Proteolytic processes underlying molt-induced claw muscle atrophy in decapod crustaceans

American Zoologist

Volumn 39, Issue 3, 1999, Pages 541-551

  Mykles, Donald L ^a  

^a Department of Environmental and Radiological Health Sciences   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 33745974594     PISSN: 00031569     EISSN: None     Source Type: Journal    
DOI: 10.1093/icb/39.3.541     Document Type: Article

References (69)

1. Aizawa, H., H. Kawahara, K. Tanaka, and H. Yokosawa. 1996. Activation of the proteasome during Xenopus egg activation implies a link between proteasome activation and intracellular calcium release. Biochem. Biophys. Res. Commun. 218: 224-228.
2. Arthur, J. S. C., S. Gauthier, and J. S. Elce. 1995. Active site residues in m-calpain: Identification by site-directed mutagenesis. FEBS Lett. 368:397400.
3. Bcrti, P. J. and A. C. Storer. 1995. Alignment/phylogeny of the papain superfamily of cysteine proteases. J. Mol. Biol. 246:273-283.
4. Beyette, J. R., Y. Emori, and D. L. Mykles. 1997. Immunological analysis of two calpain-like Ca2f-dcpcndent proteinases from lobster striated muscles: Relationship to mammalian and Drosophila calpains. Arch. Biochem. Biophys. 337:232-238.
5. Beyette, J. R., J.-S. Ma, and D. L. Mykles. 1993. Purification and autolytic degradation of a calpainlike calcium-dependent proteinase from lobster (Homarus cunericanus) striated muscle. Comp. Biochem. Physiol. 104B:95-99.
6. Beyette, J. R. and D. L. Mykles. 1997. Autolysis and biochemical properties of a lobster muscle calpain-like proteinase. J. Exp. Zool. 277:106-119.
7. Beyette, J. R. and D. L. Mykles. 1999. Crustacean calcium-dependent proteinases. In K. K. W. Wang and P.-W. Yuen (eds.). The pharmacology of calpain. Taylor & Francis, Washington, DC. (In press)
8. Cardozo, C., A. Vinitsky, C. Michaud, and M. Orlowski. 1994. Evidence that the nature of amino acid residues in the P3 position directs substrates to distinct catalytic sites of the pituitary multicatalytic proteinase complex (proteasome). Biochemistry 33:6483-6489.
9. Cong, J., V. F. Thompson, and D. E. Goll. 1993. Effect of monoclonal antibodies specific for the 28-kDa subunit on catalytic properties of the calpains. J. Biol. Chem. 268:25740-25747.
10. Couch, J. 1837. Observations on the process of exuviation in the common crab (Cancer pagurus, Linn.). Mag. Zool. Bot. 1:341-344.
11. Couch, J. 1843. On the process of exuviation and growth in crabs and lobsters, and other British species of stalk-eyed crustacean animals. Ann. Rep. R. Cornwall Polytechnic Soc. 11:1-15.
12. Coux, O., K. Tanaka, and A. L. Goldberg. 1996. Struc-. ture and functions of the 20S and 26S protcasomes. Annu. Rev. Biochem. 65:801-847.
13. Croall, D. E. and G. N. DeMartino. 1991. Calciumactivated neutral protease (calpain) system: Structure, function, and regulation. Physiol. Rev. 71: 813-847.
14. Durica, D. S. and P. M. Hopkins. 1996. Expression of the genes encoding the ecdysteroid and retinoid receptors in regenerating limb tissues from the fiddler crab, Uca pugilator. Gene 171:237-241.
15. El Haj, A. J., S. R. Clarke, P. Harrison, and E. S. Chang. 1996. In vivo muscle protein synthesis rates in the American lobster Homarus americanus during the moult cycle and in response to 20-hydroxyecdysone. J. Exp. Biol. 199:579-585.
16. El Haj, A. J., P. Harrison, and E. S. Chang. 1994. Localization of ecdysteroid receptor immunoreactivity in eyestalk and muscle tissue of the American lobster, Homams americanus. J. Exp. Zool. 270: 343-349.
