Increased compliance in diaphragm muscle of the cardiomyopathic Syrian hamster

Journal of Applied Physiology

Volumn 85, Issue 5, 1998, Pages 1762-1769

  Coirault, Catherine ^a   Samuel, Jane Lyse ^b   Chemla, Denis ^c   Pourny, Jean Claude ^a   Lambert, Francine ^a   Marotte, Françoise ^b   Lecarpentier, Yves ^c  

^a LABORATOIRE D OPTIQUE APPLIQUÉE   (France)

^b HÔPITAL LARIBOISIÈRE   (France)

^c BICÊTRE HOSPITAL   (France)

Author keywords

Extracellular matrix; Myopathy; Skeletal muscle; Stiffness; Titin

Indexed keywords

COLLAGEN TYPE 1; CONNECTIN; GLYCOPROTEIN; LAMININ;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CARDIOMYOPATHY; CONTROLLED STUDY; DIAPHRAGM MUSCLE; EXTRACELLULAR MATRIX; IMMUNOCYTOCHEMISTRY; MALE; MUSCLE STRETCHING; NONHUMAN; PRIORITY JOURNAL; SARCOMERE LENGTH; STRESS STRAIN RELATIONSHIP; SYRIAN HAMSTER; YOUNG MODULUS;

EID: 0031769060     PISSN: 87507587     EISSN: None     Source Type: Journal    
DOI: 10.1152/jappl.1998.85.5.1762     Document Type: Article

References (36)

