary structures of human protein kinase C beta I and beta II differ only in their C-terminal sequences. FEBS Lett. 1987 Oct 19;223(1):138–142. doi: 10.1016/0014-5793(87)80524-0. [DOI] [PubMed] [Google Scholar]
  100. Lazaris-Karatzas A., Montine K. S., Sonenberg N. Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5' cap. Nature. 1990 Jun 7;345(6275):544–547. doi: 10.1038/345544a0. [DOI] [PubMed] [Google Scholar]
  101. Leach K. L., Powers E. A., Ruff V. A., Jaken S., Kaufmann S. Type 3 protein kinase C localization to the nuclear envelope of phorbol ester-treated NIH 3T3 cells. J Cell Biol. 1989 Aug;109(2):685–695. doi: 10.1083/jcb.109.2.685. [DOI] [PMC free article] [PubMed] [Google Scholar]
  102. Lee M. H., Bell R. M. Mechanism of protein kinase C activation by phosphatidylinositol 4,5-bisphosphate. Biochemistry. 1991 Jan 29;30(4):1041–1049. doi: 10.1021/bi00218a023. [DOI] [PubMed] [Google Scholar]
  103. Leibersperger H., Gschwendt M., Marks F. Purification and characterization of a calcium-unresponsive, phorbol ester/phospholipid-activated protein kinase from porcine spleen. J Biol Chem. 1990 Sep 25;265(27):16108–16115. [PubMed] [Google Scholar]
  104. Leli U., Parker P. J., Shea T. B. Intracellular delivery of protein kinase C-alpha or -epsilon isoform-specific antibodies promotes acquisition of a morphologically differentiated phenotype in neuroblastoma cells. FEBS Lett. 1992 Feb 3;297(1-2):91–94. doi: 10.1016/0014-5793(92)80334-d. [DOI] [PubMed] [Google Scholar]
  105. Li P., Wood K., Mamon H., Haser W., Roberts T. Raf-1: a kinase currently without a cause but not lacking in effects. Cell. 1991 Feb 8;64(3):479–482. doi: 10.1016/0092-8674(91)90228-q. [DOI] [PubMed] [Google Scholar]
  106. Lindner D., Gschwendt M., Marks F. Down-regulation of protein kinase C in Swiss 3T3 fibroblasts is independent of its phosphorylating activity. Biochem Biophys Res Commun. 1991 May 15;176(3):1227–1231. doi: 10.1016/0006-291x(91)90416-5. [DOI] [PubMed] [Google Scholar]
  107. Link E., Kerr L. D., Schreck R., Zabel U., Verma I., Baeuerle P. A. Purified I kappa B-beta is inactivated upon dephosphorylation. J Biol Chem. 1992 Jan 5;267(1):239–246. [PubMed] [Google Scholar]
  108. Liyanage M., Frith D., Livneh E., Stabel S. Protein kinase C group B members PKC-delta, -epsilon, -zeta and PKC-L(eta). Comparison of properties of recombinant proteins in vitro and in vivo. Biochem J. 1992 May 1;283(Pt 3):781–787. doi: 10.1042/bj2830781. [DOI] [PMC free article] [PubMed] [Google Scholar]
  109. Locker J., Buzard G. A dictionary of transcription control sequences. DNA Seq. 1990;1(1):3–11. doi: 10.3109/10425179009041342. [DOI] [PubMed] [Google Scholar]
  110. Lucas S., Marais R., Graves J. D., Alexander D., Parker P., Cantrell D. A. Heterogeneity of protein kinase C expression and regulation in T lymphocytes. FEBS Lett. 1990 Jan 15;260(1):53–56. doi: 10.1016/0014-5793(90)80064-p. [DOI] [PubMed] [Google Scholar]
  111. Makowske M., Ballester R., Cayre Y., Rosen O. M. Immunochemical evidence that three protein kinase C isozymes increase in abundance during HL-60 differentiation induced by dimethyl sulfoxide and retinoic acid. J Biol Chem. 1988 Mar 5;263(7):3402–3410. [PubMed] [Google Scholar]
  112. Makowske M., Rosen O. M. Complete activation of protein kinase C by an antipeptide antibody directed against the pseudosubstrate prototope. J Biol Chem. 1989 Sep 25;264(27):16155–16159. [PubMed] [Google Scholar]
  113. Marais R. M., Parker P. J. Purification and characterisation of bovine brain protein kinase C isotypes alpha, beta and gamma. Eur J Biochem. 1989 Jun 1;182(1):129–137. doi: 10.1111/j.1432-1033.1989.tb14809.x. [DOI] [PubMed] [Google Scholar]