17. El Haj, A. J., P. Harrison, and N. M. Whiteley. 1992. Regulation of muscle gene expression in Crustacea over the moult cycle. In A. J. El Haj (ed.), Molecular biology of muscle, pp. 151-165. Society for Experimental Biology, Cambridge.
18. El Haj, A. J. and D. F. Houlihan. 1987. In vitro and in vivo protein synthesis rates in a crustacean muscle during the moult cycle. J. Exp. Biol. 127:413426.
19. El Haj, A. J., S. L. Tamone, M. Peake, P. S. Reddy, and E. S. Chang. 1997. An ecdysteroid-responsive gene in a lobster-a potential Crustacean member of the steroid hormone receptor superfamily. Gene 201:127-135.
20. Elce, J. S., C. Hegadorn, J. Simon, and C. Arthur. 1997. Autolysis, Ca2t requirement, and heterodimer stability in m-calpain. J. Biol. Chem. 272: 11268-11275.
21. Emori, Y. and K. Saigo. 1994. Calpain localization changes in coordination with actin-related cytoskeletal changes during early embryonic development of Drosophila. J. Biol. Chem. 269:2513725142.
22. Falkenburg, P.-E., C. Haass, P.-M. Kloetzel, B. Niedel, F. Kopp, L. Kuehn, and B. Dahlmann. 1988. Drosophila small cytoplasmic 19S ribonucleoprotein is homologous to the rat multicatalytic proteinase. Nature 331:190-192.
23. Figueiredo-Pereira, M. E., W.-E. Chen, H.-M. Yuan, and S. Wilk. 1995. A novel chymotrypsin-like component of the multicatalytic proteinase com-plex optimally active at acidic pH. Arch. Biochcm. Biophys. 317:69-78.
24. Godell, C. M., M. E. Smyers, C. S. Eddlcman, M. L. Ballinger, H. M. Fishman, and G. D. Bittner. 1997. Calpain activity promotes the sealing of severed giant axons. Proc. Natl. Acad. Sei. U.S.A. 94: 4751-4756.
25. Grynspan, H, W. R. Griffin, A. Cataldo, S. Katayama, and R. A. Nixon. 1997. Active site-directed antibodies identify calpain II as an early-appearing and pervasive component of neurofibrillary pathology in Alzheimer's disease. Brain Res. 763: 145-158.
26. Guttmann, R. P., J. S. Elce, P. D. Bell, J. C. Isbell, and G. V. W. Johnson. 1997. Oxidation inhibits substrate proteolysis by calpain I but not autolysis. J. Biol. Chem. 272:2005-2012.
27. Ismail, S. Z. M. and D. L. Mykles. 1992. Differential molt-induced atrophy in the dimorphic claws of male fiddler crabs, Uca pugnax. J. Exp. Zool. 263: 18-31'.
28. Kawahara. H. and H. Yokosawa. 1994. Intracellular calcium mobilization regulates the activity of 26 S proteasome during the metaphase-anaphase transition in the ascidian meiotic cell cycle. Dev. Biol. 166:623-633.
29. Kuo, W. N., T. W. Ku, D. L. Jones, and J. Jn-Baptiste. 1995. Calpain immunorcactivity in baker's yeast, lobster and wheat germ. Cytobios 81:175-180.
30. Kuo, W. N., J. B. Jn-Baptiste, R. N. Kanadia, M. L. D. McNabb, L. Zhai, K. Weeks, N. Dopson, and M. C. Chambers. 1996. Immunoreactivities of mcalpain, calpastatin, nitric oxide synthase, myelin basic protein and dynamin II in baker's yeast, wheat germ and lobster tail muscle. Cytobios 87: 251-263.
31. Martins de Sa, C., M.-E Grossi de Sa, O. Akhayat, F. Broders, K. Scherrer, A. Horsch, and H.-P. Schmid. 1986. Prosomes. Ubiquity and inter-spc'cies structural variation. J. Mol. Biol. 187:479493.
