Differential association of protein Ser/Thr phosphatase types 1 and 2A with the cytoskeleton upon platelet activation

Thrombosis and Haemostasis

Volumn 76, Issue 6, 1996, Pages 1053-1062

  Toyoda, Hideki ^a   Nakai, Keiji ^a   Omay, Serdar B ^a   Shima, Hiroshi ^b   Nagao, Minako ^b   Shiku, Hiroshi ^a   Nishikawa, Masakatsu ^a  

^a MIE UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^b NATIONAL CANCER CENTER RESEARCH INSTITUTE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ATAPROST; CELL PROTEIN; MYOSIN LIGHT CHAIN KINASE; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN KINASE C; THROMBIN; TRITON X 100;

ARTICLE; CONTROLLED STUDY; CYTOSKELETON; ENZYME ACTIVITY; ENZYME SUBUNIT; HUMAN; HUMAN CELL; IMMUNOBLOTTING; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; THROMBOCYTE ACTIVATION;

EID: 0030456762     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0038-1650706     Document Type: Article

References (45)

1. Jennings LK, Fox JEB, Edwards HH, Phillips DR. Changes in the cytoskeletal structure of human platelets following thrombin activation. J Biol Chem 1981; 256: 6927-32.
2. Carroll RC, Butler RG, Morris PA, Gerrard JM. Separable assembly of platelet pseudopodal and contractile cytoskeletons. Cell 1982; 30: 385-93.
3. Kometani M, Sato T, Fujii T. Platelet cytoskeletal components involved in shape change and secretion. Thromb Res 1986; 41: 801-9.
4. Kouns WC, Fox CF, Lamoreaux WJ, Coons LB, Jennings LK. The effect of gycoprotein IIb-IIIa receptor occupancy on the cytoskeleton of resting and activated platelets. J Biol Chem 1991; 266: 13891-900.
5. Daniel JL, Holmsen H, Adelstein RS. Thrombin-stimulated myosin phosphorylation in intact platelets and its possible involvement in secretion. Thromb Haemost 1977; 38: 984-9.
6. Fox JEB, Phillips DR. Role of phosphorylation in mediating the association of myosin with the cytoskeletal structures of human platelets. J Biol Chem 1982; 257: 4120-6.
7. 2+-calmodulin-dependent phosphorylation and platelet secretion. Nature 1980; 287: 863-5.
8. Daniel JL, Molish IR, Rigmaiden M, Stewart G. Evidence for a role of myosin phosphorylation in the initiation of the platelet shape change response. J Biol Chem 1984; 259: 9826-31.
9. Sellers JR. Regulation of cytoplasmic and smooth muscle myosin. Curr Biol 1991; 3: 98-104.
10. Naka M, Nishikawa M, Adelstein RS, Hidaka H. Phorbol ester-induced activation of human platelets is associated with protein kinase C phosphorylation of myosin light chains. Nature 1983; 306: 490-2.
11. Nishikawa M, Sellers JR, Adelstein RS, Hidaka H. Protein kinase C modulates in vitro phosphorylation of the smooth muscle heavy meromyosin by myosin light chain kinase. J Biol Chem 1984; 259: 8808-14.
12. Ikebe M, Reardon S. Phosphorylation of bovine platelet myosin by protein kinase C. Biochemistry 1990; 29: 2713-20.
13. Lamb NJC, Fernandez A, Conti MA, Adelstein RS, Glass DB, Welch WJ, Feramisco JR. Regulation of actin microfilament integrity in living nonmuscle cells by the cAMP-dependent protein kinase and the myosin light chain kinase. J Cell Biol 1988; 106: 1955-71.
14. Lerea KM. Thrombin-induced effects are selectively inhibited following treatment of intact human platelets with okadaic acid. Biochemistry 1990; 30: 6819-24.
15. Higashihara M, Takahata K, Kurokawa K, Ikebe M. The inhibitory effects of okadaic acid on platelet function. FEBS Lett 1992; 307: 206-10.
16. Nishikawa M, Toyoda H, Saito M, Morita K, Tawara I, Deguchi K, Kuno T, Shima H, Nagao M, Shirakawa S. Calyculin A and okadaic acid inhibit human platelet aggregation by blocking protein phosphatases types 1 and 2A. Cell. Signal. 1994; 6: 59-71.
17. Cohen P. The structure and regulation of protein phosphatases. Annu Rev Biochem 1989; 58: 453-508.
18. Mumby MC, Walter G. Protein serine/threonine phosphatases: Structure, regulation, and functions in cell growth. Physiol Rev 1993; 73: 673-99.
19. Ozaki H, Ishihara H, Kohama K, Nonomura Y, Shibata S, Karaki H. Calcium-independent phosphorylation of smooth muscle myosin light chain by okadaic acid isolated from black sponge (Halichondria okadai). J Pharmacol Exp Ther 1987; 243: 1167-73.
20. Ishihara H, Ozaki H, Sato K, Hori M, Karaki H, Watabe S, Kato Y, Fusetani N, Hashimoto K, Uemura D, Hartshorne, DJ. Calcium-independent activation of contractile apparatus in smooth muscle by calyculin-A. J Pharmacol Exp Ther 1989; 250: 388-96.