1. Al Zaid, N. S., M. S. Al-Adnani, and K. A. Guma. Collagen of the dystrophic hamster diaphragm. Thorax 45: 878-879, 1990.
2. Alnaqeeb, M. A., N. S. Al Zaid, and G. Goldspink. Connective tissue changes and physical properties of developing and ageing skeletal muscle. J. Anat. 139: 677-689, 1984.
3. Borg, T. K., and J. B. Caulfield. Morphology of connective tissue in skeletal muscle. Tissue Cell 12: 197-207, 1980.
4. Braun, N. M. T., N. S. Arora, and D. F. Rochester. Respiratory muscles and pulmonary function in polymyosites and other proximal myopathies. Thorax 38: 616-623, 1983.
5. Burbach, J. A., E. H. Schlenker, and J. L. Johnson. Morphometry, histochemistry, and contractility of dystrophic hamster diaphragm. Am. J. Physiol. 253 (Regulatory Integrative Comp. Physiol. 22): R275-R284, 1987.
6. Campbell, K. P., and S. D. Kahl. Association of dystrophin and an integral membrane glycoprotein. Nature 338: 259-262, 1989.
7. Chemla, D., A. Javouhey-Donzel, I. Suard, V. Maupoil, Y. Lecarpentier, J. C. Pourny, G. Rocquelin, and L. Rochette. Influence of dietary polyunsaturated fatty acids on contractility, lusitropy and compliance of isolated rat myocardium. J. Mol. Cell. Cardiol. 27: 1745-1755, 1995.
8. Chemla, D., E. Scalbert, P. Desché, J. C. Pourny, F. Lambert, and Y. Lecarpentier. Effects of perindopril on myocardial inotropy, lusitropy and economy, and on diaphragmatic contractility in the cardiomyopathic hamster. J. Pharmacol. Exp. Ther. 262: 516-525, 1992.
9. Coirault, C., D. Chemla, N. Péry-Man, I. Suard, and Y. Lecarpentier. Effects of fatigue on force-velocity relation of diaphragm: energetic implications. Am. J. Respir. Crit. Care Med. 151: 123-128, 1995.
10. Coirault, C., D. Chemla, I. Suard, J. C. Pourny, and Y. Lecarpentier. Sarcomere relaxation in hamster diaphragm muscle. J. Appl. Physiol. 81: 858-865, 1996.
11. Coirault, C., D. Chemla, I. Suard, J. C. Pourny, and Y. Lecarpentier. Optimal sarcomere length in mammalian diaphragm. J. Appl. Physiol. 82: 1712-1714, 1997.
12. Ehrig, K., I. Leivo, W. S. Argraves, E. Ruoslahti, and E. Engvall. Merosin, a tissue-specific basement membrane protein, is a laminin-like protein. Proc. Natl. Acad. Sci. USA 87: 3264-3268, 1990.
13. Ervasti, J. M., and K. P. Campbell. Membrane organization of the dystrophin-glycoprotein complex. Cell 66: 1121-1131, 1991.
14. Ervasti, J. M., and K. P. Campbell. A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J. Cell Biol. 122: 809-823, 1993.
15. Fung, Y. C. B. Elasticity of soft tissues in simple elongation. Am. J. Physiol. 213: 1532-1544, 1967.
16. Fürst, D. O., M. Osborn, R. Nave, and K. Weber. The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy. A map of ten nonrepetitive epitopes starting at the Z line extends close to the M line. J. Cell Biol. 106: 1563-1572, 1988.
17. Gosselin, L. E., D. A. Martinez, A. C. Vailas, and G. C. Sieck. Passive length-force properties of senescent diaphragm: relationship with collagen characteristics. J. Appl. Physiol. 76: 2680-2685, 1994.
18. Granzier, H. L. M., and K. Wang. Passive tension and stiffness of vertebrate skeletal and insect flight muscles: the contribution of weak cross-bridges and elastic filaments. Biophys. J. 65: 2141-2159, 1993.
19. Higuchi, L, H. Yamada, H. Fukunaga, H. Iwaki, R. Okubo, M. Nakagawa, M. Osame, S. L. Roberds, T. Shimizu, K. P. Campbell, and M. K. Matsumura. Abnormal expression of laminin suggests disturbance of sarcolemma-extracellular matrix interaction in Japanese patients with autosomal muscular dystrophy deficient in adhalin. J. Clin. Invest. 94: 601-606, 1994.
20. Horowits, R., E. S. Kempner, M. E. Bisher, and R. J. Podolsky. A physiological role for titin and nebulin in skeletal muscle. Nature 323: 160-164, 1986.
21. Ibraghimov-Beskrovnaya, O., J. M. Ervasti, C. J. Leveille, C. A. Slaughter, S. W. Sernett, and K. P. Campbell. Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix. Nature 355: 696-702, 1992.
22. Kovanen, V., H. Suominen, and E. Heikkinen. Mechanical properties of fast and slow skeletal muscles with special reference to collagen and endurance training. J. Biomech. 17: 725-735, 1984.
23. Lecarpentier, Y., C. Coirault, G. Lerebours, P. Desché, E. Scalbert, F. Lambert, and D. Chemla. Effects of angiotensin converting enzyme inhibition on crossbridge properties of diaphragm in cardiomyopathic hamsters of the dilated Bio 53-58 strain. Am. J. Respir. Crit. Care Med. 155: 630-636, 1997.
24. Magid, A., and D. J. Law. Myofibrils bear most of the resting tension in frog skeletal muscle. Science 230: 1280-1282, 1985.
25. Mirsky, I., P. F. Cohn, J. A. Levine, R. Gorlin, M. V. Herman, T. H. Kreulen, and E. H. Sonnenblick. Assessment of left ventricular stiffness in primary myocardial disease and coronary artery disease. Circulation 50: 128-136, 1974.
26. Mirsky, I., and W. W. Parmley. Assessment of passive elastic stiffness for isolated heart muscle and the intact heart. Circ. Res. 33: 233-243, 1973.
27. Moss, R. L., and W. Halpern. Elastic and viscous properties of resting frog skeletal muscle. Biophys. J. 17: 213-228, 1977.
28. Pickering, J. C., and D. R. Boughnet. Fibrosis in the transplanted heart and its relation to donor ischemic time: assessment with polarized light microscopy and digital image analysis. Circulation 81: 949-958, 1990.
29. Ramsey, R. W., and S. F. Street. The isometric length-tension diagram of isolated skeletal muscle fiber of the frog. J. Cell. Comp. Physiol. 15: 11-34, 1940.
30. Roberds, S. L., J. M. Ervasti, R. D. Anderson, K. Ohlendieck, S. D. Kahl, D. Zoloto, and K. P. Campbell. Disruption of the dystrophin-glycoprotein complex in the cardiomyopathic hamster. J. Biol. Chem. 268: 11496-11499, 1993.
31. Robert, V., J.-B. Silvestre, D. Charlemagne, A. Sabri, P. Trouvé, M. Wassef, B. Swynghedauw, and C. Delcayre. Biological determinants of aldosterone-induced cardiac fibrosis in rat. Hypertension 26: 971-978, 1995.
32. Smith, P. E. M. Practical problems in the respiratory care of patients with muscular dystrophy. N. Engl. J. Med. 316: 1197-1204, 1987.
33. Stedman, H. H., H. L. Sweeney, J. B. Shrager, H. C. Maguire, R. A. Panettieri, B. Petrof, M. Narusawa, J. M. Leferovich, J. T. Sladky, and A. M. Kelly. The mdx mouse diaphragm reproduces the degenerative changes of Duchenne muscular dystrophy. Nature 352: 536-539, 1991.
34. Strobeck, J. E., S. M. Factor, A. Bhan, M. Sole, C. C. Liew, F. Fein, and E. H. Sonnenblick. Hereditary and acquired cardiomyopathies in experimental animals: mechanical, biochemical, and structural features. Ann. NY Acad. Sci. 317: 59-88, 1979.
35. Wang, K., R. McCarter, J. Wright, J. Beverly, and R. Ramirez-Mitchell. Regulation of skeletal muscle stiffness and elasticity by titin isoforms: a test of the segmental extension model of resting tension. Proc. Natl. Acad. Sci. USA 88: 7101-7105, 1991.
36. Wang, K., R. McCarter, J. Wright, J. Beverly, and R. Ramirez-Mitchell. Viscoelasticity of the sarcomere matrix of skeletal muscles. The titin-myosin composite filament is a dual-stage molecular spring. J. Biophys. Biochem. Cytol. 64: 1161-1177, 1993.