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The effect of cytochalasin and glutaraldehyde on F-actin filaments containing muscle and non-muscle tropomyosin

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Summary

F-actin filaments are disrupted by the action of cytochalasin and glutaraldehyde. Muscle tropomyosin which is able to polymerize can protect F-actin against fragmentation caused by these two agents. This protective effect does not occur with nonpolymerizable, brain or carboxypeptidase A-treated skeletal muscle tropomyosins. The protection of F-actin against the action of cytochalasin and glutaraldehyde takes place under conditions where the F-actin filaments are saturated with tropomyosin, that is, at a molar ratio of tropomyosin to actin of 1 : 7. It is suggested that nonpolymerizable tropomyosin lacks the protective ability because its binding to F-actin is considerably weaker than the polymerizable tropomyosin and does not saturate all of the binding sites on F-actin.

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References

  • BAILEY, K. (1948) Tropomyosin a new asymmetric protein component of the muscle fibril.Biochem. J. 43, 271–9.

    Google Scholar 

  • BRAY, D. (1979) Cytochalasin action.Nature 282, 671.

    Google Scholar 

  • BRENNER, S. L. & KORN, E. D. (1979) Substoichiometric concentrations of cytochalasin D inhibit actin polymerization.J. biol. Chem. 254, 9982–5.

    Google Scholar 

  • BRENNER, S. L. & KORN, E. D. (1980) The effects of cytochalasins on actin polymerization and actin ATPase provide insights into the mechanism of polymerization.J. biol. Chem. 255, 841–4.

    Google Scholar 

  • COHEN, I. & COHEN, C. A. (1972) Tropomyosin-like protein from human platelets.J. molec. Biol. 68, 383–9.

    Google Scholar 

  • CÔTÉ, G. P., LEWIS, W. G. & SMILLIE, L. B. (1978) Non-polymerizability of platelet tropomyosin and its NH2- and COOH-terminal sequences.FEBS Lett. 91, 237–41.

    Google Scholar 

  • DĄBROWSKA, R., NOWAK, E. & DRABIKOWSKI, W. (1980a) Comparison of functional properties of non-muscle and muscle tropomyosin.Eur. J. Cell Biol. 22, 319.

    Google Scholar 

  • DĄBROWSKA, R., NOWAK, E. & DRABIKOWSKI, W. (1980b) Comparison of some functional properties of non-polymerizable and polymerizable tropomyosin.J. Musc. Res. Cell Motility 1, 466.

    Google Scholar 

  • DĄBROWSKA, R., SOSINSKI, J. & DRABIKOWSKI, W. (1980c) Comparative studies of various kinds of tropomyosin. InPlasticity of Muscle (edited by PETTE, D.), pp. 225–239. Berlin, New York: Walter de Gruyter.

    Google Scholar 

  • DOBROWOLSKI, Z., BARYŁKO, B. & DRABIKOWSKI, W. (1980) Distribution of contractile proteins in brain.J. Musc. Res. Cell Motility 1, 487.

    Google Scholar 

  • DRABIKOWSKI, W., DĄBROWSKA, R. & BARYŁKO, B. (1973) Properties of troponin and its constituents.Acta biochem. polon. 20, 181–99.

    Google Scholar 

  • DRENCKHAHN, D. & GRÖSCHEL-STEWART, U. (1980) Localization of myosin, actin and tropomyosin in rat intestinal epithelium: immunohistochemical studies at the light and electron microscope levels.J. Cell Biol. 86, 475–82.

    Google Scholar 

  • GADASI, H., OPLATKA, A., LAMED, R., HOCHBERG, A. & LOW, W. (1974) Possible uncoupling of the mechanochemical process in the actomyosin system crosslinking of F-actin.Biochim. biophys. Acta 333, 161–8.

    Google Scholar 

  • GORNALL, A. G., BARDAWILL, C. J. & DAVID, M. M. (1949) Determination of serum proteins by means of the biuret reaction.J. biol. Chem. 177, 751–66.

    Google Scholar 

  • GRUMET, M. & LIN, S. (1980) A platelet inhibitor protein with cytochalasin-like activity against actin polymerizationin vitro.Cell 21, 439–44.

    Google Scholar 

  • HARTWIG, J. H. & STOSSEL, T. P. (1979) Cytochalasin B and structure of actin gels.J. molec. Biol. 134, 539–53.

    Google Scholar 

  • HITCHCOCK-De GREGORI, S. E. (1980) Actin assembly.Nature 288, 437–8.

