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. 1989 Dec;84(6):1693–1700. doi: 10.1172/JCI114351

Molecular basis of cardiac performance. Plasticity of the myocardium generated through protein isoform switches.

B Nadal-Ginard 1, V Mahdavi 1
PMCID: PMC304044  PMID: 2687327

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Selected References

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  1. Alpert N. R., Mulieri L. A. Increased myothermal economy of isometric force generation in compensated cardiac hypertrophy induced by pulmonary artery constriction in the rabbit. A characterization of heat liberation in normal and hypertrophied right ventricular papillary muscles. Circ Res. 1982 Apr;50(4):491–500. doi: 10.1161/01.res.50.4.491. [DOI] [PubMed] [Google Scholar]
  2. Berridge M. J., Irvine R. F. Inositol trisphosphate, a novel second messenger in cellular signal transduction. Nature. 1984 Nov 22;312(5992):315–321. doi: 10.1038/312315a0. [DOI] [PubMed] [Google Scholar]
  3. Brandl C. J., Green N. M., Korczak B., MacLennan D. H. Two Ca2+ ATPase genes: homologies and mechanistic implications of deduced amino acid sequences. Cell. 1986 Feb 28;44(4):597–607. doi: 10.1016/0092-8674(86)90269-2. [DOI] [PubMed] [Google Scholar]
  4. Braun T., Buschhausen-Denker G., Bober E., Tannich E., Arnold H. H. A novel human muscle factor related to but distinct from MyoD1 induces myogenic conversion in 10T1/2 fibroblasts. EMBO J. 1989 Mar;8(3):701–709. doi: 10.1002/j.1460-2075.1989.tb03429.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Breitbart R. E., Andreadis A., Nadal-Ginard B. Alternative splicing: a ubiquitous mechanism for the generation of multiple protein isoforms from single genes. Annu Rev Biochem. 1987;56:467–495. doi: 10.1146/annurev.bi.56.070187.002343. [DOI] [PubMed] [Google Scholar]
  6. Bárány M. ATPase activity of myosin correlated with speed of muscle shortening. J Gen Physiol. 1967 Jul;50(6 Suppl):197–218. doi: 10.1085/jgp.50.6.197. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Chizzonite R. A., Everett A. W., Clark W. A., Jakovcic S., Rabinowitz M., Zak R. Isolation and characterization of two molecular variants of myosin heavy chain from rabbit ventricle. Change in their content during normal growth and after treatment with thyroid hormone. J Biol Chem. 1982 Feb 25;257(4):2056–2065. [PubMed] [Google Scholar]
  8. Chizzonite R. A., Zak R. Regulation of myosin isoenzyme composition in fetal and neonatal rat ventricle by endogenous thyroid hormones. J Biol Chem. 1984 Oct 25;259(20):12628–12632. [PubMed] [Google Scholar]
  9. Czosnek H., Nudel U., Shani M., Barker P. E., Pravtcheva D. D., Ruddle F. H., Yaffe D. The genes coding for the muscle contractile proteins, myosin heavy chain, myosin light chain 2, and skeletal muscle actin are located on three different mouse chromosomes. EMBO J. 1982;1(11):1299–1305. doi: 10.1002/j.1460-2075.1982.tb01314.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Damm K., Thompson C. C., Evans R. M. Protein encoded by v-erbA functions as a thyroid-hormone receptor antagonist. Nature. 1989 Jun 22;339(6226):593–597. doi: 10.1038/339593a0. [DOI] [PubMed] [Google Scholar]
  11. DeCaprio J. A., Ludlow J. W., Figge J., Shew J. Y., Huang C. M., Lee W. H., Marsilio E., Paucha E., Livingston D. M. SV40 large tumor antigen forms a specific complex with the product of the retinoblastoma susceptibility gene. Cell. 1988 Jul 15;54(2):275–283. doi: 10.1016/0092-8674(88)90559-4. [DOI] [PubMed] [Google Scholar]
  12. Evans R. M. The steroid and thyroid hormone receptor superfamily. Science. 1988 May 13;240(4854):889–895. doi: 10.1126/science.3283939. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Everett A. W., Clark W. A., Chizzonite R. A., Zak R. Change in synthesis rates of alpha- and beta-myosin heavy chains in rabbit heart after treatment with thyroid hormone. J Biol Chem. 1983 Feb 25;258(4):2421–2425. [PubMed] [Google Scholar]
