Hostname: page-component-669899f699-ggqkh Total loading time: 0 Render date: 2025-04-28T03:21:55.450Z Has data issue: false hasContentIssue false
  • English
  • Français

Expression of myosin heavy chain in neonatal human hearts

Published online by Cambridge University Press:  19 August 2008

Andy Wessels ,
Tom A. Mijnders ,
C. de Gier-de Vries ,
Jacqueline L. M. Vermeulen ,
Szabolcs Vir´gh ,
Wouter H. Lamers  and
Antoon F. M. Moorman
Andy Wessels*
Affiliation:
From the Department of Anatomy and Embryology, University of Amsterdam, Academic Medical Centre, Amsterdam
Tom A. Mijnders
Affiliation:
From the Department of Anatomy and Embryology, University of Amsterdam, Academic Medical Centre, Amsterdam
C. de Gier-de Vries
Affiliation:
From the Department of Anatomy and Embryology, University of Amsterdam, Academic Medical Centre, Amsterdam
Jacqueline L. M. Vermeulen
Affiliation:
From the Department of Anatomy and Embryology, University of Amsterdam, Academic Medical Centre, Amsterdam
Szabolcs Vir´gh
Affiliation:
Department of Pathology, Postgraduate Medical School, Budapest
Wouter H. Lamers
Affiliation:
From the Department of Anatomy and Embryology, University of Amsterdam, Academic Medical Centre, Amsterdam
Antoon F. M. Moorman
Affiliation:
From the Department of Anatomy and Embryology, University of Amsterdam, Academic Medical Centre, Amsterdam
*
Dr. Andy Wessels, Department of Anatomy and Embryology, University of Amsterdam, Academic Medical Centre, Meibergdreef 15, 1105 AZ Amsterdam, The Netherlands
Get access Rights & Permissions [Opens in a new window]

Abstract

We have investigated the spatial distribution of the α and β isoforms of myosin heavy chain in the force-producing ventricular myocardium, the ventricular conduction system and the atrioventricular junctional region of five neonatal human hearts–three born prior to and two at term. The results can be summarized as follows: 1) the force-producing myocardium: in each heart, the β isoform was found to be the predominating isoform, β-negative cells never being observed. Considerable amounts of the α isoform were observed only in those hearts that were obtained from patients dying within the first two weeks of postnatal life. This transient expression is probably correlated with the postnatal increase in levels of circulating thyroid hormone. 2) the ventricular conduction system: in addition to the expression of the β isoform, a strong expression of the α isoform was detected in all the components of the ventricular conduction system in the two full-term hearts. In the preterm hearts, however, this strong expression was mainly restricted to the atrioventricular node and the penetrating atrioventricular bundle. The level of expression of the α isoform in the conduction system of the neonatal hearts, therefore, might reflect the state of maturity of this system at the time of birth. 3) the atrioventricular junctional region: in each heart examined, structures were detected that resembled immunohistochemically and morphologically the atrioventricular node. Although the expression of the isoforms of myosin heavy chain in the conduction system, and in these comparable structures, cannot, as yet, be interpreted with regard to function, these resemblances, coupled with the same developmental background for these structures (they all develop from the so-called “primary ring”) suggest functional affinities during this stage of cardiac development.

Keywords

Myosinneonatalheartconduction systemprimary ringthyroid hormone
Type
Original Articles
Information
Cardiology in the Young , Volume 2 , Issue 4 , October 1992 , pp. 318 - 334
Copyright
Copyright © Cambridge University Press 1992

