Electrophoretic mobility of cardiac myosin heavy chain isoforms revisited: application of MALDI TOF/TOF analysis
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
22187528
PubMed Central
PMC3237020
DOI
10.1155/2011/634253
Knihovny.cz E-resources
- MeSH
- Electrophoresis, Polyacrylamide Gel methods MeSH
- Hyperthyroidism metabolism MeSH
- Hypothyroidism metabolism MeSH
- Ventricular Myosins chemistry isolation & purification metabolism MeSH
- Rats MeSH
- Molecular Sequence Data MeSH
- Rats, Inbred Lew MeSH
- Protein Isoforms MeSH
- Amino Acid Sequence MeSH
- Sequence Alignment MeSH
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization methods MeSH
- Myosin Heavy Chains chemistry isolation & purification metabolism MeSH
- Blotting, Western MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Male MeSH
- Female MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Ventricular Myosins MeSH
- Protein Isoforms MeSH
- Myosin Heavy Chains MeSH
The expression of two cardiac myosin heavy chain (MyHC) isoforms in response to the thyroid status was studied in left ventricles (LVs) of Lewis rats. Major MyHC isoform in euthyroid and hyperthyroid LVs had a higher mobility on SDS-PAGE, whereas hypothyroid LVs predominantly contained a MyHC isoform with a lower mobility corresponding to that of the control soleus muscle. By comparing the MyHC profiles obtained under altered thyroid states together with the control soleus, we concluded that MyHCα was represented by the lower band with higher mobility and MyHCβ by the upper band. The identity of these two bands in SDS-PAGE gels was confirmed by western blot and mass spectrometry. Thus, in contrast to the literature data, we found that the MyHCα possessed a higher mobility rate than the MyHCβ isoform. Our data highlighted the importance of the careful identification of the MyHCα and MyHCβ isoforms analyzed by the SDS-PAGE.
See more in PubMed
Mahdavi V, Periasamy M, Nadal-Ginard B. Molecular characterization of two myosin heavy chain genes expressed in the adult heart. Nature. 1982;297(5868):659–664. PubMed
McNally EM, Kraft R, Bravo-Zehnder M, Taylor DA, Leinwand LA. Full-length rat alpha and beta cardiac myosin heavy chain sequences. Comparisons suggest a molecular basis for functional differences. Journal of Molecular Biology. 1989;210(3):665–671. PubMed
Pope B, Hoh JF, Weeds A. The ATPase activities of rat cardiac myosin isoenzymes. FEBS Letters. 1980;118(2):205–208. PubMed
Schwartz K, Lecarpentier Y, Martin JL. Myosin isoenzymic distribution correlates with speed of myocardial contraction. Journal of Molecular and Cellular Cardiology. 1981;13(12):1071–1075. PubMed
Ebrecht G, Rupp H, Jacob R. Alterations of mechanical parameters in chemically skinned preparations of rat myocardium as a function of isoenzyme pattern of myosin. Basic Research in Cardiology. 1982;77(2):220–234. PubMed
Hoh JFY, McGrath PA, Hale PT. Electrophoretic analysis of multiple forms of rat cardiac myosin: effects of hypophysectomy and thyroxine replacement. Journal of Molecular and Cellular Cardiology. 1978;10(11):1053–1076. PubMed
Lompre AM, Mercadier JJ, Wisnewsky C. Species- and age-dependent changes in the relative amounts of cardiac myosin isoenzymes in mammals. Developmental Biology. 1981;84(2):286–290. PubMed
Clark WA, Chizzonite RA, Everett AW. Species correlations between cardiac isomyosins. A comparison of electrophoretic and immunological properties. The Journal of Biological Chemistry. 1982;257(10):5449–5454. PubMed
Swynghedauw B. Developmental and functional adaptation of contractile proteins in cardiac and skeletal muscles. Physiological Reviews. 1986;66(3):710–771. PubMed
Sugiura S, Kobayakawa N, Fujita H, et al. Comparison of unitary displacements and forces between 2 cardiac myosin isoforms by the optical trap technique: molecular basis for cardiac adaptation. Circulation Research. 1998;82(10):1029–1034. PubMed