  14. Glass C. K., Franco R., Weinberger C., Albert V. R., Evans R. M., Rosenfeld M. G. A c-erb-A binding site in rat growth hormone gene mediates trans-activation by thyroid hormone. Nature. 1987 Oct 22;329(6141):738–741. doi: 10.1038/329738a0. [DOI] [PubMed] [Google Scholar]
  15. Gorza L., Pauletto P., Pessina A. C., Sartore S., Schiaffino S. Isomyosin distribution in normal and pressure-overloaded rat ventricular myocardium. An immunohistochemical study. Circ Res. 1981 Oct;49(4):1003–1009. doi: 10.1161/01.res.49.4.1003. [DOI] [PubMed] [Google Scholar]
  16. Grossman W. Cardiac hypertrophy: useful adaptation or pathologic process? Am J Med. 1980 Oct;69(4):576–584. doi: 10.1016/0002-9343(80)90471-4. [DOI] [PubMed] [Google Scholar]
  17. Guharay F., Sachs F. Stretch-activated single ion channel currents in tissue-cultured embryonic chick skeletal muscle. J Physiol. 1984 Jul;352:685–701. doi: 10.1113/jphysiol.1984.sp015317. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Herrera V. L., Emanuel J. R., Ruiz-Opazo N., Levenson R., Nadal-Ginard B. Three differentially expressed Na,K-ATPase alpha subunit isoforms: structural and functional implications. J Cell Biol. 1987 Oct;105(4):1855–1865. doi: 10.1083/jcb.105.4.1855. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Hirzel H. O., Tuchschmid C. R., Schneider J., Krayenbuehl H. P., Schaub M. C. Relationship between myosin isoenzyme composition, hemodynamics, and myocardial structure in various forms of human cardiac hypertrophy. Circ Res. 1985 Nov;57(5):729–740. doi: 10.1161/01.res.57.5.729. [DOI] [PubMed] [Google Scholar]
  20. Hoh J. F., McGrath P. A., Hale P. T. Electrophoretic analysis of multiple forms of rat cardiac myosin: effects of hypophysectomy and thyroxine replacement. J Mol Cell Cardiol. 1978 Nov;10(11):1053–1076. doi: 10.1016/0022-2828(78)90401-7. [DOI] [PubMed] [Google Scholar]
  21. Honjo T., Habu S. Origin of immune diversity: genetic variation and selection. Annu Rev Biochem. 1985;54:803–830. doi: 10.1146/annurev.bi.54.070185.004103. [DOI] [PubMed] [Google Scholar]
  22. Ingwall J. S., Kramer M. F., Fifer M. A., Lorell B. H., Shemin R., Grossman W., Allen P. D. The creatine kinase system in normal and diseased human myocardium. N Engl J Med. 1985 Oct 24;313(17):1050–1054. doi: 10.1056/NEJM198510243131704. [DOI] [PubMed] [Google Scholar]
  23. Izumo S., Lompré A. M., Matsuoka R., Koren G., Schwartz K., Nadal-Ginard B., Mahdavi V. Myosin heavy chain messenger RNA and protein isoform transitions during cardiac hypertrophy. Interaction between hemodynamic and thyroid hormone-induced signals. J Clin Invest. 1987 Mar;79(3):970–977. doi: 10.1172/JCI112908. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. 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 Feb 7;231(4738):597–600. doi: 10.1126/science.3945800. [DOI] [PubMed] [Google Scholar]
  25. Izumo S., Nadal-Ginard B., Mahdavi V. Protooncogene induction and reprogramming of cardiac gene expression produced by pressure overload. Proc Natl Acad Sci U S A. 1988 Jan;85(2):339–343. doi: 10.1073/pnas.85.2.339. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Johnson P. F., McKnight S. L. Eukaryotic transcriptional regulatory proteins. Annu Rev Biochem. 1989;58:799–839. doi: 10.1146/annurev.bi.58.070189.004055. [DOI] [PubMed] [Google Scholar]
  27. Koenig R. J., Lazar M. A., Hodin R. A., Brent G. A., Larsen P. R., Chin W. W., Moore D. D. Inhibition of thyroid hormone action by a non-hormone binding c-erbA protein generated by alternative mRNA splicing. Nature. 1989 Feb 16;337(6208):659–661. doi: 10.1038/337659a0. [DOI] [PubMed] [Google Scholar]
