Calyculin-A increases the level of protein phosphorylation and changes the shape of 3T3 fibroblasts

Cell Motility and the Cytoskeleton

Volumn 18, Issue 1, 1991, Pages 26-40

  Chartier, L ^a   Rankin, L L ^a   Allen, R E ^a   Kato, Y ^a   Fusetani, N ^a   Karaki, H ^a   Watabe, S ^a   Hartshorne, D J ^a  

^a UNIVERSITY OF ARIZONA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CALYCULIN A; ENZYME INHIBITOR; PHOSPHOPROTEIN PHOSPHATASE;

ARTICLE; CELL SHAPE; FIBROBLAST; INTERMEDIATE FILAMENT; MOUSE; NONHUMAN; PROTEIN PHOSPHORYLATION;

EID: 0026011049     PISSN: 08861544     EISSN: None     Source Type: Journal    
DOI: 10.1002/cm.970180104     Document Type: Article

References (54)

1. Adelstein, R. S., and Eisenberg, E. (1980): Regulation and kinetics of the actin‐myosin‐ATP interaction. Annu. Rev. Biochem. 49: 921–956.
2. Barak, L. S., Yocum, R. R., Nothnagel, E. A., and Webb, W. W. (1980) Fluorescence staining of the actin cytoskeleton in living cells with 7‐nitrobenz‐2‐oxa‐1,3‐diazole‐phallacidin. Froc. Natl. Acad. Sci. USA 77: 980–984.
3. Bialojan, C., Rüegg, J. C., and Takai, A. (1988): Effects of okadaic acid on isometric tension and myosin phosphorylation of chemically‐skinned guinea‐pig taenia coli. J. Physiol. 398: 81–95.
4. Brautigan, D. L., Fernandez, A., and Lamb, N. J. C. (1989): Microinjection of protein phosphatase type‐1 selectively alters fibro‐blast functions and in vivo phosphorylation. Adv. Protein Phosphatases 5: 547–566.
5. Brinkley, B. R., Fuller, G. M., and Highfield, D. P. (1975): Cytoplasmic microtubules in normal and transformed cells in culture: Analysis by tubulin immunofluorescence. Proc. Natl. Acad. Sci. USA 72: 4981–4985.
6. Cabral, F., and Gottesman, M. M. (1979): Phosphorylation of the 10‐nm filament protein from Chinese hamster ovary cells. J. Biol. Chem. 254: 6203–6206.
7. Chou, Y‐H., Rosevear, E., and Goldman, R. D. (1989): Phosphory‐lation and disassembly of intermediate filaments in mitotic cells. Proc. Natl. Acad. Sci., USA 86: 1885–1889.
8. Cohen, P., Klumpp, S., and Schelling, D. L. (1989): An improved procedure for identifying and quantitating protein phosphatases in mammalian tissues. FEBS Lett. 250: 596–600.
9. Eckert, B. S., Daley, R. A., and Parysek, L. M. (1982): Assembly of keratin onto PtK 1 cytoskeletons: evidence for an intermediate filament organizing center. J. Cell Biol. 92: 575–578.
10. Evans, R. M. (1988): Cyclic AMP‐dependent protein kinase‐induced vimentin filament disassembly involves modification of the N‐terminal domain of intermediate filament subunits. FEBS Lett. 234: 73–78.
11. Evans, R. M. (1989): Phosphorylation of vimentin in mitotically selected cells. In vitro cyclic AMP‐independent kinase and calcium‐stimulated phosphatase activities. J. Cell Biol. 108: 67–78.
12. Franke, W. W., Schmid, E., Grund, C., and Geiger, B. (1982): Intermediate filament proteins in nonfilamentous structures: transient disintegration and inclusion of subunit proteins in granular aggregates. Cell 30: 103–113.
13. Geiger, B. (1987): Intermediate filaments. Looking for a function. Nature 329: 392–393.
14. Geisler, N., and Weber, K. (1988): Phosphorylation of desmin in vitro inhibits formation of intermediate filaments: identification of three kinase A sites in the amino terminai head domain. EMBO J. 7: 15–20.
15. Guerriero, V., Jr., Rowley, D. R., and Means., A. R. (1981): Production and characterization of an antibody to myosin light chain kinase and intracellular localization of the enzyme. Cell 27: 449–458.
16. Hartshorne, D. J. (1987): Biochemistry of the contractile process in smooth muscle. In L. R. Johnson, (ed) “ Physiology of the gastrointestinal tract. 2nd Ed. ” New York: Raven Press, pp. 423–482.