Vanburen P, Harris DE, Alpert NR, Warshaw DM. Cardiac V1 and V3 myosins differ in their hydrolytic and mechanical activities in vitro. Circulation Research. 1995;77(2):439–444. PubMed
Gupta MP. Factors controlling cardiac myosin-isoform shift during hypertrophy and heart failure. Journal of Molecular and Cellular Cardiology. 2007;43(4):388–403. PubMed PMC
d’Albis A, Pantaloni C, Bechet JJ. An electrophoretic study of native myosin isozymes and of their subunit content. European Journal of Biochemistry. 1979;99(2):261–272. PubMed
Lompre AM, Schwartz K, d’Albis A. Myosin isoenzyme redistribution in chronic heart overload. Nature. 1979;282(5734):105–107. PubMed
Mercadier JJ, Lompre AM, Wisnewsky C. Myosin isoenzymic changes in several models of rat cardiac hypertrophy. Circulation Research. 1981;49(2):525–532. PubMed
Rupp H, Maisch B. Separation of large mammalian ventricular myosin differing in ATPase activity. Canadian Journal of Physiology and Pharmacology. 2007;85(3-4):326–331. PubMed
Esser KA, Boluyt MO, White TP. Separation of cardiac myosin heavy chains by gradient SDS-PAGE. American Journal of Physiology. 1988;255(3):H659–H663. PubMed
Caforio ALP, Grazzini M, Mann JM, et al. Identification of α- and β-cardiac myosin heavy chain isoforms as major autoantigens in dilated cardiomyopathy. Circulation. 1992;85(5):1734–1742. PubMed
Sweitzer NK, Moss RL. Determinants of loaded shortening velocity in single cardiac myocytes permeabilized with α-hemolysin. Circulation Research. 1993;73(6):1150–1162. PubMed
Reiser PJ, Kline WO. Electrophoretic separation and quantitation of cardiac myosin heavy chain isoforms in eight mammalian species. American Journal of Physiology. 1998;274(3):H1048–H1053. PubMed
Mansén A, Yu F, Forrest D, Larsson L, Vennström B. TRs have common and isoform-specific functions in regulation of the cardiac myosin heavy chain genes. Molecular Endocrinology. 2001;15(12):2106–2114. PubMed
Sant’Ana Pereira JAA, Greaser M, Moss RL. Pulse electrophoresis of muscle myosin heavy chains in sodium dodecyl sulfate-polyacrylamide gels. Analytical Biochemistry. 2001;291(2):229–236. PubMed
Piao S, Yu F, Mihm MJ, et al. A simplified method for identification of human cardiac myosin heavy-chain isoforms. Biotechnology and Applied Biochemistry. 2003;37(1):27–30. PubMed
Warren CM, Greaser ML. Method for cardiac myosin heavy chain separation by sodium dodecyl sulfate gel electrophoresis. Analytical Biochemistry. 2003;320(1):149–151. PubMed
Izumo S, Nadal-Ginard B, Mahdavi V. All members of the MHC multigene family respond to thyroid hormone in a highly tissue-specific manner. Science. 1986;231(4738):597–600. PubMed
Lompre AM, Nadal-Ginard B, Mahdavi V. Expression of the cardiac ventricular α- and β-myosin heavy chain genes is developmentally and hormonally regulated. The Journal of Biological Chemistry. 1984;259(10):6437–6446. PubMed
Morkin E, Flink IL, Goldman S. Biochemical and physiologic effects of thyroid hormone on cardiac performance. Progress in Cardiovascular Diseases. 1983;25(5):435–464. PubMed
Morkin E. Control of cardiac myosin heavy chain gene expression. Microscopy Research and Technique. 2000;50(6):522–531. PubMed
Ojamaa K, Klein I. In vivo regulation of recombinant cardiac myosin heavy chain gene expression by thyroid hormone. Endocrinology. 1993;132(3):1002–1006. PubMed
Fletcher AK, Weetman AP. Hypertension and hypothyroidism. Journal of Human Hypertension. 1998;12(2):79–82. PubMed
Stevenson LW. Beta-blockers for stable heart failure. The New England Journal of Medicine. 2002;346(18):1346–1347. PubMed
Danzi S, Klein S, Klein I. Differential regulation of the myosin heavy chain genes α and β in rat atria and ventricles: role of antisense RNA. Thyroid. 2008;18(7):761–768. PubMed PMC
Danzi S, Klein I. Thyroid hormone and the cardiovascular system. Minerva Endocrinologica. 2004;29(3):139–150. PubMed
Kahaly GJ, Dillmann WH. Thyroid hormone action in the heart. Endocrine Reviews. 2005;26(5):704–728. PubMed