  114. McGlynn E., Liebetanz J., Reutener S., Wood J., Lydon N. B., Hofstetter H., Vanek M., Meyer T., Fabbro D. Expression and partial characterization of rat protein kinase C-delta and protein kinase C-zeta in insect cells using recombinant baculovirus. J Cell Biochem. 1992 Jul;49(3):239–250. doi: 10.1002/jcb.240490306. [DOI] [PubMed] [Google Scholar]
  115. Meek D. W., Street A. J. Nuclear protein phosphorylation and growth control. Biochem J. 1992 Oct 1;287(Pt 1):1–15. doi: 10.1042/bj2870001. [DOI] [PMC free article] [PubMed] [Google Scholar]
  116. Megidish T., Mazurek N. A mutant protein kinase C that can transform fibroblasts. Nature. 1989 Dec 14;342(6251):807–811. doi: 10.1038/342807a0. [DOI] [PubMed] [Google Scholar]
  117. Meldrum E., Parker P. J., Carozzi A. The PtdIns-PLC superfamily and signal transduction. Biochim Biophys Acta. 1991 Mar 19;1092(1):49–71. doi: 10.1016/0167-4889(91)90177-y. [DOI] [PubMed] [Google Scholar]
  118. Melloni E., Pontremoli S., Michetti M., Sacco O., Cakiroglu A. G., Jackson J. F., Rifkind R. A., Marks P. A. Protein kinase C activity and hexamethylenebisacetamide-induced erythroleukemia cell differentiation. Proc Natl Acad Sci U S A. 1987 Aug;84(15):5282–5286. doi: 10.1073/pnas.84.15.5282. [DOI] [PMC free article] [PubMed] [Google Scholar]
  119. Melloni E., Pontremoli S., Viotti P. L., Patrone M., Marks P. A., Rifkind R. A. Differential expression of protein kinase C isozymes and erythroleukemia cell differentiation. J Biol Chem. 1989 Nov 5;264(31):18414–18418. [PubMed] [Google Scholar]
  120. Michaeli J., Busquets X., Orlow I., Younes A., Colomer D., Marks P. A., Rifkind R. A., Kolesnick R. N. A rise and fall in 1,2-diacylglycerol content signal hexamethylene bisacetamide-induced erythropoiesis. J Biol Chem. 1992 Nov 25;267(33):23463–23466. [PubMed] [Google Scholar]
  121. Miller S. G., Kennedy M. B. Regulation of brain type II Ca2+/calmodulin-dependent protein kinase by autophosphorylation: a Ca2+-triggered molecular switch. Cell. 1986 Mar 28;44(6):861–870. doi: 10.1016/0092-8674(86)90008-5. [DOI] [PubMed] [Google Scholar]
  122. Mischak H., Bodenteich A., Kolch W., Goodnight J., Hofer F., Mushinski J. F. Mouse protein kinase C-delta, the major isoform expressed in mouse hemopoietic cells: sequence of the cDNA, expression patterns, and characterization of the protein. Biochemistry. 1991 Aug 13;30(32):7925–7931. doi: 10.1021/bi00246a008. [DOI] [PubMed] [Google Scholar]
  123. Mischak H., Kolch W., Goodnight J., Davidson W. F., Rapp U., Rose-John S., Mushinski J. F. Expression of protein kinase C genes in hemopoietic cells is cell-type- and B cell-differentiation stage specific. J Immunol. 1991 Dec 1;147(11):3981–3987. [PubMed] [Google Scholar]
  124. Mitchell F. E., Marais R. M., Parker P. J. The phosphorylation of protein kinase C as a potential measure of activation. Biochem J. 1989 Jul 1;261(1):131–136. doi: 10.1042/bj2610131. [DOI] [PMC free article] [PubMed] [Google Scholar]
  125. Mizuno K., Kubo K., Saido T. C., Akita Y., Osada S., Kuroki T., Ohno S., Suzuki K. Structure and properties of a ubiquitously expressed protein kinase C, nPKC delta. Eur J Biochem. 1991 Dec 18;202(3):931–940. doi: 10.1111/j.1432-1033.1991.tb16453.x. [DOI] [PubMed] [Google Scholar]
  126. Mochly-Rosen D., Khaner H., Lopez J. Identification of intracellular receptor proteins for activated protein kinase C. Proc Natl Acad Sci U S A. 1991 May 1;88(9):3997–4000. doi: 10.1073/pnas.88.9.3997. [DOI] [PMC free article] [PubMed] [Google Scholar]
  127. Mochly-Rosen D., Koshland D. E., Jr Domain structure and phosphorylation of protein kinase C. J Biol Chem. 1987 Feb 15;262(5):2291–2297. [PubMed] [Google Scholar]