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

Article purchase

Temporarily unavailable

References

1.Swynghedauw, B. Developmental and functional adaptation of contractile proteins in cardiac and skeletal muscles. Physiol Rev 1986; 66: 710–771.CrossRefGoogle ScholarPubMed
2.Tanigawa, G, Jarcho, JA, Kass, S. A molecular basis for familial hvpertrophic cardiomyopathy: an α/β cardiac myosin heavy chain hybrid gene. Cell 1990; 62: 991–998.CrossRefGoogle ScholarPubMed
3.Reiser, PJ, Greaser, MLMoss, RL. Myosin heavy chain composition of single cells from avian slow skeletal muscle is strongly correlated with velocity of shortening during development. Dev Biol 1988; 129: 400–407.Google Scholar
4.Schwartz, K, Lecarpentier, Y, Martin, JLLompre, AM, Mercadier, JJ, Swynghedauw, B. Myosin isoenzymic distribution corre lates with speed of myocardial contraction. J Mol Cell Cardiol 1981; 13: 1074–1075.CrossRefGoogle Scholar
5.Bouvagnet, P, Leger, J, Pons, F, Dechesrie, C, Leger, JJ. Fiber types and myosin types in human atrial and ventricular myocardium. Circ Res 1984; 55: 794–804.CrossRefGoogle ScholarPubMed
6.Bouvagnet, P, Neveu, S, Montoya, M, Leger, JJ. Developmental changes in the human cardiac isomyosin distribution: an immunohistochemical study using monoclonal antibodies. Circ Res 1987; 61: 329–336.Google Scholar
7.de Groot, IJM, Lamers, WH, Moorman, AFM. Isomyosin expression pattern during rat heart morphogenesis: an immunohistochemical study. Anat Rec 1989; 224: 365–373.Google Scholar
8.Gorza L Mercadier, JJ, Schwartz, K, Thornell, LE, Sartore, S. Schiaffino, S. Myosin types in the human heart: an immunofluorescence study of normal and hypertrophied atrial and ventricular myocardium. Circ Res 1984; 54: 694–702.Google Scholar
9.Wessels, A, Vermeulen, JLM, Viragh, Sz, Moorman, AFM. The ontogenesis of myosin heavy chain isoforms in the developing human heart. Ann NY Acad Sci 1990; 588: 461–464.CrossRefGoogle Scholar
10.Wessels, A, Vermeulen, JLM, Viragh, Sz, Kalman, F, Lamers, WH, Moorman, AFM. Spatial distribution of “tissue specific” antigens in the developing human heart and skeletal muscle: II. An immunohistochemical analysis of myosin heavy chain isoform expression patterns in the embryonic heart. Anat Rec 1991; 229: 355–368.Google Scholar
11.Everett, AW. Isomyosin expression in human heart in early pre- and post-natal life. J Mol Cardiol 1986; 18: 607–615.Google Scholar
12.Lompre, AM, Mercadier, JJ, Wisnewsky, C. Species- and age- dependent changes in the relative amounts of cardiac myosin isoenzymes in mammals. Dev Biol 1981; 84: 286–290.Google Scholar
13.Lompre, AM, Nadal-Ginard, B, Mahdavi, V. Expression of the cardiac ventricular α- and β-myosin heavy chain genes is developmentally and hormonally regulated. J Biol Chem 1984; 259: 6437–6446.CrossRefGoogle Scholar
14.Morano L Gerstner, J, Ruegg, JC, Ganten, U, Ganten, D, Vosberg, HP. Regulation of myosin heavy chain expression in the hearts of hypertensive rats by testosterone. Circ Res 1990; 66: 1585–1590.Google Scholar
15.Sheer, D, Morkin, E. Myosin isoenzyme expression in rat ventricle: effects of thyroid hormone analogs, catecholamines, glucocorticosteroids and high carbohydrate diet. J Pharmac Exp Therapuetics 1984; 229: 872–879.Google Scholar
16.Winegrad, S, Weisberg, A. Isozyme specific modification of myosin ATPase by cAMP in rat heart. Circ Res 1987; 60: 384–392.Google Scholar
17.Bouvagnet, P, Leger, J, Dechesne, CA, Dureau, G, Anoal, M, Leger, JJ. Local changes in myosin types in diseased human atrial myocardium: a quantitative immunofluorescence study. Circulation 1985; 72: 272–279.Google Scholar
