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Inositol trisphosphate and excitation-contraction coupling in skeletal muscle

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Abstract

The role of inositol trisphosphate as a chemical messenger in excitation-contraction coupling is discussed, both in terms of positive and negative results. The evidence presented includes experiments on the effect of inositol trisphosphate in intact and skinned fibers, in calcium release from isolated sarcoplasmic reticulum vesicles, in activation of single calcium release channels incorporated in planar bilayers, and biochemical experiments that have established the presence of all the intermediate steps involved in the metabolism of phosphoinositides, both in intact muscle and in isolated membranes. From these results, it is clear that a role for inositol triphosphate in skeletal muscle function is highly likely; whether this molecule is the physiological messenger in excitation-contraction coupling remains to be established.

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References

  • Adunyah, S. A., and Dean, M. (1986).J. Biol. Chem. 261, 3122–3127.

    Google Scholar 

  • Berridge, M. J. (1987).Annu. Rev. Biochem. 56, 159–193.

    Google Scholar 

  • Berridge, M. J., and Irvine, R. F. (1984).Nature 312, 315–321.

    Google Scholar 

  • Blinks, J. R., Cai, Y. D., and Lee, N. K. M. (1987).J. Physiol. (Lond.) 394, 39P.

    Google Scholar 

  • Campbell, K. P., Knudson, C. M., Imagawa, T., Leung, A. T., Sutko, J. L., Kahi, S. D., Reynolds, C. R., and Madson, L. (1987).J. Biol. Chem. 262, 6460–6463.

    Google Scholar 

  • Carrasco, M. A., Magendzo, K., Jaimovich, E., and Hidalgo, C. (1988).Arch. Biochem. Biophys. 262, 306–366.

    Google Scholar 

  • Di Virgilio, F., Salviati, G., Pozzan, T., and Volpe, P. (1986).EMBO J. 5, 259–262.

    Google Scholar 

  • Donaldson, S. K. (1986).Acta Physiol. Scand. 128, 157–166.

    Google Scholar 

  • Donaldson, S. K., Goldberg, N. D., Walseth, T. F., and Huettemann, D. A. (1987).Biochem. Biophys. Acta 927, 92–99.

    Google Scholar 

  • Donaldson, S. K., Goldberg, N. D., Walseth, T. F., and Huetteman, D. A. (1988).Proc. Natl. Acad. Sci. USA 85, 5749–5753.

    Google Scholar 

  • Fosset, M., Jaimovich, E., Delpont, E., and Lazdunski, M. (1983).J. Biol. Chem. 258, 6089–6091.

    Google Scholar 

  • Franzini-Armstrong, C. (1970).J. Cell. Biol. 47, 488–499.

    Google Scholar 

  • Hannon, J. D., Lee, N. K. M., and Blinks, J. R. (1988).Biophys. J. 53, 607a.

    Google Scholar 

  • Hidalgo, C., Carrasco, M. A., Magendzo, K. and Jaimovich, E. (1986).FEBS Lett. 202, 69–73.

    Google Scholar 

  • Hokin, M. R., and Hokin, L. E. (1953).J. Biol. Chem. 203, 967–977.

    Google Scholar 

  • Hymel, L., Inui, M., Fleischer, S., and Schindler, H. (1988).Proc. Natl. Acad. Sci. USA 85, 441–445.

    Google Scholar 

  • Imagawa, T., Smith, J. S., Coronado, R., and Campbell, K. P. (1987).J. Biol. Chem. 262, 16,636–16,643.

    Google Scholar 

  • Inui, M., Saito, A., and Fleischer, S. (1987).J. Biol. Chem. 262, 1740–1747.

    Google Scholar 

  • Isac, M., Morano, I., and Ruegg, J. C. (1988).Pflugers Archiv. 412, 253–258.

    Google Scholar 

  • Janiak, M. J., Small, D. M., and Shipley, G. G. (1979).J. Biol. Chem. 254, 6068–6078.

    Google Scholar 

  • Lai, F. A., Erickson, H. P., Rousseau, E., Liu, Q. Y., and Meissner, G. (1988).Nature 331, 315–319.

    Google Scholar 

  • Lea, T. J., Griffiths, D. J., Treagar, R. T., and Ashley, C. C. (1986).FEBS Lett. 207, 153–161.

    Google Scholar 

  • Majerus, P. W., Connolly, T. M., Deckmyn, H., Ross, T. S., Bross, T. E., Ishii, H., Bansal, V. S., and Wilson, D. B. (1986).Science 234, 1519–1526.

    Google Scholar 

  • Majerus, P. W., Connolly, T. M., Bansal, V. S., Inhorn, R. C., Ross, T. S., and Lips, D. L. (1988).J. Biol. Chem. 263, 051–3054.