17. Hartshorne, D. J., Ishihara, H., Karaki, H., Ozaki, H., Sato, K., Hori, M., and Watabe, S. (1989): Okadaic acid and calyculin A: effects on smooth muscle systems. Adv. Prot. Phosphatases 5: 219–231.
18. Haystead. T. A. J. Sim. A. T. R., Carling. D., Honnor. R. C., Tsuki‐tani, Y., Cohen, P., and Hardie, D. G. (1989): Effects of the tumour promoter okadaic acid on intracellular protein phos‐phorylation and metabolism. Nature 337: 78–81.
19. Herrmann, H., and Wiche, G. (1983): Specific in situ phospho‐ylation of plectin in detergent‐resistant cytoskeletons from cultured chinese hamster ovary cells. J. Biol. Chem. 258: 14610–14618.
20. Hescheler, J., Mieskes, G., Rüegg, J. C., Takai, A., and Trautwein, W. (1988): Effects of a protein phosphatase inhibitor, okadaic acid, on membrane currents of isolated guinea‐pig cardiac myocytes. Pflügers Arch. 412: 248–252.
21. Hollenbeck, P. J., Bershadsky, A. D., Pletjushkina, O. Y., Tint, I. S., and Vasiliev, J. M. (1989): Intermediate filament collapse is an ATP‐dependent and actin‐dependent process. J. Cell Sci. 92: 621–631.
22. Horwitz, B., Kupfer, H., Eshhar, Z., and Geiger, B. (1981): Reorganization of arrays of prekeratin filaments during mitosis. Im‐munofluorescence microscopy with multiclonal and mono‐clonal prekeratin antibodies. Exp. Cell Res. 134: 281–290.
23. Hu, D. H., Kimura, S., and Maruyama, K. (1988): Cross‐linking of native myosin forms oligomers of myosin heavy chain dimers. J. Biochem. (Tokyo) 104: 509–511.
24. Ikebe, M., and Hartshorne, D. J. (1985): Effect of Ca 2+ on the conformation and enzymatic activity of smooth muscle myosin. J. Biol. Chem. 260: 13146–13153.
25. Inagaki, M., Gonda, Y., Matsuyama, M., Nishizawa, K., Nishi, Y., and Sato, C. (1988): Intermediate filament reconstitution in vitro. The role of phosphorylation on the assembly‐disassembly of desmin. J. Biol. Chem. 263: 5970–5978.
26. Ishihara, H., Ozaki, H., Sato, K., Karaki, H., Kato, Y., Watabe, S., Fusetani, N., Hashimoto, K., Uemura, D., and Hartshorne, D. J. (1989a): Calcium‐independent activation of contractile apparatus in smooth muscle by calyculin‐A. J. Pharmacol. Exp. Ther. 250: 388–396.
27. Ishihara, H., Martin, B. L., Brautigan, D. L., Karaki, H., Ozaki, H., Kato, Y., Fusetani, N., Watabe, S., Hashimoto, K., Uemura, D., and Hartshorne, D. J. (1989b): Calyculin A and okadaic acid: inhibitors of protein phosphatase activity. Biochem. Biophys. Res. Commun. 159: 871–877.
28. Ito, M., Pierce, P. R., Allen, R. E., and Hartshorne, D. J. (1989): Effect of monoclonal antibodies on the properties of smooth muscle myosin. Biochemistry 28: 5567–5572.
29. Jones, J. C. R., Goldman, A. E., Yang, H‐Y., and Goldman, R. D. (1985) The organizational fate of intermediate filament networks in two epithelial cell types during mitosis. J. Cell Biol. 100: 93–102.
30. Kato, Y., Fusetani, N., Matsunaga, S., and Hashimoto, K. (1986): Calyculin A, a novel antitumor metabolite from the marine sponge. Discodermia caly. J. Am. Chem. Soc. 108: 2780–2781.
31. Kawamoto, S., and Adelstein, R. S. (1987): Characterization of myosin heavy chains in cultured aorta smooth muscle cells. A comparative study. J. Biol. Chem. 262: 7282–7288.
32. King, S. M., and Witman, G. B. (1988): Structure of the α and β heavy chains of the outer arm dynein from Chlamydomonas flagella. Location of epitopes and protease‐sensitive sites. J. Biol. Chem. 263: 9244–9255.
33. Kitamura, S., Ando, S., Shibata, M., Tanabe, K., Sato, C., and Inagaki, M. (1989): Protein kinase C phosphorylation of desmin at four serine residues within the non‐α‐helical head domain. J. Biol. Chem. 264: 5674–5678.