32. Mattson, J. M. and D. L. Mykles. 1993. Differential degradation of myofibrillar proteins by four calcium-dependent proteinase activities from lobster muscle. J. Exp. Zool. 265:97-106.
33. Mellgrcn, R. L. and T. Murachi. (eds.) 1990. Intracellular calcium-dependent proteolysis. CRC Press, Boca Raton.
34. Moffett, S. 1987. Muscles proximal to the fracture plane atrophy after limb autotomy in decapod crustaceans. J. Exp. Zool. 244:485-490.
35. 2+activated neutral protease is active in the erythrocyte membrane in its nonautolyzed 80-kDa form. J. Biol. Chem. 269:27992-27995.
36. Mykles, D. L. 1989<7. Purification and characterization of a multicatalytic proteinase from crustacean muscle: Comparison of latent and heat-activated forms. Arch. Biochem. Biophys. 274:216-228.
37. Mykles, D. L. 1989/x High-molecular-weight serine proteinase from lobster muscle that degrades myofibrillar proteins. J. Exp. Zool. 250:244-252.
38. Mykles, D. L. 1990. Calcium-dependent proteolysis in crustacean claw closer muscle maintained in vitro. J. Exp. Zool. 256:16-30.
39. Mykles, D. L. 1992. Getting out of a tight squeezeenzymatic regulation of claw muscle atrophy in molting. Am. Zodl. 32:485-494.
40. Mykles, D. L. 1993. Lobster muscle proteasome and the degradation of myofibrillar proteins. Enzyme Protein 47:220-231.
41. Mykles, D. L. 1996. Differential effects of bovine PA28 on six peptidase activities of the lobster muscle proteasome (multicatalytic proteinase). Arch. Biochem. Biophys. 325:77-81.
42. Myjdes, D. L. 1997n. Crustacean muscle plasticity: Molecular mechanisms determining mass and contractile properties. Comp. Biochem. Physiol. 1176:367-378.
43. Mykles, D. L. 1991b. Biochemical properties of insect and crustacean proteasomes. Mol. Biol. Rep. 24: 133-138.
44. Mykles, D. L. 1998. Intracellular proteinases of invertebrates: Calcium-dependent and proteasome/ ubiquitin-dependent systems. Int. Rev. Cytol. 184: -157-289.
45. Mykles, D. L. and M. F. Haire. 1991. Sodium dodecyl sulfate and heat induce two distinct forms of lobster muscle multicatalytic proteinase: The heat-activated form degrades myofibrillar proteins. Arch. Biochem. Biophys. 288:543-551.
46. Mykles, D. L. and M. F. Haire. 1995. Branched-chainamino-acid-preferring peptidase activity of the lobster multicatalytic proteinase (proteasome) and the degradation of myofibrillar proteins. Biochem. J. 306:285-291.
47. Mykles, D. L. and D. M. Skinner. 1981. Preferential loss of thin filaments during molt-induced atrophy in crab claw muscle. J. Ultrastruct. Res. 75:314325.
48. Mykles, D. L. and D. M. Skinner. 1982a. Crustacean muscles: Atrophy and regeneration during molting. In B. M. Twarog, R. J. C. Levine, and M. M. Dewey (cds.), Basic biology of muscles: A comparative approach, pp. 337-357. Raven Press, New York.
49. Mykles, D. L. and D. M. Skinner. I982b. Molt cycleassociated changes in calcium-dependent proteinase activity that degrades actin and myosin in crustacean muscle. Dcv. Biol. 92:386-397.
50. Mykles, D. L. and D. M. Skinner. 1983. Ca2 -dependent proteolytic activity in crab claw muscle. Effects of inhibitors and specificity for myofibrillar proteins. J. Biol. Chem. 258:10474-10480.
51. Mykles, D. L. and D. M. Skinner. 1985. The role of calcium-dependent proteinase in molt-induced claw muscle atrophy. In E. A. Khairallah, J. S. Bond, and J. W. C. Bird (eds.), Intracellular protein catabolism, pp. 141-150. Alan R. Liss, New York.