18.Dillmann, WH. Diabetes mellitus induces changes in cardiac myosin of the rat. Diabetes 1980; 29: 579–582.Google Scholar
19.Saez, LJ, Gianola, KM, McNally, EM, Eddy, R, Shows, TB, Leinwand, LA. Human cardiac myosin heavy chain genes and their linkage in the genome. Nucl Acids Res 1987; 15: 5443–5459.Google Scholar
20.Geisterfer-Lowrance, AAT, Kass, S, Tanigawa, G. A molecular basis for familial hypotrophic cardiomyopathy: α/β cardiac myosin heavy chain gene missense mutation. Cell 1990; 62: 999–1006.CrossRefGoogle Scholar
21.Bredman, JJ, Wessels, A, Weijs, WA, Korfage, JAM, Soffers, CAS, Moorman, AFM. Demonstration of ‘cardiac-specific’ myosin heavy chain in masticatory muscles of human and rabbit. Histochem J 1991; 23: 160–170.CrossRefGoogle ScholarPubMed
22.Wessels, A, Soffers, CAS, Vermeulen, JLM, Mijnders, TA, Bredman, JJ, Moorman, AFM. Expression of a ‘cardiac-spe cific’ myosin heavy chain in intrafusal fibres of the developing human muscle spindle. In: Marechal, G, Carraro, U (eds). Muscle and Motility. Hampshire:Intercept, Andover, 1990 pp 71–78.Google Scholar
23.Gonzalez-Sanchez, A, Bader, D. Characterization of a myosin heavy chain in the conductive system of the adult and developing chicken heart. J Cell Biol 1985; 100: 270–275.Google Scholar
24.Gorza, L, Sartore, S, Thornell, LE, Schiaffino, S. Myosin types and fiber types in cardiac muscle. III. Nodal conduction tissue. J Cell Biol 1986; 102: 1758–1766.CrossRefGoogle ScholarPubMed
25.Gorza, L, Saggin, L, Sartore, S, Ausoni, S. An embryonic-like myosin heavy chain is transiently expressed in nodal conduction tissue of the rat heart. J Mol Cell Cardiol 1988; 20: 931–941.Google Scholar
26.Komuro, I, Nomoto, K, Sugiyama, T, Kurabayashi, M, Takaku, F, Yazaki, Y. Isolation and characterization of myosin heavy chain isozymes of the bovine conduction system. Circ Res 1987; 61: 859–865.Google Scholar
27.Sanders, E, de Groot, IJM, Geerts, WJC. The local expression of adult chicken heart myosins during development. II. Ventricular conducting tissue. Anat Embryol 1986; 174: 187–193.CrossRefGoogle ScholarPubMed
28.de Groot, IJM, Hardy, GPMA, Sanders, E, Los, JA, Moorman, AFM. The conducting tissue in the adult chicken atria: a histological and immunohistochemical analysis. Anat Embryol 1985; 172: 239–245.Google Scholar
29.Kuro-o, M, Tsuchimochi, H, Ueda, S, Takaku, F, Yazaki, Y. Distribution of cardiac myosin isoenzymes in human conducting systems. J Clin Invest 1986; 77: 340–347.CrossRefGoogle Scholar
30.Wessels, A, Vermeulen, JLM, Verbeek, FJ. Spatial distribution of “tissue-specific” antigens in the developing human heart and skeletal muscle: III. An immunohistochemical analysis of the distribution of the neural tissue antigen GLN in the embryonic heart; implications for the development of the atrioventricular conduction system. Anat Rec 1992; 232: 97–111.CrossRefGoogle Scholar
31.Lamers, WH, Wessels, A, Verbeek, FJ. New findings concerning ventricular septation in the human heart-their implications for maldevelopment. Circulation 1992. [In Press]CrossRefGoogle Scholar
32.Anderson, RH, Davies, MJ, Becker, AE. Atrioventricular ring specialized tissue in the normal heart. EurJ Cardiol 1974; 2: 219–230.Google Scholar
33.Buttrick, PM, Malhotra, A, Brodman, R, McDermott, L, Lam, L. Myosin isoenzyme distribution in overloaded human atrial tissue. Circulation 1986; 74: 477–483.CrossRefGoogle ScholarPubMed
34.Cummins, P, Lambert, SJ. Myosin transitions in the bovine and human heart. Circ Res 1986; 58: 846–858.Google Scholar
35.Hoffman, U, Axmann, C, Palm, N. Atrial and ventricular myosins from human hearts. II. Isoenzyme distnbution after myocardial infarction. Basic Res Cardiol 1987; 82: 359–369.CrossRefGoogle Scholar
