Electrophoretic separation and quantitation of cardiac myosin heavy chain isoforms in eight mammalian species

American Journal of Physiology - Heart and Circulatory Physiology

Volumn 274, Issue 3 43-3, 1998, Pages

  Reiser, Peter J ^a   Kline, William O ^a  

^a OHIO STATE UNIVERSITY   (United States)

Author keywords

Contractile proteins; Heart; Isoenzymes; Myocardium; Sodium dodecyl sulfate polyacrylamide gel electrophoresis

Indexed keywords

MYOSIN HEAVY CHAIN;

ANIMAL TISSUE; ARTICLE; BABOON; DOG; GEL ELECTROPHORESIS; GUINEA PIG; HEART; HUMAN; HUMAN TISSUE; MAMMAL; MOUSE; PRIORITY JOURNAL; PROTEIN DETERMINATION; QUANTITATIVE ASSAY; RABBIT; RAT; SPECIES DIFFERENCE; SWINE;

EID: 0031893185     PISSN: 03636135     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpheart.1998.274.3.h1048     Document Type: Article

References (32)

1. Aigner, S., B. Gohlsch, N. Hamalainen, R. S. Staron, A. Uber, U. Wehrle, and D. Pette. Fast myosin heavy chain diversity in skeletal muscles of the rabbit: heavy chain IId, not IIb, predominates. Eur. J. Biochem. 211: 367-372, 1993.
2. Alpert, N. R., L. A. Mulieri, and R. Z. Litten. Functional significance of altered myosin adenosine triphosphatase activity in enlarged hearts. Am. J. Cardiol. 44: 947-953, 1979.
3. Blough, E. R., E. R. Rennie, F. Zhang, and P. J. Reiser. Enhanced electrophoretic separation and resolution of myosin heavy chains in mammalian and avian skeletal muscles. Anal. Biochem. 233: 31-35, 1996.
4. Clark, W. A., R. A. Chizzonite, A. W. Everett, M. Rabinowitz, and R. Zak. Species correlations between cardiac isomyosins. A comparison of electrophoretic and immunological properties. J. Biol. Chem. 257: 5449-5454, 1982.
5. Cuda, G., E. Pate, R. Cooke, and J. R. Sellers. In vitro actin filament sliding velocities produced by mixtures of different types of myosin. Biophys. J. 72: 1767-1779, 1997.
6. Cummins, P., and S. J. Lambert. Myosin transitions in the bovine and human heart: a developmental and anatomical study of the heavy and light chain subunits in the atrium and ventricle. Circ. Res. 58: 846-858, 1986.
7. Eble, D. M., J. D. Walker, R. Mukherjee, A. M. Samarel, and F. G. Spinale. Myosin heavy chain synthesis is increased in a rabbit model of heart failure. Am. J. Physiol. 272 (Heart Circ. Physiol. 41): H969-H978, 1997.
8. Esser, K. A., M. O. Boluyt, and T. P. White. Separation of cardiac myosin heavy chains by gradient SDS-PAGE. Am. J. Physiol. 255 (Heart Circ. Physiol. 24): H659-H663, 1988.
9. Everett, A. W., G. Prior, W. A. Clark, and R. Zak. Quantitation of myosin in muscle. Anal. Biochem. 130: 102-107, 1983.
10. Fritz, J. D., D. R. Swartz, and M. L. Greaser. Factors affecting polyacrylamide gel electrophoresis and electroblotting of high-molecular-weight myofibrillar proteins. Anal. Biochem. 180: 205-210, 1989.
11. Giulian, G. G., R. L. Moss, and M. L. Greaser. Improved methodology for analysis and quantitation of proteins on one-dimensional silver-stained slab gels. Anal. Biochem. 129: 277-287, 1983.
12. Hames, B. D. Gel Electrophoresis of Proteins: A Practical Approach (2nd ed.), edited by B. D. Hames and D. Rickwood. Oxford, UK: Oxford University, 1990, p. 1-148.
13. Hamilton, N., and C. D. Ianuzzo. Contractile and calcium regulating capacities of myocardia of different sized mammals scale with resting heart rate. Mol. Cell. Biochem. 106: 133-141, 1991.