21. Fernandez A, Brautigan DL, Mumby M, Lamb NJT. Protein phosphatase type-1, not type-2A, modulates actin microfilament integrity and myosin light chain phosphorylation in living nonmuscle cells. J Cell Biol 1990; 111: 103-12.
22. M) is the enzyme that dephosphorylates native myosin in skeletal and cardiac muscle. Biochim Biophys Acta. 1988; 971: 163-9.
23. Haeberle GR, Hathaway DR, DePaoli-Roach AA. Dephosphorylation of myosin by the catalytic subunit of a type-2A phosphatase produces relaxation of chemically skinned uterine smooth muscle. J Biol Chem 1985; 260: 9965-8.
24. Erdodi F, Rokolya A, Barany M, Barany K. Dephosphorylation ofdistinct sites in myosin light chain by two types of phosphatase in aortic smooth muscle. Biochim Biophys Acta 1989; 1011: 67-74.
25. Perrie WT, Perry, S.V. An electrophoretic study of the low-molecular weight components of myosin. Biochem J 1970; 119: 31-8.
26. Nishikawa M, Hidaka H. Role of calmodulin in platelet aggregation. Structure-activity relationship of calmodulin antagonists. J Clin Invest 1982; 69: 1348-55.
27. ras GTPase-activating protein with the membrane skeleton. J Biol Chem 1993; 268: 25973-84.
28. 3- induced monocytic differentiation of HL-60 cells. Cancer Res 1995; 55: 774-80.
29. Pato MD, Kerc E. Purification and characterization of a smooth muscle myosin phosphatase from turkey gizzards. J Biol Chem 1985; 260: 12359-66.
30. Sasaki K, Shima H, Kitagawa Y, Irino S, Sugimura T, Nagao M. Identification of members of the protein phosphatase 1 gene family in the rat and enhanced expression of protein phosphatase 1α gene in rat hepatocellular carcinoma. Jpn J Cancer Res 1990; 81: 1272-80.
31. Shima H, Hatano Y, Chun YS, Sugimura T, Zhang Z, Lee EYC, Nagao M. Identification of PP1 catalytic subunit isotypes PP1γ1, PP1δ and PP1α in various rat tissues. Biochem Biophys Res Commun 1993; 192:1289-96.
32. Nishikawa M, de Lanerolle P, Linoln TM, Adelstein RS. Phosphorylation of mammalian myosin light chain kinases by the catalytic subunit of cyclic AMP-dependent protein kinase and by cyclic GMP-dependent protein kinase. J Biol Chem 1984; 259: 8429-36.
33. Bechtel PJ, Beavo JA, Krebs EG. Purification and characterization of catalytic subunit of skeletal muscle adenosine 3':5'-monophosphate-dependent protein kinase J Biol Chem 1977; 252: 2691-7.
34. 2 analog, in experimental animals. II. Mechanism of its antiplatelet effect. Jap J Pharmacol 1990; 53: 25-33.
35. Kouns WC, Kirchhofer D, Hadvary P, Edenhofer A, Weller T, Pfenninger G, Baumgartner HR, Jennings LK, Steiner B. Reversible conformational changes induced in glycoprotein IIb-IIIa by a potent and selective peptidomimetic inhibitor. Blood 1992; 80: 2539-47.
36. Graber SE, Hawiger J. Evidence that changes in platelet cyclic AMP levels regulate the fibrinogen receptor on human platelets. J Biol Chem 1982; 257: 14606-9.
37. Carroll RC, Gerrard JM. Phosphorylation of platelet actin-binding protein during platelet activation. Blood 1982; 59: 466-71.
38. Sellers JR, Pato MD. Binding of smooth muscle myosin light chain kinase and phosphatases to actin and myosin. J Biol Chem 1984; 259: 7740-6.
39. Alessi D, Macdougall LK, Sola MM, Ikebe M, Cohen P, The control of protein phosphatase-1 by targetting subunits. The major myosin phosphatase in avian smooth muscle is a novel form of protein phosphatase-1. Eur J Biochem 1992; 210: 1023-35.
40. Shimizu H, Ito M, Miyahara M. Ichikawa K, Okubo S, Konishi T, Naka M, Tanaka T, Hirano K, Hartshorne DJ, Nakano T. Characterization of the myosin-binding subunit of smooth muscle myosin phosphatase. J Biol Chem 1994; 269: 30407-11.
41. Beckerle MC, Yeh RK. Talin: Role at sites of cell-substratum adhesion. Cell Motility and Cytoskeleton. 1990; 16: 7-13.
42. Bertagnolli ME, Locke SJ, Hensler ME, Bray PF, Beckerle MC. Talin distribution and phosphorylation in thrombin-activated platelets. J Cell Sci 1993; 106: 1189-99.
43. Murata K, Sakon M, Kambayashi J, Okuyama M, Hase T, Mori T. Platelet talin is phosphorylated by calyculin A. J Cell Biochem 1993; 57: 120-6.
44. Zhang J, Fry MJ, Waterfield MD, Jaken S, Liao L, Fox JEB, Rittenhouse SE. Activated phosphoinositide 3-kinase associates with membrane skeleton in thrombin-exposed platelets. J Biol Chem 1992; 267: 4686-92.
45. Shattil SJ, Brass LF. Induction of the fibrinogen receptor on human platelets by intracellular mediators. J Biol Chem 1987; 262: 992-1000.