  128. Molina C. A., Ashendel C. L. Tumor promoter 12-O-tetradecanoylphorbol-13-acetate and sn-1,2-dioctanoylglycerol increase the phosphorylation of protein kinase C in cells. Cancer Res. 1991 Sep 1;51(17):4624–4630. [PubMed] [Google Scholar]
  129. Morley S. J., Dever T. E., Etchison D., Traugh J. A. Phosphorylation of eIF-4F by protein kinase C or multipotential S6 kinase stimulates protein synthesis at initiation. J Biol Chem. 1991 Mar 15;266(8):4669–4672. [PubMed] [Google Scholar]
  130. Morley S. J., Traugh J. A. Differential stimulation of phosphorylation of initiation factors eIF-4F, eIF-4B, eIF-3, and ribosomal protein S6 by insulin and phorbol esters. J Biol Chem. 1990 Jun 25;265(18):10611–10616. [PubMed] [Google Scholar]
  131. Morrison D. K., Kaplan D. R., Escobedo J. A., Rapp U. R., Roberts T. M., Williams L. T. Direct activation of the serine/threonine kinase activity of Raf-1 through tyrosine phosphorylation by the PDGF beta-receptor. Cell. 1989 Aug 25;58(4):649–657. doi: 10.1016/0092-8674(89)90100-1. [DOI] [PubMed] [Google Scholar]
  132. Muramatsu M., Kaibuchi K., Arai K. A protein kinase C cDNA without the regulatory domain is active after transfection in vivo in the absence of phorbol ester. Mol Cell Biol. 1989 Feb;9(2):831–836. doi: 10.1128/mcb.9.2.831. [DOI] [PMC free article] [PubMed] [Google Scholar]
  133. Nakanishi H., Exton J. H. Purification and characterization of the zeta isoform of protein kinase C from bovine kidney. J Biol Chem. 1992 Aug 15;267(23):16347–16354. [PubMed] [Google Scholar]
  134. Newton A. C., Koshland D. E., Jr High cooperativity, specificity, and multiplicity in the protein kinase C-lipid interaction. J Biol Chem. 1989 Sep 5;264(25):14909–14915. [PubMed] [Google Scholar]
  135. Newton A. C., Koshland D. E., Jr Protein kinase C autophosphorylates by an intrapeptide reaction. J Biol Chem. 1987 Jul 25;262(21):10185–10188. [PubMed] [Google Scholar]
  136. Niino Y. S., Ohno S., Suzuki K. Positive and negative regulation of the transcription of the human protein kinase C beta gene. J Biol Chem. 1992 Mar 25;267(9):6158–6163. [PubMed] [Google Scholar]
  137. Nishizuka Y. The molecular heterogeneity of protein kinase C and its implications for cellular regulation. Nature. 1988 Aug 25;334(6184):661–665. doi: 10.1038/334661a0. [DOI] [PubMed] [Google Scholar]
  138. Obeid L. M., Blobe G. C., Karolak L. A., Hannun Y. A. Cloning and characterization of the major promoter of the human protein kinase C beta gene. Regulation by phorbol esters. J Biol Chem. 1992 Oct 15;267(29):20804–20810. [PubMed] [Google Scholar]
  139. Ogita K., Miyamoto S., Yamaguchi K., Koide H., Fujisawa N., Kikkawa U., Sahara S., Fukami Y., Nishizuka Y. Isolation and characterization of delta-subspecies of protein kinase C from rat brain. Proc Natl Acad Sci U S A. 1992 Mar 1;89(5):1592–1596. doi: 10.1073/pnas.89.5.1592. [DOI] [PMC free article] [PubMed] [Google Scholar]
  140. Ohno S., Akita Y., Hata A., Osada S., Kubo K., Konno Y., Akimoto K., Mizuno K., Saido T., Kuroki T. Structural and functional diversities of a family of signal transducing protein kinases, protein kinase C family; two distinct classes of PKC, conventional cPKC and novel nPKC. Adv Enzyme Regul. 1991;31:287–303. doi: 10.1016/0065-2571(91)90018-h. [DOI] [PubMed] [Google Scholar]
  141. Ohno S., Akita Y., Konno Y., Imajoh S., Suzuki K. A novel phorbol ester receptor/protein kinase, nPKC, distantly related to the protein kinase C family. Cell. 1988 Jun 3;53(5):731–741. doi: 10.1016/0092-8674(88)90091-8. [DOI] [PubMed] [Google Scholar]
  142. Ohno S., Kawasaki H., Imajoh S., Suzuki K., Inagaki M., Yokokura H., Sakoh T., Hidaka H. Tissue-specific expression of three distinct types of rabbit protein kinase C. Nature. 1987 Jan 8;325(7000):161–166. doi: 10.1038/325161a0. [DOI] [PubMed] [Google Scholar]