    Google Scholar 

  • Mikos, G. J., and Snow, T. R. (1987).Biochim. Biophys. Acta 927, 256–260.

    Google Scholar 

  • Milani, D., Volpe, P., and Pozzan, T. (1988).Biochem. J. 254, 525–529.

    Google Scholar 

  • Nishizuka, Y. (1984).Nature 308, 693–697.

    Google Scholar 

  • Nosek, T. M., Williams, M. F., Zeigler, J. T., and Godt, R. E. (1986).Am. J. Physiol. 250, C807-C810.

    Google Scholar 

  • Novotny, I., Ziviny, A., and Saleh, F. (1978).Physiol. Bohemoslov. 27, 477–483.

    Google Scholar 

  • Novotny, I., Saleh, F., and Novotna, R. (1983).Gen. Physiol. Biophys. 2, 329–337.

    Google Scholar 

  • Palade, P. (1987).J. Biol. Chem. 262, 6149–6157.

    Google Scholar 

  • Rios, E., and Brum, G. (1987).Nature 325, 717–720.

    Google Scholar 

  • Rojas, E., Nassar-Gentina, V., Luxoro, M., Pollard, M. E., and Carrasco, M. A. (1987).Can. J. Physiol. Pharmacol. 65, 672–680.

    Google Scholar 

  • Rojas, C., Rojas, E., Kukuljan, M., and Jaimovich, E. (1988).Biophys. J. 53, 467a.

    Google Scholar 

  • Rousseau, E., Smith, J. S., Henderson, J. S., and Meissner, G. (1986).Biophys. J. 50, 1009–1014.

    Google Scholar 

  • Salviati, G., Betto, R., Tegazzin, V., and Della Puppa A. (1988).Biophys. J. 53, 332a.

    Google Scholar 

  • Sanchez, J. A., and Stefani, E. (1978).J. Physiol. (Lond.)283, 197–209.

    Google Scholar 

  • Scherer, N. M., and Ferguson, J. E. (1985).Biochem. Biophys. Res. Commun. 316, 347–349.

    Google Scholar 

  • Schwartz, L. M., McCleskey, E. W., and Almers, W. (1985).Nature 314, 747–751.

    Google Scholar 

  • Sekar, M. C., and Hokin, L. E. (1986).J. Membr. Biol. 89, 193–210.

    Google Scholar 

  • Smith, J. S., Coronado, R., and Meissner, G. (1985).Nature 316, 446–449.

    Google Scholar 

  • Smith, J. S., Coronado, R., and Meissner, G. (1986).J. Gen. Physiol. 88, 573–588.

    Google Scholar 

  • Somlyo, A. P., Walker, J. W., Goldman, J. E., Trentham, D. R., Kobayashi, S., Kitazawa, T., and Somlyo, A. V. (1988).Philos. Trans. R. Soc. Lond. Biol. 320, 399–414.

    Google Scholar 

  • Suárez-Isla, B. A., Irribarra, V., Oberhauser, A., Larralde, L., Bull, R., Hidalgo, C., and Jaimovich, E. (1988).Biophys. J. 54, 737–741.

    Google Scholar 

  • Varsanyi, M., Messer, M., Brandt, N. R., and Heilmeyer, L. M. G. (1986).Biochem. Biophys. Res. Commun. 138, 1395–1401.

    Google Scholar 

  • Vergara, J., and Delay, M. (1986).Proc. R. Soc. London. 229, 97–110.

    Google Scholar 

  • Vergara, J., Tsien, R. Y., and Delay, M. (1985).Proc. Natl. Acad. Sci. USA B2, 6352–6356.

    Google Scholar 

  • Vergara, J., Asotra, K., and Delay, M. (1987). InCell Calcium and the Control of Membrane Transport (Mandel L. J., Faton D. G., eds.), Rockefeller University Press, New York, pp. 133–151.

    Google Scholar 

  • Volpe, P., Salviati, G., Di Virgilio, F., and Pozzan, T. (1985).Nature 316, 347–349.

    Google Scholar 

  • Volpe, P., Di Virgilio, F., Pozzan, T., and Salviati, G., (1986).FEBS Lett. 197, 1–4.

    Google Scholar 

  • Walker, J. W., Somlyo, A. V., Goldman, Y. E., Somlyo, A. P., and Trentham, D. A. (1987).Nature 327, 249–252.

    Google Scholar 

  • Whitman, M., Downes, C. P., Keeler, M., Keller, T., and Cantley, L. (1988).Nature 332, 644–646.

    Google Scholar 

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Hidalgo, C., Jaimovich, E. Inositol trisphosphate and excitation-contraction coupling in skeletal muscle. J Bioenerg Biomembr 21, 267–281 (1989). https://doi.org/10.1007/BF00812072

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