  28. Lassar A. B., Paterson B. M., Weintraub H. Transfection of a DNA locus that mediates the conversion of 10T1/2 fibroblasts to myoblasts. Cell. 1986 Dec 5;47(5):649–656. doi: 10.1016/0092-8674(86)90507-6. [DOI] [PubMed] [Google Scholar]
  29. Leinwand L. A., Fournier R. E., Nadal-Ginard B., Shows T. B. Multigene family for sarcomeric myosin heavy chain in mouse and human DNA: localization on a single chromosome. Science. 1983 Aug 19;221(4612):766–769. doi: 10.1126/science.6879174. [DOI] [PubMed] [Google Scholar]
  30. Litten R. Z., 3rd, Martin B. J., Low R. B., Alpert N. R. Altered myosin isozyme patterns from pressure-overloaded and thyrotoxic hypertrophied rabbit hearts. Circ Res. 1982 Jun;50(6):856–864. doi: 10.1161/01.res.50.6.856. [DOI] [PubMed] [Google Scholar]
  31. Lompre A. M., Schwartz K., d'Albis A., Lacombe G., Van Thiem N., Swynghedauw B. Myosin isoenzyme redistribution in chronic heart overload. Nature. 1979 Nov 1;282(5734):105–107. doi: 10.1038/282105a0. [DOI] [PubMed] [Google Scholar]
  32. Lompré A. M., Nadal-Ginard B., Mahdavi V. Expression of the cardiac ventricular alpha- and beta-myosin heavy chain genes is developmentally and hormonally regulated. J Biol Chem. 1984 May 25;259(10):6437–6446. [PubMed] [Google Scholar]
  33. MacLennan D. H., Brandl C. J., Korczak B., Green N. M. Amino-acid sequence of a Ca2+ + Mg2+-dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence. Nature. 1985 Aug 22;316(6030):696–700. doi: 10.1038/316696a0. [DOI] [PubMed] [Google Scholar]
  34. Mahdavi V., Chambers A. P., Nadal-Ginard B. Cardiac alpha- and beta-myosin heavy chain genes are organized in tandem. Proc Natl Acad Sci U S A. 1984 May;81(9):2626–2630. doi: 10.1073/pnas.81.9.2626. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Malhotra A., Penpargkul S., Fein F. S., Sonnenblick E. H., Scheuer J. The effect of streptozotocin-induced diabetes in rats on cardiac contractile proteins. Circ Res. 1981 Dec;49(6):1243–1250. doi: 10.1161/01.res.49.6.1243. [DOI] [PubMed] [Google Scholar]
  36. Mercadier J. J., Bouveret P., Gorza L., Schiaffino S., Clark W. A., Zak R., Swynghedauw B., Schwartz K. Myosin isoenzymes in normal and hypertrophied human ventricular myocardium. Circ Res. 1983 Jul;53(1):52–62. doi: 10.1161/01.res.53.1.52. [DOI] [PubMed] [Google Scholar]
  37. Mercadier J. J., Lompré A. M., Wisnewsky C., Samuel J. L., Bercovici J., Swynghedauw B., Schwartz K. Myosin isoenzyme changes in several models of rat cardiac hypertrophy. Circ Res. 1981 Aug;49(2):525–532. doi: 10.1161/01.res.49.2.525. [DOI] [PubMed] [Google Scholar]
  38. Nishizuka Y. The role of protein kinase C in cell surface signal transduction and tumour promotion. Nature. 1984 Apr 19;308(5961):693–698. doi: 10.1038/308693a0. [DOI] [PubMed] [Google Scholar]
  39. Obinata T., Maruyama K., Sugita H., Kohama K., Ebashi S. Dynamic aspects of structural proteins in vertebrate skeletal muscle. Muscle Nerve. 1981 Nov-Dec;4(6):456–488. doi: 10.1002/mus.880040604. [DOI] [PubMed] [Google Scholar]
  40. Pette D., Vrbová G. Neural control of phenotypic expression in mammalian muscle fibers. Muscle Nerve. 1985 Oct;8(8):676–689. doi: 10.1002/mus.880080810. [DOI] [PubMed] [Google Scholar]
  41. Pope B., Hoh J. F., Weeds A. The ATPase activities of rat cardiac myosin isoenzymes. FEBS Lett. 1980 Sep 8;118(2):205–208. doi: 10.1016/0014-5793(80)80219-5. [DOI] [PubMed] [Google Scholar]
  42. Rothman J. E. Signal-peptide recognition. GTP and methionine bristles. Nature. 1989 Aug 10;340(6233):433–434. doi: 10.1038/340433a0. [DOI] [PubMed] [Google Scholar]
  43. Ruoslahti E., Pihko H., Seppälä M. Alpha-fetoprotein: immunochemical purification and chemical properties. Expression in normal state and in malignant and non-malignant liver disease. Transplant Rev. 1974;20(0):38–60. doi: 10.1111/j.1600-065x.1974.tb00140.x. [DOI] [PubMed] [Google Scholar]