    Google Scholar 

  • ISENBERG, G., AEBI, U. & POLLARD, T. D. (1980) An actin binding protein from Acanthamoeba regulates actin filament polymerization and interactions.Nature 288, 455–9.

    Google Scholar 

  • KITAGAWA, S., DRABIKOWSKI, W. & GERGELY, J. (1968) Exchange and release of the bound nucleotide of F-actin.Archs Biochem. Biophys. 125, 707–14.

    Google Scholar 

  • LAZARIDES, E. (1975) Two general classes of cytoplasmic actin filaments in tissue culture cells: the role of tropomyosin.J. Cell Biol. 65, 549–61.

    Google Scholar 

  • LAZARIDES, E. (1977) Actin, α-actinin and tropomyosin interaction in the structural organization of actin filaments in nonmuscle cells.J. Supramolec. Struct. 5, 531–63.

    Google Scholar 

  • LEHRER, S. S. (1972) The crosslinking of actin and tropomyosin by glutaraldehyde.Biochem. biophys. Res. Commun. 48, 967–76.

    Google Scholar 

  • LIN, D. K., TOBIN, D., GRUMET, M. & LIN, S. (1980) Cytochalasins inhibit nuclei-induced actin polymerization by blocking filament elongation.J. Cell. Biol. 84, 455–60.

    Google Scholar 

  • LÖW, I., DANCKER, P. & WIELAND, T. H. (1975) Stabilization of F-actin by phalloidin; reversal of the destabilizing effect of cytochalasin B.FEBS Lett. 54, 263–65.

    Google Scholar 

  • LOWRY, O. H., ROSEBROUGH, R. J., FARR, A. R. & RANDALL, R. J. (1951) Protein measurements with the Folin reagent.J. biol. Chem. 193, 265–75.

    Google Scholar 

  • MARUYAMA, K., HARTWIG, J. H. & STOSSEL, T. P. (1980) Cytochalasin B and the structure of actin gels. II. Further evidence for the splitting of F-actin by cytochalasin B.Biochim. biophys. Acta 626, 494–500.

    Google Scholar 

  • MAUPIN-SZAMIER, P. & POLLARD, T. D. (1978) Actin filament destruction by osmium tetroxide.J. Cell Biol. 77, 837–52.

    Google Scholar 

  • MIKAWA, T. (1979) ‘Freezing’ of Ca-regulated conformation of reconstituted thin filaments of skeletal muscle.Nature 278, 473.

    Google Scholar 

  • OOSAWA, F., FUJIME, S., ISHIWATA, S. & MIHASHI, K. (1972) Dynamic property of F-actin and thin filament.Cold Spring Harb. Symp. quant. Biol. 23, 277–85.

    Google Scholar 

  • PRÒCHNIEWICZ, E. (1979) Effect of crosslinking by glutaraldehyde on interaction of F-actin with heavy meromyosin.Biochim. biophys. Acta 579, 346–58.

    Google Scholar 

  • SCHLOSS, J. A. & GOLDMAN, R. D. (1980) Microfilaments and tropomyosin of cultured mammalian cells: isolation and characterization.J. Cell Biol. 87, 633–42.

    Google Scholar 

  • SPUDICH, J. A. (1972) Effect of cytochalasin B on actin filaments.Cold Spring Harb. Symp. quant. Biol. 37, 585–93.

    Google Scholar 

  • STRZELECKA-GOŁASZEWSKA, H., JAKUBIAK, M. & DRABIKOWSKI, W. (1975) Changes in the state of actin during superprecipitation of actomyosin.Eur. J. Biochem. 55, 221–30.

    Google Scholar 

  • UENO, H., TAWADA, Y. & OOI, T (1976) Properties of non-polymerizable tropomyosin obtained by carboxy-peptidase A digestion.J. Biochem. 80, 238–90.

    Google Scholar 

  • WEBER, K. & OSBORN, M. (1969) The reliability of molecular weight determinations by dodecyl sulphate-polyacrylamide gel electrophoresis.J. biol. Chem. 244, 4406–10.

    Google Scholar 

  • WEHLAND, J. & WEBER, K. (1980) Distribution of fluorescently labeled actin and tropomyosin after microinjection in living tissue culture cells as observed with TV image intensification.Expl Cell Res. 127, 397–408.

    Google Scholar 

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Dabrowska, R., Próchniewicz, E. & Drabikowski, W. The effect of cytochalasin and glutaraldehyde on F-actin filaments containing muscle and non-muscle tropomyosin. J Muscle Res Cell Motil 4, 83–93 (1983). https://doi.org/10.1007/BF00711959

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