Activation of human platelets by protein kinase C antibody: Role for surface phosphorylation in homeostasis

American Journal of Physiology - Heart and Circulatory Physiology

Volumn 271, Issue 5 40-5, 1996, Pages

  Babinska, Anna ^b   Ehrlich, Yigal H ^b   Kornecki, Elizabeth ^a  

^a SUNY DOWNSTATE MEDICAL CENTER   (United States)

^b NONE

Author keywords

ecto protein kinase C; platelet aggregation and secretion; protein kinase C pseudosubstrate peptides; stimulatory monoclonal antibody; surface protein phosphorylation and dephosphorylation

Indexed keywords

MONOCLONAL ANTIBODY; PROTEIN KINASE C;

ANTIGEN BINDING; ARTICLE; DEPHOSPHORYLATION; FEMALE; FLOW CYTOMETRY; HUMAN; HUMAN CELL; MALE; NORMAL HUMAN; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN PHOSPHORYLATION; THROMBOCYTE ACTIVATION; THROMBOCYTE AGGREGATION;

EID: 0029959503     PISSN: 03636135     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpheart.1996.271.5.h2134     Document Type: Article

References (35)

1. Amano, R., T. Kitagawa, and Y. Akamatsu. Protein kinase activity on the cell surface of a macrophage-like cell line, J774.1 cells. Biochim. Biophys.Acta 803: 163-173, 1984.
2. Asch, A. S., I. Liu, F. M. Briccetti, J. W. Barnwell, F. Kwakye-Berko, A. Kokon, J. Goldberger, and M. Pernambuco. Analysis of CD36 binding domains: ligand specificity controlled by dephosphorylation of an ectodomain. Science Wash. DC 262: 1436-1440, 1993.
3. Berman, C. L., E. L. Yeo, J. D. Wencel-Drake, B. C. Furie, M. H. Ginsberg, and B. Furie. A platelet alpha granule membrane protein that is associated with the plasma membrane after activation. J. Clin. Invest. 78: 130-137, 1986.
4. Chang, T. M., E. S. Kang, and A. H. Kang. Ecto-protein kinase activity of fibroblasts. Arch. Biochem. Biophys. 1295: 515-518, 1979.
5. Chen, W., A. Wieraszko, M. V. Hogan, H.-A. Yang, E. Kornecki, and Y. H. Ehrlich. Surface protein phosphorylation by ecto-protein kinase is required for the maintenance of hippocampal long-term potentiation. Proc. Natl. Acad. Sci. USA 93: 8688-8693, 1996.
6. Chen, X. Y., and T. C. Lo. Involvement of a cell surface protein and an ecto-protein kinase in myogenesis. Biochem. J. 279: 475-482, 1991.
7. Ehrlich, Y. H. Extracellular protein phosphorylation in neuronal responsiveness and adaptation. In: Advances in Experimental Medicine and Biology. New York: Plenum, 1987, vol. 221, p. 187-200.
8. Ehrlich, Y. H., T. D. Davis, E. Bock, E. Kornecki, and R. H. Lenox. Ecto-protein kinase activity on the external surface of intact neural cells. Nature Lond. 320: 67-70, 1986.
9. Ehrlich, Y. H., M. V. Hogan, Z. Pawlowska, U. Naik, and E. Kornecki. Ecto-protein kinase in the regulation of cellular responsiveness to extracellular ATP. Ann. NY Acad. Sci. 603: 410-416, 1990.
10. Ehrlich, Y. H., and E. Kornecki. Extracellular protein phosphorylation systems in the regulation of cellular responsiveness. In: Mechanisms of Signal Transduction by Hormones and Growth Factors, edited by M. C. Cabot and W. L. McKeehan. New York: Liss, 1987, p. 193-204.
11. Essex, D. W., K. Chen, and M. Swiatkowska. Localization of protein disulfide isomerase to the external surface of the platelet plasma membrane. Blood 86: 2168-2173, 1995.
12. 2-purinoceptor antagonists. Rev. Ann. NY Acad. Sci. 603: 527-529, 1990.
13. Friedberg, I., I. Belzer, O. Oged-Plesz, and D. Kübler. Activation of cell growth inhibitor by ectoprotein kinase-mediated phosphorylation in transformed mouse fibroblasts. J. Biol. Chem. 270: 20560-20567, 1995.
14. Gordon, J. L. Extracellular ATP: effects, sources and fate. Biochem. J. 233: 309-319, 1986.
15. Haldar, S., and G. C. Kajumder. Phosphorylation of external cell-surface proteins by an endogenous ecto-protein kinase of goat epididymal intact spermatozoa. Biochim. Biophys. Acta 887: 291-303, 1986.