  143. Ohno S., Kawasaki H., Konno Y., Inagaki M., Hidaka H., Suzuki K. A fourth type of rabbit protein kinase C. Biochemistry. 1988 Mar 22;27(6):2083–2087. doi: 10.1021/bi00406a040. [DOI] [PubMed] [Google Scholar]
  144. Ohno S., Konno Y., Akita Y., Yano A., Suzuki K. A point mutation at the putative ATP-binding site of protein kinase C alpha abolishes the kinase activity and renders it down-regulation-insensitive. A molecular link between autophosphorylation and down-regulation. J Biol Chem. 1990 Apr 15;265(11):6296–6300. [PubMed] [Google Scholar]
  145. Okuda T., Sawada H., Kato Y., Yumoto Y., Ogawa K., Tashima M., Okuma M. Effects of protein kinase A and calcium/phospholipid-dependent kinase modulators in the process of HL-60 cell differentiation: their opposite effects between HL-60 cell and K-562 cell differentiation. Cell Growth Differ. 1991 Sep;2(9):415–420. [PubMed] [Google Scholar]
  146. Olivier A. R., Parker P. J. Expression and characterization of protein kinase C-delta. Eur J Biochem. 1991 Sep 15;200(3):805–810. doi: 10.1111/j.1432-1033.1991.tb16248.x. [DOI] [PubMed] [Google Scholar]
  147. Ono Y., Fujii T., Igarashi K., Kikkawa U., Ogita K., Nishizuka Y. Nucleotide sequences of cDNAs for alpha and gamma subspecies of rat brain protein kinase C. Nucleic Acids Res. 1988 Jun 10;16(11):5199–5200. doi: 10.1093/nar/16.11.5199. [DOI] [PMC free article] [PubMed] [Google Scholar]
  148. Ono Y., Fujii T., Igarashi K., Kuno T., Tanaka C., Kikkawa U., Nishizuka Y. Phorbol ester binding to protein kinase C requires a cysteine-rich zinc-finger-like sequence. Proc Natl Acad Sci U S A. 1989 Jul;86(13):4868–4871. doi: 10.1073/pnas.86.13.4868. [DOI] [PMC free article] [PubMed] [Google Scholar]
  149. Ono Y., Fujii T., Ogita K., Kikkawa U., Igarashi K., Nishizuka Y. Protein kinase C zeta subspecies from rat brain: its structure, expression, and properties. Proc Natl Acad Sci U S A. 1989 May;86(9):3099–3103. doi: 10.1073/pnas.86.9.3099. [DOI] [PMC free article] [PubMed] [Google Scholar]
  150. Ono Y., Fujii T., Ogita K., Kikkawa U., Igarashi K., Nishizuka Y. The structure, expression, and properties of additional members of the protein kinase C family. J Biol Chem. 1988 May 15;263(14):6927–6932. [PubMed] [Google Scholar]
  151. Ono Y., Kikkawa U., Ogita K., Fujii T., Kurokawa T., Asaoka Y., Sekiguchi K., Ase K., Igarashi K., Nishizuka Y. Expression and properties of two types of protein kinase C: alternative splicing from a single gene. Science. 1987 May 29;236(4805):1116–1120. doi: 10.1126/science.3576226. [DOI] [PubMed] [Google Scholar]
  152. Ono Y., Kurokawa T., Fujii T., Kawahara K., Igarashi K., Kikkawa U., Ogita K., Nishizuka Y. Two types of complementary DNAs of rat brain protein kinase C. Heterogeneity determined by alternative splicing. FEBS Lett. 1986 Oct 6;206(2):347–352. doi: 10.1016/0014-5793(86)81010-9. [DOI] [PubMed] [Google Scholar]
  153. Orr J. W., Newton A. C. Interaction of protein kinase C with phosphatidylserine. 2. Specificity and regulation. Biochemistry. 1992 May 19;31(19):4667–4673. doi: 10.1021/bi00134a019. [DOI] [PubMed] [Google Scholar]
  154. Osada S., Mizuno K., Saido T. C., Akita Y., Suzuki K., Kuroki T., Ohno S. A phorbol ester receptor/protein kinase, nPKC eta, a new member of the protein kinase C family predominantly expressed in lung and skin. J Biol Chem. 1990 Dec 25;265(36):22434–22440. [PubMed] [Google Scholar]
  155. Osada S., Mizuno K., Saido T. C., Suzuki K., Kuroki T., Ohno S. A new member of the protein kinase C family, nPKC theta, predominantly expressed in skeletal muscle. Mol Cell Biol. 1992 Sep;12(9):3930–3938. doi: 10.1128/mcb.12.9.3930. [DOI] [PMC free article] [PubMed] [Google Scholar]