14. Harris, D. E., S. S. Work, R. K. Wright, N. R. Alpert, and D. M. Warshaw. Smooth, cardiac and skeletal muscle myosin force and motion generation assessed by cross-bridge interactions in vitro. J. Muscle Res. Cell Motil. 15: 11-19, 1994.
15. Hirzel, H. O., C. R. Tuchschmid, J. Schneider, H. P. Krayenbuehl, and M. C. Schaub. Relationship between myosin isoenzyme composition, hemodynamics, and myocardial structure in various forms of human cardiac hypertrophy. Circ. Res. 57: 729-740, 1985.
16. 2+] and pH in rat skinned cardiac myocytes. Am. J. Physiol. 269 (Heart Circ. Physiol. 38): H1656-H1663, 1995.
17. Hoh, J. F. Y., G. P. S. Yeoh, M. A. W. Thomas, and L. Higginbottom. Structural differences in the heavy chains of rat ventricular myosin isoenzymes. FEBS Lett. 97: 330-334, 1979.
18. Li, P., P. A. Hofmann, B. Li, A. Malhotra, W. Cheng, E. H. Sonnenblick, L. G. Meggs, and P. Anversa. Myocardial infarction alters myofilament calcium sensitivity and mechanical behavior of myocytes. Am. J. Physiol. 272 (Heart Circ. Physiol. 41): H360-H370, 1997.
19. Liu, Y.-H., X.-P. Yang, O. Nass, H. N. Sabbah, E. Peterson, and O. A. Carretero. Chronic heart failure induced by coronary artery ligation in Lewis inbred rats. Am. J. Physiol. 272 (Heart Circ. Physiol. 41): H722-H727, 1997.
20. Lompre, A.-M., K. Schwartz, A. d'Albis, G. Lacombe, N. Van Thiem, and B. Swynghedauw. Myosin isoenzyme redistribution in chronic heart overload. Nature 282: 105-107, 1979.
21. McNally, E. M., R. Kraft, M. Bravo-Zehnder, D. A. Taylor, and L. A. Leinwand. Full-length rat alpha and beta cardiac myosin heavy chain sequences. J. Mol. Biol. 210: 665-671, 1989.
22. O'Neill, L., N. J. Holbrook, J. Fargnoli, and E. G. Lakatta. Progressive changes from young adult age to senescence in mRNA for rat cardiac myosin heavy chain genes. Cardioscience 2: 1-5, 1991.
23. Parry, D. J., and D. Zardini. Characterization of IIx fibres in mouse muscles. In: The Dynamic State of Muscle Fibers, edited by D. Pette. Berlin, Germany: de Gruyter, 1990, p. 343-354.
24. Reiser, P. J., W. O. Kline, and P. L. Vaghy. Induction of neuronal type nitric oxide synthase in skeletal muscle by chronic electrical stimulation in vivo. J. Appl. Physiol. 82: 1250-1255, 1997.
25. Rennie, E. R., and P. J. Reiser. Altered molecular free mobility of proteins during electrophoresis in the presence of glycerol: conditions for enhanced separation of tropomyosin and troponin subunits (Abstract). Biophys. J. 70: A48, 1996.
26. Samarel, A. M., and G. L. Engelmann. Contractile activity modulates myosin heavy chain-β expression in neonatal rat heart cells. Am. J. Physiol. 261 (Heart Circ. Physiol. 30): H1067-H1077, 1991.
27. Schiaffino, S., and C. Reggiani. Molecular diversity of myofibrillar proteins: gene regulation and functional significance. Physiol. Rev. 76: 371-423, 1996.
28. Syrovy, I., and Z. Hodny. Staining and quantification of proteins separated by polyacrylamide gel eletrophoresis. J. Chromatogr. A 569: 175-196, 1991.
29. Talmadge, R. J., and R. R. Roy. Electrophoretic separation of rat skeletal muscle myosin heavy-chain isoforms. J. Appl. Physiol. 75: 2337-2340, 1993.
30. VanBuren, P., D. E. Harris, N. R. Alpert, and D. M. Warshaw. Cardiac V1 and V3 myosins differ in their hydrolytic and mechanical activities in vitro. Circ. Res. 77: 439-444, 1995.
31. Weiss, A., and L. A. Leinwand. The mammalian myosin heavy chain gene family. Ann. Rev. Cell Dev. Biol. 12: 417-439, 1996.
32. Wirth, P. J., and A. Romano. Staining methods in gel electrophoresis, including the use of multiple detection methods. J. Chromatogr. A 698: 123-145, 1995.