Activity of mi and m-calpain in regenerating fast and slow twitch skeletal muscle

• Autorzy: Moraczewski J. , Piekarska E. , Zimowska M. , Sobolewska M.
• Języki publikacji: EN

Abstrakty

EN

Calpains — non-lysosomal intracellular calcium-activated neutral proteinases, form a family consisting of several distinct members. Two of the isoenzymes: ji (calpain I) and m (calpain II) responded differently to the injury during complete regeneration of Extensor digitorum longus (EDL) muscle and partial regeneration of Soleus muscle. In the crushed EDL the level of m-calpain on the 3rd and 7th day of regeneration was higher than in non-operated muscles, whereas the activity of this calpain in injured Soleus decreased. The level of n-calpain in EDL oscillated irregularly during regeneration whereas in Soleus of both injured and contralateral muscles its level rapidly rose. Our results support the hypothesis that m-calpain is involved in the process of fusion of myogenic cells whereas u-calpain plays a significant but indirect role in muscle regeneration.

Słowa kluczowe

EN

myogenic cell; calpain; regeneration; proteinase; skeletal muscle

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 1996
• Tom: 43
• Numer: 4
• Opis fizyczny: p.693-700,fig.

Twórcy

autor

Moraczewski J.

• University of Warsaw, Warsaw, Poland

autor

Piekarska E.

autor

Zimowska M.

autor

Sobolewska M.