  156. Otte A. P., Moon R. T. Protein kinase C isozymes have distinct roles in neural induction and competence in Xenopus. Cell. 1992 Mar 20;68(6):1021–1029. doi: 10.1016/0092-8674(92)90074-m. [DOI] [PubMed] [Google Scholar]
  157. Pai J. K., Pachter J. A., Weinstein I. B., Bishop W. R. Overexpression of protein kinase C beta 1 enhances phospholipase D activity and diacylglycerol formation in phorbol ester-stimulated rat fibroblasts. Proc Natl Acad Sci U S A. 1991 Jan 15;88(2):598–602. doi: 10.1073/pnas.88.2.598. [DOI] [PMC free article] [PubMed] [Google Scholar]
  158. Pan T., Coleman J. E. GAL4 transcription factor is not a "zinc finger" but forms a Zn(II)2Cys6 binuclear cluster. Proc Natl Acad Sci U S A. 1990 Mar;87(6):2077–2081. doi: 10.1073/pnas.87.6.2077. [DOI] [PMC free article] [PubMed] [Google Scholar]
  159. Parker P. J., Coussens L., Totty N., Rhee L., Young S., Chen E., Stabel S., Waterfield M. D., Ullrich A. The complete primary structure of protein kinase C--the major phorbol ester receptor. Science. 1986 Aug 22;233(4766):853–859. doi: 10.1126/science.3755547. [DOI] [PubMed] [Google Scholar]
  160. Parker P. J., Goris J., Merlevede W. Specificity of protein phosphatases in the dephosphorylation of protein kinase C. Biochem J. 1986 Nov 15;240(1):63–67. doi: 10.1042/bj2400063. [DOI] [PMC free article] [PubMed] [Google Scholar]
  161. Patel G., Stabel S. Expression of a functional protein kinase C-gamma using a baculovirus vector: purification and characterisation of a single protein kinase C iso-enzyme. Cell Signal. 1989;1(3):227–240. doi: 10.1016/0898-6568(89)90040-5. [DOI] [PubMed] [Google Scholar]
  162. Patel H. R., Choi H. S., Sytkowski A. J. Activation of two discrete signaling pathways by erythropoietin. J Biol Chem. 1992 Oct 25;267(30):21300–21302. [PubMed] [Google Scholar]
  163. Pears C. J., Kour G., House C., Kemp B. E., Parker P. J. Mutagenesis of the pseudosubstrate site of protein kinase C leads to activation. Eur J Biochem. 1990 Nov 26;194(1):89–94. doi: 10.1111/j.1432-1033.1990.tb19431.x. [DOI] [PubMed] [Google Scholar]
  164. Pears C., Parker P. J. Down-regulation of a kinase defective PKC-alpha. FEBS Lett. 1991 Jun 17;284(1):120–122. doi: 10.1016/0014-5793(91)80776-y. [DOI] [PubMed] [Google Scholar]
  165. Pears C., Schaap D., Parker P. J. The regulatory domain of protein kinase C-epsilon restricts the catalytic-domain-specificity. Biochem J. 1991 May 15;276(Pt 1):257–260. doi: 10.1042/bj2760257. [DOI] [PMC free article] [PubMed] [Google Scholar]
  166. Pears C., Stabel S., Cazaubon S., Parker P. J. Studies on the phosphorylation of protein kinase C-alpha. Biochem J. 1992 Apr 15;283(Pt 2):515–518. doi: 10.1042/bj2830515. [DOI] [PMC free article] [PubMed] [Google Scholar]
  167. Perin M. S., Fried V. A., Mignery G. A., Jahn R., Südhof T. C. Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C. Nature. 1990 May 17;345(6272):260–263. doi: 10.1038/345260a0. [DOI] [PubMed] [Google Scholar]
  168. Persons D. A., Owen R. D., Ostrowski M. C., Finn O. J. Protein kinase C gamma expression mimics phorbol ester-induced transcriptional activation of a murine VL30 enhancer element. Cell Growth Differ. 1991 Jan;2(1):7–14. [PubMed] [Google Scholar]
  169. Persons D. A., Wilkison W. O., Bell R. M., Finn O. J. Altered growth regulation and enhanced tumorigenicity of NIH 3T3 fibroblasts transfected with protein kinase C-I cDNA. Cell. 1988 Feb 12;52(3):447–458. doi: 10.1016/s0092-8674(88)80037-0. [DOI] [PubMed] [Google Scholar]
