Acceleration of actin polymerization and rapid microfilament reorganization in cultured hepatocytes by cyclochlorotin, a hepatotoxic cyclic peptide

Toxicon

Volumn 39, Issue 2-3, 2001, Pages 303-308

  Ohmi, Kazuhiro ^a   Enosawa, Shin ^a   Nonomura, Yoshiaki ^b   Tatsuno, Takashi ^c   Ueno, Yoshio ^d  

^a NATIONAL RESEARCH INSTITUTE FOR CHILD HEALTH AND DEVELOPMENT   (Japan)

^b TEIKYO UNIVERSITY   (Japan)

^c INST OF PHYS AND CHEMICAL RESEARCH   (Japan)

^d Department of Pathology   (Japan)

Author keywords

Cyclochlorotin; Hepatocytes; Microfilament

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; CYCLOCHLOROTIN; CYCLOPEPTIDE; GELSOLIN; MYCOTOXIN; PYRENE; UNCLASSIFIED DRUG;

ACTIN POLYMERIZATION; ANIMAL CELL; CONFERENCE PAPER; CONTROLLED STUDY; DOSE TIME EFFECT RELATION; FLUORESCENCE; LIPID BILAYER; LIVER CELL CULTURE; LIVER TOXICITY; MEMBRANE TRANSPORT; MICROFILAMENT; MICROSCOPY; NONHUMAN; PENICILLIUM; PENICILLIUM ISLANDICUM; PRIORITY JOURNAL; PROTEIN FAMILY; RABBIT; VISCOSITY;

PENICILLIUM ISLANDICUM;

EID: 0034598653     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0041-0101(00)00128-8     Document Type: Conference Paper

References (29)

1. Ayscough K.R. In vivo functions of actin-binding proteins. Curr. Opin. Cell Biol. 10:1998;102-111.
2. Cooper J.A., Pollard T.D. Methods to measure actin polymerization. Methods Enzymol. 85:1982;182-210.
3. 2+-regulation of vertebrate smooth muscle thin filaments mediated by an 84 kMr actin-binding protein: purification and characterization of the protein. Biomedical Res. 6:1985;161-173.
4. Ichihara A., Nakamura T., Tanaka K., Tomita Y., Aoyama K., Kato S., Shinno H. Biochemical functions of adult rat hepatocytes in primary culture. Ann. NY Acad. Sci. 349:1980;77-84.
5. Ishii K., Ueno Y. Production of the hepatotoxic chlorine-containing peptide by Penicillium islandicum Sopp. Appl. Microbiol. 26:1973;359-363.
6. Ishii M., Washioka H., Tonosaki A., Toyota T. Regional orientation of actin filaments in the pericanalicular cytoplasm of rat hepatocytes. Gastroenterology. 101:1991;1663-1672.
7. Ito T., Kosugi E., Niwa M., Ishikawa I., Ueno Y. Effects of chloropeptide on liver components and serum enzyme activities in mice. J. Toxicol. Sci. 6:1981;105-113.
8. Kouyama T., Mihashi K. Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labeled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin. Eur. J. Biochem. 114:1981;33-38.
9. Kurokawa H., Fujii W., Ohmi K., Sakurai T., Nonomura Y. Simple and rapid purification of brevin. Biochem. Biophys. Res. Commun. 168:1990;451-457.
10. 2+ signaling: a new view of an old problem. J. Cell Physiol. 180:1999;19-34.
11. Nonomura T., Ito K., Ohmi K., Sakakibara K., Ueno Y. The effects of chloropeptide (cyclochlorotin) on the fragmentation action of the gelsolin family on actin filaments. Natori S., Hashimoto K., Ueno Y. Mycotoxins and Phycotoxins' 88. 1989;91-97 Elsevier, Amsterdam.
12. Okamoto Y., Komatsu I., Kinjo E., Sekine J. Actin and actin-associated proteins of rabbit liver cell. Biochem. (Tokyo). 94:1983;645-653.
13. Pollard T.D., Cooper J.A. Actin and actin-binding proteins. A critical evaluation of mechanisms and functions. Ann. Rev. Biochem. 55:1986;987-1035.
14. Prentki M., Chaponnier C., Jeanrenaud B., Gabbiani G. Actin microfilaments, cell shape, and secretory processes in isolated rat hepatocytes. Effect of phalloidin and cytochalasin D. J. Cell Biol. 81:1979;592-607.
15. Puius Y.A., Mahoney N.M., Almo S.C. The modular structure of actin-regulatory proteins. Curr. Opin. Cell Biol. 10:1998;23-34.
16. Sawamoto K., Takahashi N. Modulation of hepatocyte function by changing the cell shape in primary culture. In Vitro Cell Dev. Biol. Anim. 33:1997;569-574.
17. Schmidt A., Hall M.N. Signaling to the actin cytoskeleton. Ann. Rev. Cell Dev. Biol. 14:1998;305-338.
18. Spudich J.A., Watt S.J. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246:1971;4866-4871.
19. Tranter M.P., Sugrue S.P., Schwartz M.A. Evidence for a direct, nucleotide-sensitive interaction between actin and liver cell membranes. J. Cell Biol. 109:1989;2833-2840.
20. Tranter M.P., Sugrue S.P., Schwartz M.A. Binding of actin to liver cell membranes: the state of membrane-bound actin. J. Cell Biol. 112:1991;891-901.
21. Tsukada N., Phillips M.J. Bile canalicular contraction is coincident with reorganization of pericanalicular filaments and co-localization of actin and myosin-II. J. Histochem. Cytochem. 41:1993;353-363.
22. Ueno Y., Ito T., Hashimoto N., Ueno I. Acute toxicity of chloropeptide, a hepatotoxic metabolite of Penicillium islandicum Sopp. J. Toxicol. Sci. 2:1977;349-362.
23. Ueno Y., Ito T., Matsumoto H., Ueno I. Acute toxicity, tissue distribution and fate of chloropeptide, a hepatotoxin of Penicillium islandicum Sopp. Proc. Jpn. Assoc. Mycotoxicol. 5/6:1977;45-49.
24. Ueno Y., Ito T., Ueno I. Impairments of glycogen and drug metabolisms by chloropeptide, a hepatotoxic mycotoxin of Penicillium islandicum Sopp. J. Toxicol. Sci. 3:1978;11-24.
25. Ueno Y., Ito T., Yoshizawa-Nakaki H., Omata Y., Ichiman K. Cytotoxicity of chloropeptide in isolated hepatocytes and its inactivation by microsomes. J. Toxicol. Sci. 7:1982;111-122.
26. Ueno Y., Tanaka Y., Sato K., Sakakibara K., Tachibana T., Tanaka A. Similarity of chloropeptide to phalloidin in toxicity to isolated hepatocytes. J. Toxicol. Sci. 9:1984;117-130.
27. Uraguchi K., Tatsuno T., Sakaki F., Tsukioka M., Sakai M., Yonemitsu O., Ito H. Isolation of two toxic agents, luteoskyrin and chlorine-containing peptide, from the metabolites of Penicillium islandicum Sopp. Jpn. J. Exp. Med. 31:1961;193-207.
28. Uraguchi K., Saito M., Noguchi Y., Takahashi K., Enomoto M. Chronic toxicity and carcinogenicity in mice of the purified mycotoxins, Luteoskyrin and cyclochlorotine. Food Cosmet. Toxicol. 10:1972;193-207.
29. Yoshioka, H., Nakatsu, K., Sato, K., Tatsuno, T., 1972. The molecular structure of cyclochlorotine, a toxic chlorine-containing peptide. Chem. Lett., 1319-1322.