Bibliografia

• 1. Campion, D.R. (1984) The muscle satellite cell: A review. Intern. Rev. Cytol. 87, 225-251.
• 2. Grounds, M.D. (1991) Towards understanding skeletal muscle regeneration. Path. Res. Prac. 187,1-22.
• 3. Goll, D.E., Kleese, W.C., Okitani, A., Kurna- moto, T., Cong, J. & Kaprell, H.-P. (1990) Historical background and current status of the Ca2*-dependent proteinase system; in Intra­cellular Calcium-Dependent Proteolysis (Mallgren, R.L. & Murachi, T., eds.) pp. 3-24, CRC Press, Boca Raton, FL.
• 4. Suzuki, K., Saido, T.C. & Shuichi, H. (1992) Modulation of cellular signals by calpain. Ann. NY Acad. Sci. 674,218-227.
• 5. Dayton, W.R., Reville, W.J.,Goll, D.F.&Stromer, M.H. (1976) ACa2" activated protease possibly involved in myofibryllar turnover: Partial characterization of the purified enzyme. Biochemistry 15,2159-2167.
• 6. Siromachi, H., Saido, T.C. & Suzuki, K. (1994) New era of calpain research. Discovery of tissue-specific calpains. FEBS Lett. 343,1-5.
• 7. Suzuki, K. & Ohno, S. (1990) Calcium activated neutral protease structure function relationship and functional implicatons. Cell Struc. Funct. 15, 1-6.
• 8. Sorimachi, H., Toyama-Sorimachi, N., Saido, T.C., Kawsak, H., Sugita, H., Miyasaka, M., Arahata, K., Ishiura, S. & Suzuki, K. (1993) Muscle specific calpain, p94, is degraded by autolysis immediately after translation, resul­ting in disappearance from muscle. J. Biol. Chem. 268,10593-10605.
• 9. Meloni, E. & Pontremoli, S. (1989) The caipains. Trends Neurosci 12,438-^444.
• 10. Johnson, P. (1990) Calpains (intracellular cal­cium-activated cysteine proteinases): Structure- -activity relationships and involvement in normal and abnormal cellular metabolism. Int. /. Biochem. 22, 811-822.
• 11. Kwak, K.B., Chung, S.S., Kim, O.M., Kang, M.S., Ha, D.B. & Chung, C.H. (1993) Increase in level of m-calpain correlates with the elevated cleavage of filamin during myogenic differen­tiation of embryonic muscle cells. Biochim. Biophys. Acta 1175,243-249.
• 12. Kumamoto, T., Kleese, W., Cong, J., Goll, D.E.. Pierce, PR. & Allen, R.E. (1992) Localization of Ca2+-dependent proteinases and their inhibitor in normal, fasted, and denervated rat skeletal muscle. Anat. Rec. 232,60-77.
• 13. Goll, D.E., Thompson, V.F., Taylor. R.G. & Christiansen, J.A. (1992) Role of the calpain system in muscle growth. Biochimie 74,225-237.
• 14. Goll, D.E., Otsuka, Y., Nagainis, A., Shannon, J.D., Sathe, S. & Maguruma, M. (1983) Role of muscle proteinases in maintenance of muscle integrity and mass. /. Food Biochem. 7,137-177.
• 15. Scholmayer, J.E. (1986) Role of Ca2+ and Ca24- -activated proteases in myoblast fusion. Exp. Cell Res. 162,411-422.
• 16. Bassaglia, Y. & Gautron, J. (1995) Fast and slow rat muscles degenerate and regenerate di­fferently after whole crush injury. /. Muscle Res. Cell Motility 16,420-429.
• 17. Savart, M., Belamri, M., Pallet, V. & Ducastaing, A. (1987) Association of calpains 1 and 2 with protein kinase C activities. FEBS Lett. 216,22-26.
• 18. Bradford, M.M. (1976) A rapid and sensitive method for the quantification of microgram quantity of protein utilizing the principle of dye binding. Anal. Chem. 72, 248-254.
• 19. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Mature (London) 227,680-685.
• 20. Spencer, M.J., Croall, D.E. & Tidbald, J.G. (1995) Calpains are activated in necrotic fibers from mdx dystrophic mice. /. Biol. Chem. 270,10909- -10914.
• 21. Moraczewski, J., Martelly, I., Trawicki, W., Pilarska, M., Le Moigne, A.'& Gautron, J. (1990) Activity of protein kinase C during develop­ment in rat skeletal muscle. Neurosci. Res. Commun. 7,183-189.22. Savart, M., Verret, C, Dutaud, D., Touyarot, K., Elamrani, N. & Ducastaing, A. (1995) Isolation and identification of a ji-calpain-protein kinase C a complex in skeletal muscle. FEBS Lett. 359, 60-64.
• 23. Kawashima, S., Hayashi, M., Saito, Y., Kasai, Y. & Imahori, K. (1988) Tissue distribution of calcium-activated neutral proteinases in rat. Biodtim. Biophys. Acta 965,130-135.
• 24. Kim, S.Y., Sainz, R.D. & Lee, Y.-B. (1993) Note on the comparison of calpains I, II and cal pa sta tin activity in two different types of porcine skeletal muscles. Cotnp. Biochem. Physiol. 105A, 235-237.
• 25. Brustis, J.-J., Elamrani, N\, Balcerzak, D., Sawate, A., Soriano, M., Poussard, S., Cottin, P. & Ducastaing, A. (1994) Rat myoblast fusion requires exteriorized m-calpain activity. Eur. /. Cell. Biol. 64, 320-327.
• 26. Moraczewski, J., Piekarska, E., Bonavaud, $., Wosinska, K., Chazud, B. & Barlovatz-Meimon, G. (19%) Different intracellular distribution and activities of fi- and m-calpains during the di­fferentiation of human myogenic cells in culture. C.R Acad. Sci. Paris 319,681-686.
• 27. Elce, J.S., Hasspieler, R. & Boegman, R.J. (1983) Ca2~ activated protease in denervated rat skeletal muscle measured by an immunoassay. Exp. Neurol. 81,320-329.
• 28. Parr, T., Bradsley, R.G., Gilmour, R.S. & Buttery, P.J. (1992) Changes in calpain and calpastatin mRNA induced by p-adrencrgic stimulation of bovine skeletal muscle. Eur. /. Biochem. 208, 333-339.
• 29. Siromachi, H. & Suzuki. K. (1992) Sequence comparison among muscles-specific calpain, p94 and calpain subunits. Biochim. Biophys. Acta 1160,55-62.