  170. Pfeffer L. M., Eisenkraft B. L., Reich N. C., Improta T., Baxter G., Daniel-Issakani S., Strulovici B. Transmembrane signaling by interferon alpha involves diacylglycerol production and activation of the epsilon isoform of protein kinase C in Daudi cells. Proc Natl Acad Sci U S A. 1991 Sep 15;88(18):7988–7992. doi: 10.1073/pnas.88.18.7988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  171. Pfeffer L. M., Strulovici B., Saltiel A. R. Interferon-alpha selectively activates the beta isoform of protein kinase C through phosphatidylcholine hydrolysis. Proc Natl Acad Sci U S A. 1990 Sep;87(17):6537–6541. doi: 10.1073/pnas.87.17.6537. [DOI] [PMC free article] [PubMed] [Google Scholar]
  172. Pontremoli S., Michetti M., Melloni E., Sparatore B., Salamino F., Horecker B. L. Identification of the proteolytically activated form of protein kinase C in stimulated human neutrophils. Proc Natl Acad Sci U S A. 1990 May;87(10):3705–3707. doi: 10.1073/pnas.87.10.3705. [DOI] [PMC free article] [PubMed] [Google Scholar]
  173. Powell C. T., Leng L., Dong L., Kiyokawa H., Busquets X., O'Driscoll K., Marks P. A., Rifkind R. A. Protein kinase C isozymes epsilon and alpha in murine erythroleukemia cells. Proc Natl Acad Sci U S A. 1992 Jan 1;89(1):147–151. doi: 10.1073/pnas.89.1.147. [DOI] [PMC free article] [PubMed] [Google Scholar]
  174. Quest A. F., Bloomenthal J., Bardes E. S., Bell R. M. The regulatory domain of protein kinase C coordinates four atoms of zinc. J Biol Chem. 1992 May 15;267(14):10193–10197. [PubMed] [Google Scholar]
  175. Reuben R. C., Rifkind R. A., Marks P. A. Chemically induced murine erythroleukemic differentiation. Biochim Biophys Acta. 1980 Sep 22;605(3):325–346. doi: 10.1016/0304-419x(80)90015-3. [DOI] [PubMed] [Google Scholar]
  176. Rogue P., Labourdette G., Masmoudi A., Yoshida Y., Huang F. L., Huang K. P., Zwiller J., Vincendon G., Malviya A. N. Rat liver nuclei protein kinase C is the isozyme type II. J Biol Chem. 1990 Mar 5;265(7):4161–4165. [PubMed] [Google Scholar]
  177. Rose-John S., Dietrich A., Marks F. Molecular cloning of mouse protein kinase C (PKC) cDNA from Swiss 3T3 fibroblasts. Gene. 1988 Dec 30;74(2):465–471. doi: 10.1016/0378-1119(88)90179-5. [DOI] [PubMed] [Google Scholar]
  178. Rutherford T. R., Clegg J. B., Weatherall D. J. K562 human leukaemic cells synthesise embryonic haemoglobin in response to haemin. Nature. 1979 Jul 12;280(5718):164–165. doi: 10.1038/280164a0. [DOI] [PubMed] [Google Scholar]
  179. Ryves W. J., Evans A. T., Olivier A. R., Parker P. J., Evans F. J. Activation of the PKC-isotypes alpha, beta 1, gamma, delta and epsilon by phorbol esters of different biological activities. FEBS Lett. 1991 Aug 19;288(1-2):5–9. doi: 10.1016/0014-5793(91)80989-g. [DOI] [PubMed] [Google Scholar]
  180. Saido T. C., Mizuno K., Konno Y., Osada S., Ohno S., Suzuki K. Purification and characterization of protein kinase C epsilon from rabbit brain. Biochemistry. 1992 Jan 21;31(2):482–490. doi: 10.1021/bi00117a026. [DOI] [PubMed] [Google Scholar]
  181. Sakane F., Yamada K., Kanoh H., Yokoyama C., Tanabe T. Porcine diacylglycerol kinase sequence has zinc finger and E-F hand motifs. Nature. 1990 Mar 22;344(6264):345–348. doi: 10.1038/344345a0. [DOI] [PubMed] [Google Scholar]
  182. Schaap D., Hsuan J., Totty N., Parker P. J. Proteolytic activation of protein kinase C-epsilon. Eur J Biochem. 1990 Jul 31;191(2):431–435. doi: 10.1111/j.1432-1033.1990.tb19139.x. [DOI] [PubMed] [Google Scholar]
  183. Schaap D., Parker P. J., Bristol A., Kriz R., Knopf J. Unique substrate specificity and regulatory properties of PKC-epsilon: a rationale for diversity. FEBS Lett. 1989 Jan 30;243(2):351–357. doi: 10.1016/0014-5793(89)80160-7. [DOI] [PubMed] [Google Scholar]
  184. Schaap D., Parker P. J. Expression, purification, and characterization of protein kinase C-epsilon. J Biol Chem. 1990 May 5;265(13):7301–7307. [PubMed] [Google Scholar]
  185. Sekiguchi K., Tsukuda M., Ase K., Kikkawa U., Nishizuka Y. Mode of activation and kinetic properties of three distinct forms of protein kinase C from rat brain. J Biochem. 1988 May;103(5):759–765. doi: 10.1093/oxfordjournals.jbchem.a122343. [DOI] [PubMed] [Google Scholar]