Tribulova N, Knezl V, Shainberg A, Seki S, Soukup T. Thyroid hormones and cardiac arrhythmias. Vascular Pharmacology. 2010;52(3-4):102–112. PubMed
Miyata S, Minobe W, Bristow MR, Leinwand LA. Myosin heavy chain isoform expression in the failing and nonfailing human heart. Circulation Research. 2000;86(4):386–390. PubMed
Reiser PJ, Portman MA, Ning XH, Moravec CS. Human cardiac myosin heavy chain isoforms in fetal and failing adult atria and ventricles. American Journal of Physiology. 2001;280(4):H1814–H1820. PubMed
Helmke SM, Yen CY, Cios KJ, et al. Simultaneous quantification of human cardiac alpha- and beta-myosin heavy chain proteins by MALDI-TOF mass spectrometry. Analytical Chemistry. 2004;76(6):1683–1689. PubMed
Soukup T, Zachařová G, Smerdu V, Jirmanová I. Body, heart, thyroid gland and skeletal muscle weight changes in rats with altered thyroid status. Physiological Research. 2001;50(6):619–626. PubMed
Rauchová H, Mráček T, Novák P, Vokurková M, Soukup T. Glycerol-3-phosphate dehydrogenase expression and oxygen consumption in liver mitochondria of female and male rats with chronic alteration of thyroid status. Hormone and Metabolic Research. 2011;43(1):43–47. PubMed
Agbulut O, Li Z, Mouly V, Butler-Browne GS. Analysis of skeletal and cardiac muscle from desmin knock-out and normal mice by high resolution separation of myosin heavy-chain isoforms. Biology of the Cell. 1996;88(3):131–135. PubMed
Choi JK, Yoon SH, Hong HY, Choi DK, Yoo GS. A modified Coomassie blue staining of proteins in polyacrylamide gels with Bismark brown R. Analytical Biochemistry. 1996;236(1):82–84. PubMed
Blum H, Beier H, Gross HJ. Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis. 1987;8:33–99.
Rudnicki MA, Jackowski G, Saggin L, McBurney MW. Actin and myosin expression during development of cardiac muscle from cultured embryonal carcinoma cells. Developmental Biology. 1990;138(2):348–358. PubMed
Rupp H. Differential effect of physical exercise routines on ventricular myosin and peripheral catecholamine stores in normotensive and spontaneously hypertensive rats. Circulation Research. 1989;65(2):370–377. PubMed
Scheuer J, Malhotra A, Hirsch C. Physiologic cardiac hypertrophy corrects contractile protein abnormalities associated with pathologic hypertrophy in rats. The Journal of Clinical Investigation. 1982;70(6):1300–1305. PubMed PMC
Wang B, Ouyang J, Xia Z. Effects of triiodo-thyronine on angiotensin-induced cardiomyocyte hypertrophy: reversal of increased β-myosin heavy chain gene expression. Canadian Journal of Physiology and Pharmacology. 2006;84(8-9):935–941. PubMed
Yazaki Y, Raben MS. Effect of the thyroid state on the enzymatic characteristics of cardiac myosin. A difference in behavior of rat and rabbit cardiac myosin. Circulation Research. 1975;36(1):208–215. PubMed
Thyrum PT, Kritcher EM, Luchi RJ. Effect of l-thyroxine on the primary structure of cardiac myosin. Biochimica et Biophysica Acta. 1970;197(2):335–336. PubMed
Eisenberg BR, Edwards JA, Zak R. Transmural distribution of isomyosin in rabbit ventricle during maturation examined by immunofluorescence and staining for calcium-activated adenosine triphosphatase. Circulation Research. 1985;56(4):548–555. PubMed
Bugaisky LB, Anderson PG, Hall RS, Bishop SP. Differences in myosin isoform expression in the subepicardial and subendocardial myocardium during cardiac hypertrophy in the rat. Circulation Research. 1990;66(4):1127–1132. PubMed
Esber HJ, Menninger FF, Bogden AE. Variation in serum hormone concentrations in different rat strains. Proceedings of the Society for Experimental Biology and Medicine. 1974;146(4):1050–1053. PubMed
Novák P, Zacharová G, Soukup T. Individual, age and sex differences in fiber type composition of slow and fast muscles of adult lewis rats: comparison with other rat strains. Physiological Research. 2010;59(5):783–801. PubMed
Reiser PJ, Wick M, Pretzman CI. Electrophoretic variants of cardiac myosin heavy chain-α in Sprague Dawley rats. Electrophoresis. 2004;25(3):389–395. PubMed