16. Hogan, M. V., Z. Pawlowska, H.-A. Yang, E. Kornecki, and Y. H. Ehrlich. Surface phosphorylation by ecto-protein kinase C in brain neurons: a target for Alzheimer's β-amyloid peptides. J. Neurochem. 65: 2022-2031, 1995.
17. Johannes, F. J., J. Prestle, S. Eis, P. Oberhagemann, and K. Pfizenmaier. PKCμ is a novel, atypical member of the protein kinase C family. J. Biol. Chem. 269: 6140-6148, 1994.
18. Kalafatis, M., M. D. Rand, R. J. Jenny, Y. H. Ehrlich, and K. G. Mann. Phosphorylation of Factor Va and Factor VIIIa by activated platelets. Blood 81: 704-719, 1993.
19. Kang, E. S., R. E. Gates, T. M. Chiang, and A. H. Kang. Ectoprotein kinase activity of the isolated rat adipocyte. Biochem. Biophys. Res. Commun. 86: 769-778, 1979.
20. Kornecki, E., B. Walkowiak, U. P. Naik, and Y. H. Ehrlich. Activation of human platelets by a stimulatory antibody. J. Biol. Chem. 265: 10042-10048, 1990.
21. Kübler, D., W. Pyerin, and V. Kinzel. Protein kinase activity and substrates at the surface of intact HeLa cells. J. Biol. Chem. 257: 322-329, 1982.
22. Masters, A. M., and E. Rozengurt. Endogenous protein kinase in outer plasma membrane of cultured 3T3 cells. J. Biol. Chem. 251: 7899-7906, 1976.
23. Mochly-Rosen, D., and D. E. Koshland. Domain structure and phosphorylation of protein kinase C. J. Biol. Chem. 262: 2291-2297, 1987.
24. Mochly-Rosen, D., and D. E. Koshland. A general procedure for screening inhibitory antibodies: application for identifying anti-protein kinase C antibodies. Anal. Biochem. 170: 31-37, 1988.
25. Myers, L. K., and E. S. Kang. Modulation of natural killer cell activity by surface phosphorylation reactions. Exp. Cell. Res. 187: 270-276, 1990.
26. Naik, U. P., Y. H. Ehrlich, and E. Kornecki. Mechanisms of platelet activation by a stimulatory antibody: cross-linking of a novel platelet receptor for monoclonal antibody F11 with the FcγRII receptor. Biochem. J. 310: 155-162, 1995.
27. Naik, U. P., E. Kornecki, and Y. H. Ehrlich. Phosphorylation of human platelet surface proteins by an ecto-protein kinase system: association with a platelet surface ecto-protein phosphatase. Biochim. Biophys. Acta 1092: 256-264, 1991.
28. Pawlowska, Z., M. V. Hogan, E. Kornecki, and Y. H. Ehrlich. Ecto-protein kinase and surface protein phosphorylation in PC12 cells: interactions with nerve growth factor. J. Neurochem. 60: 678-686, 1993.
29. Pirrotton, S., O. Boutherin-Falson, B. Robaye, and J.-M. Boeynaems. Ecto-phosphorylation on aortic endothelial cells. Biochem. J. 285: 585-591, 1992.
30. 32P-labeled adenosine triphosphate. Acta Chem. Scand. Ser. B. Org. Chem Biochem. 28: 1169-1174, 1974.
31. Skubitz, K. M., D. D. Ehresmann, and T. P. Ducker. Characterization of human neutrophil ecto-protein kinase activity released by kinase substrates. J. Immunol. 147: 638-650, 1991.
32. Slupsky, J. R., J. G. Seehafer, S-C, Tang, A. Masellis-Smith, and A. R. E. Shaw. Evidence that monoclonal antibodies against. CD9 antigen induce specific association between CD9 and the platelet glycoprotein IIb-IIIa complex. J. Biol. Chem. 264: 12289-12293, 1989.
33. Soslau, G., and J. Parker. Modulation of platelet function by extracellular adenosine triphosphate. Blood 74: 984-993, 1989.
34. Wang, F., U. P. Naik, Y. H. Ehrlich, Z. Freyberg, S.-I. Osada, S. Ohno, T. Kuroki, K. Suzuki, and E. Kornecki. A new protein kinase C, nPKCn' and PKCq are expressed in human platelets: involvement of nPKCn' and nPKCq in signal transduction stimulated by PAF. Biochem. Biophys. Res. Commun. 191: 240-246, 1993.
35. Wang, F., U. P. Naik, Y. H. Ehrlich, S-I. Osada, S. Ohno, and E. Kornecki. Stimulatory antibody-induced activation and selective translocation of protein kinase C isoenzymes in human platelets. Biochem. J. 311: 401-406, 1995.