  186. Shearman M. S., Naor Z., Sekiguchi K., Kishimoto A., Nishizuka Y. Selective activation of the gamma-subspecies of protein kinase C from bovine cerebellum by arachidonic acid and its lipoxygenase metabolites. FEBS Lett. 1989 Jan 30;243(2):177–182. doi: 10.1016/0014-5793(89)80125-5. [DOI] [PubMed] [Google Scholar]
  187. Shen S. S., Buck W. R. A synthetic peptide of the pseudosubstrate domain of protein kinase C blocks cytoplasmic alkalinization during activation of the sea urchin egg. Dev Biol. 1990 Aug;140(2):272–280. doi: 10.1016/0012-1606(90)90077-v. [DOI] [PubMed] [Google Scholar]
  188. Shirakawa F., Mizel S. B. In vitro activation and nuclear translocation of NF-kappa B catalyzed by cyclic AMP-dependent protein kinase and protein kinase C. Mol Cell Biol. 1989 Jun;9(6):2424–2430. doi: 10.1128/mcb.9.6.2424. [DOI] [PMC free article] [PubMed] [Google Scholar]
  189. Siegel J. N., Klausner R. D., Rapp U. R., Samelson L. E. T cell antigen receptor engagement stimulates c-raf phosphorylation and induces c-raf-associated kinase activity via a protein kinase C-dependent pathway. J Biol Chem. 1990 Oct 25;265(30):18472–18480. [PubMed] [Google Scholar]
  190. Smith M. J., Charron-Prochownik D. C., Prochownik E. V. The leucine zipper of c-Myc is required for full inhibition of erythroleukemia differentiation. Mol Cell Biol. 1990 Oct;10(10):5333–5339. doi: 10.1128/mcb.10.10.5333. [DOI] [PMC free article] [PubMed] [Google Scholar]
  191. Smith M. R., Jaramillo M., Tuazon P. T., Traugh J. A., Liu Y. L., Sonenberg N., Kung H. F. Modulation of the mitogenic activity of eukaryotic translation initiation factor-4E by protein kinase C. New Biol. 1991 Jun;3(6):601–607. [PubMed] [Google Scholar]
  192. Soderling T. R. Protein kinases. Regulation by autoinhibitory domains. J Biol Chem. 1990 Feb 5;265(4):1823–1826. [PubMed] [Google Scholar]
  193. Stabel S., Parker P. J. Protein kinase C. Pharmacol Ther. 1991;51(1):71–95. doi: 10.1016/0163-7258(91)90042-k. [DOI] [PubMed] [Google Scholar]
  194. Stabel S., Schaap D., Parker P. J. Expression of protein kinase C isotypes using baculovirus vectors. Methods Enzymol. 1991;200:670–673. doi: 10.1016/0076-6879(91)00179-z. [DOI] [PubMed] [Google Scholar]
  195. Stahl M. L., Ferenz C. R., Kelleher K. L., Kriz R. W., Knopf J. L. Sequence similarity of phospholipase C with the non-catalytic region of src. Nature. 1988 Mar 17;332(6161):269–272. doi: 10.1038/332269a0. [DOI] [PubMed] [Google Scholar]
  196. Strulovici B., Daniel-Issakani S., Baxter G., Knopf J., Sultzman L., Cherwinski H., Nestor J., Jr, Webb D. R., Ransom J. Distinct mechanisms of regulation of protein kinase C epsilon by hormones and phorbol diesters. J Biol Chem. 1991 Jan 5;266(1):168–173. [PubMed] [Google Scholar]
  197. Sullivan J. P., Connor J. R., Tiffany C., Shearer B. G., Burch R. M. NPC 15437 interacts with the C1 domain of protein kinase C. An analysis using mutant PKC constructs. FEBS Lett. 1991 Jul 8;285(1):120–123. doi: 10.1016/0014-5793(91)80739-p. [DOI] [PubMed] [Google Scholar]
  198. Susa M., Olivier A. R., Fabbro D., Thomas G. EGF induces biphasic S6 kinase activation: late phase is protein kinase C-dependent and contributes to mitogenicity. Cell. 1989 Jun 2;57(5):817–824. doi: 10.1016/0092-8674(89)90796-4. [DOI] [PubMed] [Google Scholar]
  199. Sözeri O., Vollmer K., Liyanage M., Frith D., Kour G., Mark G. E., 3rd, Stabel S. Activation of the c-Raf protein kinase by protein kinase C phosphorylation. Oncogene. 1992 Nov;7(11):2259–2262. [PubMed] [Google Scholar]