34. Kuznicki, J. (1986): Phosphorylation of myosin in non‐muscle and smooth muscle cells. FEBS Lett. 204: 169–176.
35. Laemmli, U. K. (1970): Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685.
36. Lane, E. B., Goodman, S. L., and Trejdosiewicz, C. K. (1982): Disruption of the keratin filament network during epithelial cell division. EMBO J 1: 1365–1372.
37. Mittal, B., Sanger, J. M., and Sanger, J. W. (1989): Visualization of intermediate filaments in living cells using fluorescently labeled desmin. Cell Motil. Cytoskeleton 12: 127–138.
38. O'Connor, C. M., Balzer, D. R. Jr., and Lazarides, E. (1979): Phosphorylation of subunit protein of intermediate filaments from chicken muscle and nonmuscle cells. Proc. Natl. Acad. Sci. USA 76: 819–823.
39. O'Connor, C. M., Gard, D. L., and Lazarides, E. (1981): Phosphory‐lation of intermediate filament proteins by cAMP‐dependent protein kinases. Cell 23: 135–143.
40. O'Farrell, P. H. (1975): High resolution two‐dimensional electro‐phoresis of proteins. J. Biol. Chem. 250: 4007–4021.
41. Ozaki, H., Kohama, K., Nonomura, Y., Shibata, S., and Karaki, H. (1987): Direct activation by okadaic acid of the contractile elements in the smooth muscle of guinea‐pig taenia coli. Naunyn Schmiedebergs Arch. Pharmacol. 335: 356–358.
42. Rosen, O. M., and Krebs, E. G. (1981): Protein Phosphorylation. Cold Spring Harbor Conf. Cell Proliferation.
43. Sandoval, I. V., Colaco, C. A. L. S., and Lazardes, E. (1983): Purification of the intermediate filament‐associated protein, syn‐emin, from chicken smooth muscle. Studies on its physico‐chemical properties, interaction with desmin, and phosphory‐lation. J. Biol. Chem. 258: 2568–2576.
44. Spruill, W. A., Zysk, J. R., Tres, L. L., and Kierszenbaum, A. L. (1983): Calcium/calmodulin‐dependent phosphorylation of vimentin in rat Sertoli cells. Proc. Natl. Acad. Sci. USA 80: 760–764.
45. Suganuma, M., Fujiki, H., Suguri, H., Yoshizawa, S., Hirota, M., Nakayasu., M., Ojika, M., Wakamatsu, K., Yamada, K., and Sugimura, T. (1988): Okadaic acid: an additional non‐phorbol‐12‐tetradecanoate‐13‐acetate‐type tumor promoter. Proc. Natl. Acad. Sci. USA 85: 1768–1771.
46. Tachibana, K., Sheuer, P. J., Tsukitani, Y., Kikuchi, H., van Eugene, E., Clardy., J., Gopichand, Y., and Schmitz, F. J. (1981): Okadaic acid, a cytotoxic polyether from two marine sponges of the genus Halichondria. J. Am. Chem. Soc. 103: 2469–2471.
47. Takai, A., Bialojan, C., Troschka, M., and Rüegg, J. C. (1987): Smooth muscle myosin phosphatase inhibition and force enhancement by black sponge toxin. FEBS Lett. 217: 81–84.
48. Towbin, H., Staehelin, T., and Gordon, J. (1979): Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76: 4350–4354.
49. Vikstrom, K. L., Borisy, G. G., and Goldman, R. D. (1989): Dynamic aspects of intermediate filament networks in BHK‐21 cells. Proc. Natl. Acad. Sci. USA 86: 549–553.
50. Walsh, M. P., Hinkins, S., Dabrowska, R., and Haitshorne, D. J. (1983): Smooth muscle myosin light chain kinase. Methods Enzymol. 99: 279–288.
51. Wiche, G., Krepler, R., Artlieb, U., Pltela, R., and Denk, H. (1983): Occurrence and immunolocalization of plectin in tissues. J. Cell Biol. 97: 887–901.
52. Wolfe, F. H., Sathe, S. K., Goll, D. E., Kleese, W. C., Edmunds, T., and Duperret, S. M. (1989): Chicken skeletal muscle has three Ca 2+ ‐dependent proteinases. Biochim. Biophys. Acta 998: 236–250.
53. Yang, H‐Y., Lieska, N., Goldman, A. E., and Goldman, R. D. (1985): A 300,000‐mol‐wt intermediate filament‐associated protein in baby hamster kidney (BHK‐21) cells. J. Cell Biol. 100: 620–631.
54. Zackroff, R. V., and Goldman, R. D. (1979): In vitro assembly of intermediate filaments from baby hamster kidney (BHK‐21) cells. Proc. Natl. Acad. Sci. USA 76: 6226–6230.