52. 2+ and inhibitors. J. Biol. Chem. 261: 9865-9871.
53. Mykles, D. L. and D. M. Skinner. 19906. Atrophy of crustacean somatic muscle and the proteinases that do the job. A review. J. Crustacean Biol. 10: 577-594.
54. Mykles, D. L. and D. M. Skinner. 1990fl. Calciumdependent proteinases in crustaceans. In R. L. Mellgren and T. Murachi (eds.), Intracellular calcium-dependent proteolysis, pp. 139-154. CRC Press, Boca Raton.
55. 2+ levels 'and inhibited by some anticonvulsants. J. Neurobiol. 14:916.
56. Reamur, M. 1718a. Aux observations sur la mue des ecrevisses, donnée dans les mémoires de 1712. Hist. Acad. Roy. Sei. 1718:263-274.
57. Reamur, M. 17186. Sur la mue des ecrevisses. Hist. Acad. Roy. Sei. 1718:22-24.
58. Saido, T. C., S. Nagao, M. Shiramine, M. Tsukaguchi, T. Yoshizawa, H. Sorimachi, H. Ito, T. Tsuchiya, S. Kawashima, and K. Suzuki. 1994. Distinct kinetics of subunit autolysis in mammalian m-calpain activation. FEBS Lett. 346:263-267.
59. Saitoh, Y., H. Yokosavva, K. Takahashi, and S. Ishii. 1989. Purification and characterization of multicatalytic proteinase from eggs of the ascidian Holocynthia roretzi. J. Biochem. (Tokyo) 105:254260.
60. Schmiege, D. L., R. L. Ridgway, and S. B. Moffett. 1992. Ultrastructure of autotomy-induced atrophy of muscles in the crab Carciniis maenas. Can. J. Zool. 70:841-851.
61. Shean, B. S. and D. L. Mykles. 1995. Polyubiquitin in crustacean striated muscle: Increased expression and conjugation during molt-induced claw muscle atrophy. Biochim. Biophys. Acta 1264:312-322.
62. Skinner, D. M. 1965. Amino acid incorporation into protein during the molt cycle of the land crab, Gecarcinus lateral. J. Exp. Zool. 160:225-234.
63. Skinner, D. M. 1966. Breakdown and reformation of somatic muscle during the molt cycle of the land crab, Gecarcinus lateralis. J. Exp. Zool. 163:115124.
64. Skinner, D. M. and J. S. Cook. 1991. New limbs for old: some highlights in the history of regeneration in Crustacea. In C. E. Dinsmore (éd.), A history of regeneration research. Milestones in the evolution of a science, pp. 25-45. Cambridge University Press, Cambridge.
65. Theopold, U., M. Pintér, S. Daffre, Y. Tryselius, P. Friedrich, D. R. Nässei, and D. Hultmark. 1995. CalpA, a Drosophila calpain homolog specifically expressed in a small set of nerve, midgut, and blood cells. Mol. Cell. Biol. 15:824-834.
66. Vinitsky, A., C. Cardozo, L. Sepp-Lorenzino, C. Michaud, and M. Orlowski. 1994. Inhibition of the proteolytic activity of the multicatalytic proteinase complex (proteasome) by substrate-related peptidyl aldehydes. J. Biol. Chem. 269:29860-29866.
67. Wang, J.-H., W.-C. Ma, J.-C. Su, C.-S. Chen, and S.T. Jiang. 1993. Comparison of the properties of mcalpain from tilapia and grass shrimp muscles. J. Agric. Food Chem. 41:1379-1384.
68. West, J. M. 1997. Ultrastructural and contractile activation properties of crustacean muscle fibres over the moult cycle. Comp. Biochem. Physiol. 117B: 333-345.
69. West, J. M., D. C. Humphris, and D. G. Stephenson. 1995. Characterization of ultrastructural and contractile activation properties of crustacean (Clicrax destructor) muscle fibres during claw regeneration and moulting. J. Muscle Res. Cell Motil. 16:267284.