  44. Saez L. J., Gianola K. M., McNally E. M., Feghali R., Eddy R., Shows T. B., Leinwand L. A. Human cardiac myosin heavy chain genes and their linkage in the genome. Nucleic Acids Res. 1987 Jul 10;15(13):5443–5459. doi: 10.1093/nar/15.13.5443. [DOI] [PMC free article] [PubMed] [Google Scholar]
  45. Sap J., Muñoz A., Damm K., Goldberg Y., Ghysdael J., Leutz A., Beug H., Vennström B. The c-erb-A protein is a high-affinity receptor for thyroid hormone. Nature. 1986 Dec 18;324(6098):635–640. doi: 10.1038/324635a0. [DOI] [PubMed] [Google Scholar]
  46. Scheuer J., Malhotra A., Hirsch C., Capasso J., Schaible T. F. Physiologic cardiac hypertrophy corrects contractile protein abnormalities associated with pathologic hypertrophy in rats. J Clin Invest. 1982 Dec;70(6):1300–1305. doi: 10.1172/JCI110729. [DOI] [PMC free article] [PubMed] [Google Scholar]
  47. Schwartz K., Lecarpentier Y., Martin J. L., Lompré A. M., Mercadier J. J., Swynghedauw B. Myosin isoenzymic distribution correlates with speed of myocardial contraction. J Mol Cell Cardiol. 1981 Dec;13(12):1071–1075. doi: 10.1016/0022-2828(81)90297-2. [DOI] [PubMed] [Google Scholar]
  48. Schwartz K., Lecarpentier Y., Martin J. L., Lompré A. M., Mercadier J. J., Swynghedauw B. Myosin isoenzymic distribution correlates with speed of myocardial contraction. J Mol Cell Cardiol. 1981 Dec;13(12):1071–1075. doi: 10.1016/0022-2828(81)90297-2. [DOI] [PubMed] [Google Scholar]
  49. Simpson P. Norepinephrine-stimulated hypertrophy of cultured rat myocardial cells is an alpha 1 adrenergic response. J Clin Invest. 1983 Aug;72(2):732–738. doi: 10.1172/JCI111023. [DOI] [PMC free article] [PubMed] [Google Scholar]
  50. Simpson P. Stimulation of hypertrophy of cultured neonatal rat heart cells through an alpha 1-adrenergic receptor and induction of beating through an alpha 1- and beta 1-adrenergic receptor interaction. Evidence for independent regulation of growth and beating. Circ Res. 1985 Jun;56(6):884–894. doi: 10.1161/01.res.56.6.884. [DOI] [PubMed] [Google Scholar]
  51. Siu G., Kronenberg M., Strauss E., Haars R., Mak T. W., Hood L. The structure, rearrangement and expression of D beta gene segments of the murine T-cell antigen receptor. 1984 Sep 27-Oct 3Nature. 311(5984):344–350. doi: 10.1038/311344a0. [DOI] [PubMed] [Google Scholar]
  52. Stiles G. L., Caron M. G., Lefkowitz R. J. Beta-adrenergic receptors: biochemical mechanisms of physiological regulation. Physiol Rev. 1984 Apr;64(2):661–743. doi: 10.1152/physrev.1984.64.2.661. [DOI] [PubMed] [Google Scholar]
  53. Swynghedauw B. Developmental and functional adaptation of contractile proteins in cardiac and skeletal muscles. Physiol Rev. 1986 Jul;66(3):710–771. doi: 10.1152/physrev.1986.66.3.710. [DOI] [PubMed] [Google Scholar]
  54. Thompson C. C., Weinberger C., Lebo R., Evans R. M. Identification of a novel thyroid hormone receptor expressed in the mammalian central nervous system. Science. 1987 Sep 25;237(4822):1610–1614. doi: 10.1126/science.3629259. [DOI] [PubMed] [Google Scholar]
  55. Weinberger C., Thompson C. C., Ong E. S., Lebo R., Gruol D. J., Evans R. M. The c-erb-A gene encodes a thyroid hormone receptor. Nature. 1986 Dec 18;324(6098):641–646. doi: 10.1038/324641a0. [DOI] [PubMed] [Google Scholar]
  56. Whyte P., Buchkovich K. J., Horowitz J. M., Friend S. H., Raybuck M., Weinberg R. A., Harlow E. Association between an oncogene and an anti-oncogene: the adenovirus E1A proteins bind to the retinoblastoma gene product. Nature. 1988 Jul 14;334(6178):124–129. doi: 10.1038/334124a0. [DOI] [PubMed] [Google Scholar]
  57. Wright W. E., Sassoon D. A., Lin V. K. Myogenin, a factor regulating myogenesis, has a domain homologous to MyoD. Cell. 1989 Feb 24;56(4):607–617. doi: 10.1016/0092-8674(89)90583-7. [DOI] [PubMed] [Google Scholar]

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