  200. Takai Y., Kishimoto A., Iwasa Y., Kawahara Y., Mori T., Nishizuka Y. Calcium-dependent activation of a multifunctional protein kinase by membrane phospholipids. J Biol Chem. 1979 May 25;254(10):3692–3695. [PubMed] [Google Scholar]
  201. Tamaoki T., Nakano H. Potent and specific inhibitors of protein kinase C of microbial origin. Biotechnology (N Y) 1990 Aug;8(8):732–735. doi: 10.1038/nbt0890-732. [DOI] [PubMed] [Google Scholar]
  202. Tanaka Y., Yoshihara K., Tsuyuki M., Itaya-Hironaka A., Inada Y., Kamiya T. Retinoic acid-specific induction of a protein kinase C isoform during differentiation of HL-60 cells. J Biochem. 1992 Feb;111(2):265–271. doi: 10.1093/oxfordjournals.jbchem.a123747. [DOI] [PubMed] [Google Scholar]
  203. Tang Y. M., Ashendel C. L. Isolation of cloned mouse protein kinase C beta-II cDNA and its sequence. Nucleic Acids Res. 1990 Sep 11;18(17):5310–5310. doi: 10.1093/nar/18.17.5310. [DOI] [PMC free article] [PubMed] [Google Scholar]
  204. Taylor S. S., Buechler J. A., Yonemoto W. cAMP-dependent protein kinase: framework for a diverse family of regulatory enzymes. Annu Rev Biochem. 1990;59:971–1005. doi: 10.1146/annurev.bi.59.070190.004543. [DOI] [PubMed] [Google Scholar]
  205. Trayner I. D., Clemens M. J. Stimulation of proliferation of HL60 cells by low concentrations of 12-O-tetradecanoylphorbol-13-acetate and its relationship to the mitogenic effects of insulin. Exp Cell Res. 1992 Mar;199(1):154–161. doi: 10.1016/0014-4827(92)90473-l. [DOI] [PubMed] [Google Scholar]
  206. Wada H., Ohno S., Kubo K., Taya C., Tsuji S., Yonehara S., Suzuki K. Cell type-specific expression of the genes for the protein kinase C family: down regulation of mRNAs for PKC alpha and nPKC epsilon upon in vitro differentiation of a mouse neuroblastoma cell line neuro 2a. Biochem Biophys Res Commun. 1989 Nov 30;165(1):533–538. doi: 10.1016/0006-291x(89)91102-9. [DOI] [PubMed] [Google Scholar]
  207. Wetsel W. C., Khan W. A., Merchenthaler I., Rivera H., Halpern A. E., Phung H. M., Negro-Vilar A., Hannun Y. A. Tissue and cellular distribution of the extended family of protein kinase C isoenzymes. J Cell Biol. 1992 Apr;117(1):121–133. doi: 10.1083/jcb.117.1.121. [DOI] [PMC free article] [PubMed] [Google Scholar]
  208. Wolf M., Baggiolini M. Identification of phosphatidylserine-binding proteins in human white blood cells. Biochem J. 1990 Aug 1;269(3):723–728. doi: 10.1042/bj2690723. [DOI] [PMC free article] [PubMed] [Google Scholar]
  209. Wooten M. W., Seibenhener M. L., Soh Y., Ewald S. J., White K. R., Lloyd E. D., Olivier A., Parker P. J. Characterization and differential expression of protein kinase C isoforms in PC12 cells. Differentiation parallels an increase in PKC beta II. FEBS Lett. 1992 Feb 17;298(1):74–78. doi: 10.1016/0014-5793(92)80025-c. [DOI] [PubMed] [Google Scholar]
  210. Yasuda I., Kishimoto A., Tanaka S., Tominaga M., Sakurai A., Nishizuka Y. A synthetic peptide substrate for selective assay of protein kinase C. Biochem Biophys Res Commun. 1990 Feb 14;166(3):1220–1227. doi: 10.1016/0006-291x(90)90996-z. [DOI] [PubMed] [Google Scholar]
  211. Yoshida Y., Huang F. L., Nakabayashi H., Huang K. P. Tissue distribution and developmental expression of protein kinase C isozymes. J Biol Chem. 1988 Jul 15;263(20):9868–9873. [PubMed] [Google Scholar]
  212. Zidovetzki R., Lester D. S. The mechanism of activation of protein kinase C: a biophysical perspective. Biochim Biophys Acta. 1992 Apr 7;1134(3):261–272. doi: 10.1016/0167-4889(92)90185-e. [DOI] [PubMed] [Google Scholar]
  213. van den Berghe N., Vaandrager A. B., Bot A. G., Parker P. J., de Jonge H. R. Dual role for protein kinase C alpha as a regulator of ion secretion in the HT29cl.19A human colonic cell line. Biochem J. 1992 Jul 15;285(Pt 2):673–679. doi: 10.1042/bj2850673. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES