Calpain II expression is increased by changes in mechanical loading of muscle in vivo

Journal of Cellular Biochemistry

Volumn 64, Issue 1, 1997, Pages 55-66

  Spencer, Melissa J ^a   Lu, Brandon ^a   Tidball, James G ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CALPAIN;

ANIMAL TISSUE; ARTICLE; CELL SHAPE; ENZYME SPECIFICITY; MUSCLE FUNCTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FAMILY; PROTEIN MODIFICATION; SKELETAL MUSCLE; THROMBOCYTE ACTIVATION; WEIGHT BEARING;

NON-PROGRAMMATIC;

ANIMALS; ANTIBODIES; CALPAIN; CYTOPLASM; ENZYME ACTIVATION; IMMUNOBLOTTING; ISOENZYMES; MUSCLE FIBERS; MUSCLE, SKELETAL; POLYMERASE CHAIN REACTION; RATS; RNA, MESSENGER; STRESS, MECHANICAL; UP-REGULATION;

ANIMALIA;

EID: 0031044857     PISSN: 07302312     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4644(199701)64:1<55::AID-JCB9>3.0.CO;2-Z     Document Type: Article

References (68)

1. Balcerzak D, Poussard S, Brustis JJ, Elamrani N, Soriano M, Cottin P, Ducastaing A (1995): An antisense oligodeoxyribonucleotide to m-calpain mRNA inhibits myoblast fusion. J Cell Sci 108:2077-2082.
2. Baracos V, Greenberg RE, Goldberg AL (1986): Influence of calcium and other divalent cations on protein turnover in rat skeletal muscle. Am J Physiol 250(6 Pt 1):E702-710.
3. Baracos VE, Goldberg AL (1986): Maintenance of normal length improves protein balance and energy status in isolated rat skeletal muscles. Am J Physiol 251(4 Pt 1):C588-596.
4. Beckerle MC, O'Halloran T, Burridge K (1986): Demonstration of a relationship between talin and P235, a major substrate of the calcium-dependent protease in platelets. J Cell Biochem 30(3):259-270.
5. Bekastro AN (1993): Skeletal muscle calcium-activated neutral protease (calpain) with exercise. J Appl Physiol 74(3):1381-1386.
6. Booth F (1982): Effect of limb immobilization on skeletal muscle. J Appl Physiol 521113-21118.
7. Booth F, Gollnick P (1983): Effects of disuse on the structure and function of skeletal muscle. Med Sci Sports Exer 15415-15420.
8. Booth FW, Kirby CR (1992): Changes in skeletal muscle gene expression consequent to altered weight bearing. Am J Physiol 262(3 Pt 2):R329-332.
9. Brown N, Crawford C (1993): Structural modifications associated with the change in Ca2+ sensitivity on activation of m-calpain. FEBS Letters 322(1):65-68.
10. Busch WA, Stromer MH, Goll DE, Suzuki A (1972): Calcium-specific removal of Z-lines from rabbit skeletal muscle. J Cell Biol 52:367-381.
11. Chomczynski P, Sacchi N (1987): Single-step method of RNA isolation by acid quanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 162:156-159.
12. Clarke MSF, Khakee R, McNeil PL (1993): Loss of cytoplasmic basic fibroblast growth factor from physiologically wounded myofibers of normal and dystrophic muscle. J Cell Sci 106:121-133.
13. Crawford C, Willis, AC, Gagnon J (1987): The effects of autolysis on the structure of chicken calpain II. Biochem J 248(2):579-588.
14. Croall DE (1989): Proteolytic modification of calcium-dependent protease 1 in erythrocytes treated with ionomycin and calcium. Biochemistry 28(17):6882-6888.
15. Croall DE, DeMartino GN (1990): Regulation of calcium-dependent protease activity in vitro: Clues for determining their physiological functions. In: 'Intracellular Calcium-Dependent Proteolysis.' Boca Raton, FL: CRC Press Inc.
16. Croall DE, DeMartino GN (1991): Calcium-activated neutral protease (calpain) system: structure, function, and regulation. Physiol Rev 71(3):813-847.
17. Croall DE, Slaughter CA, Wortham HS, Skelly CM, DeOgny L, Moomaw CR (1992): Polyclonal antisera specific for the proenzyme form of each calpain. Biochim Biophys Acta 1121(1-2):47-53.
18. DeLuca CI, Davies PL, Samis JA, Elce JS (1993): Molecular cloning and bacterial expression of cDNA for rat calpain II 80 kDa subunit. Biochim Biophys Acta 121681-121693.
19. Desplanches D, Mayer M, Sempore B, Flandrois R (1987): Structural and functional responses to prolonged hindlimb suspension in rat muscle. J Appl Physiol 63558-63563.
20. Duncan CJ (1987): Role of calcium in triggering rapid ultrastructural damage in muscle: A study with chemically skinned fibres. J Cell Sci 87581-87594.
21. Emery AE, Burt D (1980): Intracellular calcium and pathogenesis and antenatal diagnosis of Duchenne muscular dystrophy. Br Med J 280(6211):355-357.
22. Fox JE (1985): Hydrolysis of cytoskeletal proteins by the Ca-dependent protease during platelet activation. Adv Exp Med Biol 192(201):201-213.
23. Fox JE, Reynolds CC, Phillips DR (1983): Calcium-dependent proteolysis occurs during platelet aggregation. J Biol Chem 258(16):9973-9981.
24. Fox JE, Taylor RG, Taffarel M, Boyles JK, Goll DE (1993): Evidence that activation of platelet calpain is induced as a consequence of binding of adhesive ligand to the integrin, glycoprotein IIb-IIIa. J Cell Biol 120(6):1501-1507.
25. Fox JEB, Goll DE, Reynolds CC, Phillips DR (1985): Identification of two proteins (actin-binding protein and p235) that are hydrolyzed by endogenous Ca2+-dependent protease during platelet aggregation. J Biol Chem 260(2): 1060-1066.
26. Furuno K, Goldberg AL (1986): The activation of protein degradation in muscle by calcium or muscle injury does not involve a lysosomal mechanism. Biochem J 237:859-864.
27. Furuno K, Goodman MN, Goldberg A (1990): Different proteolytic systems in the degradation of muscle proteins during denervation atrophy. J Biol Chem 265(15):8550-8557.
28. Goll DE, Dayton WR, Singh I, Robson RM (1991): Studies of the alpha-actinin/actin interaction in the Z-disk by using calpain. J Biol Chem 266(13):8501-8510.
29. Hata A, Ohno S, Suzuki K (1992): Transcriptional activation of the gene for the large subunit of human m-calpain by 12-o-tetradecanoyl-phorbol-13-acetate. FEBS Lett 304(2-3):241-244.
30. Hathaway DR, Werth DK, Haeberle JR (1982): Limited autolysis reduces the calcium requirement of a smooth muscle calcium-activated protease. J Biol Chem 257(15): 9072-9077.
31. Johnson P, Hammer JL (1988): Calpain and calpastatin levels in dystrophic hamster skeletal muscles. Intl J Biochem 20(11):1227-1230.
32. Kasper CE (1995): Sarcolemmal disruption in reloaded atrophic skeletal muscle. J Appl Physiol 79(2):607-614.
33. Komuro I, Kaida T, Shibazaki Y, Kurabayashi M, Katoh Y, Hoh E, Takaku F, Yazaki Y (1990): Stretching cardiac myocytes stimulates protooncogene expression. J Biol Chem 265(7):3595-3598.
34. Llados FT (1985): Muscle damage induced by the ionophore A23187 can be prevented by prostaglandin inhibitors and leupeptin. Experientia 76121-76138.
35. Maki M, Takano E, Osawa T, Ooi T, Murachi T, Hatanaka M (1988): Analysis of structure-function relationship of pig calpastatin by expression of mutated cDNAs in Escherichia coli. J Biol Chem 263(21):10254-10261.
36. Mokri B, Engel A (1975): Duchenne dystrophy: Electron microscopic findings pointing to a basic or early abnormality in the plasma membrane of the muscle fiber. Neurology 251111-251120.
37. Morey-Holton E, Wronski J (1981): Animal models for simulating weightlessness. Physiologist 24(Suppl.)S45-S48.
38. Nishizuka Y (1984): The role of protein kinase C in cell surface signal transduction and tumour promotion. Nature 308(5961):693-698.
39. Nuovo GJ, Becker J, Simsir A, Margiotta M, Khalife G, Shevchuk M (1994): HIV-1 nucleic acids localize to the spermatogonia and their progeny. A study by polymerase chain reaction in situ hybridization. Am J Pathology 144(6):1142-1148.
40. O'Halloran T, Beckerle MC, Burridge K (1985): Identification of talin as a major cytoplasmic protein implicated in platelet activation. Nature 317(6036):449-451.
41. Ogilvie RW, Armstrong RB, Baird KE, Bottoms CL (1988): Lesions in the rat soleus muscle following eccentrically biased exercise. Amer J Anat 182:335-346.
42. Oshimi Y, Miyazaki S (1995): Fas antigen-mediated DNA fragmentation and apoptotic morphologic changes are regulated by elevated cytosolic calcium level. J Immunol 154:599-609.
43. Plopper GE, Mc Namee HP, Dike LE, Bojanowski K, Ingber DE (1995): Convergence of integrin and growth factor receptor signaling pathways within the focal adhesion complex. Mol Biol Cell 6:1349-1365.
44. Reddy MK, Etlinger JD, Rabinowitz M, Fischman DA, Zak R (1975): Removal of Z-lines and alpha-actinin from isolated myofibrils by a calcium-activated neutral protease. J Biol Chem 250(11):4278-4284.
45. Reddy PA, Anandavalli TE, Anandaraj MP (1986): Calcium activated neutral proteases (milli- and micro-CANP) and endogenous CANP inhibitor of muscle in Duchenne muscular dystrophy (DMD). Clin Chim Acta 160(3):281-288.
46. Richard I, Broux O, Allamand V, Fougerousse F, Chiannikulchai N, Bourg N, Brenguier L, Devaud C, Pasturaud P, Roudaut C, Hillaire D, Passos-Bueno M, Jackson CE, Cohen D, Beckmann JS (1995): Mutations in the proteolytic enzyme calpain 3 cause Limb Girdle Muscular Dystrophy Type 2A. Cell 81:27-40.
47. Riley DA, Slocum GR, Bain LW, Sedlak FR, Sowa TE, Mellender JW (1990): Rat hindlimb unloading: soleus histochemistry, ultrastructure, and electromyography. J Appl Physiol 69(1):58-66.
48. Sadoshima J, Izumo S (1993): Mechanical stretch rapidly activates multiple signal transduction pathways in cardiac myocytes: Potential involvement of an autocrine/ paracrine mechanism. EMBO J 12(4):1681-1692.
49. Saido TC, Nagao S, Shiramine M, Tsukaguchi M, Sorimachi H, Murofushi H, Tsuchiya T, Ito H, Suzuki K (1992): Autolytic transition of μ-calpain upon activation as resolved by antibodies distinguishing between the pre- and post-autolysis forms. J Biochem (Tokyo) 111(1):81-86.
50. Saido TC, Suzuki H, Yamazaki H, Tanoue K, Suzuki K (1993): In situ capture of μ-calpain activation in platelets. J Biol Chem 268(10):7422-7426.
51. Sambrook J, Fritsch EF, Maniatis T (1989). Molecular Cloning, A Laboratory Manual. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
52. Samis JA, Back DW, Graham EJ, DeLuca CI, Elce JS (1991): Constitutive expression of calpain II in the rat uterus during pregnancy and involution. Biochem J 276(Pt 2): 293-299.
53. Schollmeyer JE (1986): Possible role of calpain I and calpain II in differentiating muscle. Exp Cell Res 163:413-422.
54. Schollmeyer JE (1986): Role of calcium and calcium activated-protease in myoblast fusion. Exp Cell Res 162:411-422.
55. Schunkert H, Jahn L, Izumo S, Apstein CS, Lorell BH (1991): Localization and regulation of c-fos and c-jun protooncogene induction by systolic wall stress in normal and hypertrophied rat hearts. Proc Natl Acad Sci USA 88(24):11480-11484.
56. Sorimachi H, Imajoh-Ohmi S, Emori Y, Kawasaki H, Ohno S, Minami Y, Suzuki K (1989): Molecular cloning of a novel mammalian calcium-dependent protease distinct from m- and μ-types. J Biol Chem 264(33):20106-20111.
57. Sorimachi H, Suzuki K (1992): Sequence comparison among muscle-specific calpain, p94, and calpain subunits. Biochim Biophys Acta 116:55-62.
58. Spencer MJ, Croall DE, Tidball JG (1995): Calpains are activated in necrotic fibers from mdx dystrophic mice. J Biol Chem 270(18):10909-10914.
59. Squier MKT, Miller ACK, Malkinson AM, Cohen JJ (1994): Calpain activation in apoptosis. J Cell Physiol 159:229-237.
60. St. Pierre B, Tidball JG (1994): Macrophage activation and muscle remodeling at myotendinous junctions after modifications in muscle loading. Am J Pathol 145(6):1463-1471.
61. Takahashi K (1990): Calpain substrate specificity. In: 'Intracellular Calcium Dependent Proteolysis.' Boca Raton, FL: CRC Press.
62. Tidball JG (1995): Inflammatory cell response to acute muscle injury. Med Sci Sports Exer 27(7):1022-1032.
63. Tidball JG, Quan DM (1992): Reduction in myotendinous junction surface area of rats subjected to 4-day space-flight. J Appl Physiol 73(1):59-64.
64. Tischler ME, Rosenberg S, Satarug S, Henriksen EJ, Kirby CR, Tome M, Chase P (1990): Different mechanisms of increased proteolysis in atrophy induced by denervation or unweighting of rat soleus muscle. Metabolism 39(7): 756-763f.
65. Turner PR, Westwood T, Regen CM, Steinhardt RA (1988): Increased protein degradation results from elevated free calcium levels found in muscle from mdx mice. Nature 335(6192):735-738.
66. Vandenburgh HH (1992): Mechanical forces and their second messengers in stimulating cell growth in vitro. Am J Physiol 262(3 Pt 2):R350-355.
67. Yoshimura T, Tsujihata M, Satoh A, Mori M, Hazama R, Kinoshita N, Takashima H, Nagataki S (1986): Ultrastructural study of the effect of calcium ionophore, A23187, on rat muscle. Acta Neuropath 69:184-192.
68. Zeman RJ, Tsuneo K, Kuzee M, Bernstein P, Etlinger JD (1985): Regulation of protein degradation in muscle by calcium. J Biol Chem 260(2):13619-13624.