36.Hoffman, U, Siegert, E. Atrial and ventricular myosins from human hearts. I. Isoenzyme distnbution during development and in the adult. Basic Res Cardiol 1987; 82: 348–358.CrossRefGoogle Scholar
37.Wessels, A, Vermeulen, JLM, Moorman, AFM, Becker, AE. Immunohistochemical detection of myosin heavy chain isoforms in large sections of whole human hearts. In: Carraro, U (ed). Sarcomeric and Non-sarcomeric Muscles: Basic and Applied Research Prospects for the 90's. Unipress, Padova, 1988, pp 311–316.Google Scholar
38.Wessels, A, Vermeulen, JLM, Viragh, SZ. Spatial distribution of “tissue-specific” antigens in the developing human heart and skeletal muscle. I. An immunohistochemical analysis of creatine kinase isoenzyme expression patterns. Anat Rec 1990; 228: 163–176.Google Scholar
39.Christensen, L, Strange, L. Universal imunoperoxidase staining protocol to optimize the use of polyclonal and monoclonal antibodies. J Histotechnol 1987; 10: 11–15.CrossRefGoogle Scholar
40.Everett, AW, Clark, WA, Chizzonite, RA, Zak, R. Change in synthesis rates of a- and b-myosin synthesis by thyroid hormone. J Biol Chem 1983; 258: 2421–2425.Google Scholar
41.Everett, AW, Sinha, AM, Umeda, PK, Jakovcic, S, Rabinowitz, M, Zak, R. Regulation of myosin synthesis by thyroid hormone. Relative change in the a- and, b-myosin heavy chain mRNA levels in rabbit heart. Biochemistry 1984; 23: 1596–1599.CrossRefGoogle Scholar
42.Hoh, JFY, McGrath, PA, Hale, PT. Electrophoretic analysis of multiple forms of rat cardiac myosin: effects of hypophysectomy and thyroxine replacement. J Mol Cell Cardiol 1978; 10: 1053–1076.Google Scholar
43.Chizzonite, RA, Zak, R. Regulation of myosin isoenzyme composition in fetal and neonatal rat ventricle by endogenous thyroid hormones. J Biol Chem 1984; 259: 12628–12632.CrossRefGoogle ScholarPubMed
44.Kok, JH. Thyroid function in preterm infants with and with out the respiratory distress syndrome. Thesis, University of Amsterdam, Amsterdam, 1985.Google Scholar
45.Walker, A. Developmental aspects of cardiac physiology and morphology. In: Lipshitz, J, Maloney, J, Nimrod, C, Carson, G (eds). Research in Perinatal Medicine (V). Perinatal Development of the Heart and Lung. Perinatology Press, Ithaca, N.Y., 1987, pp 73–82.Google Scholar
46.Anderson, PAW. The fetal left ventricle and the effect of birth. In: Lipshitz, J, Maloney, J, Nimrod, C, Carson, G (eds). Research in Perinatal Medicine (V). Perinatal Development of the Heart and Lung. Perinatology Press, Ithaca, N.Y., 1987, pp 23–48.Google Scholar
47.Anderson, RH, Taylor, IM. Development of atrioventricular specialized tissue in the human heart. Brit Heart J 1972; 34: 1205–1214.Google Scholar
48.Lamers, WH, Moorman, AFM. Neural tissue antigen identifies the evolutionary origin of the left and right ventricle. In: Marechal, G, Carraro, U (eds). Muscle and Motility. Hampshire:Intercept, Andover, 1990, pp 91–98.Google Scholar
49.Moorman, AFM, Wessels, A, Lamers, WH. Cardiac septation revisited: the developing conduction system as a “reference-structure”. In: De Gruyter, Berlin-New York, 1991, pp 195–200.Google ScholarPubMed
50.Kurosawa, H, Becker, AE. Dead-end tracts of the conduction axis. Int J Cardiol 1985; 7: 13–18.CrossRefGoogle ScholarPubMed
51.Truex, RC, Bishof, JK. Conduction system in human hearts with interventricular septal defects. J Thoracic Surg 1958; 35: 421–439.CrossRefGoogle ScholarPubMed
52.Becker, AE, Anderson, RH. Anomalies in the ventricular out flow tracts. In: Becker, AE, Anderson, RH (eds). Cardiac Pathology. Churchill Livingstone, Edinburgh, 1983.Google Scholar
53.Kurosawa, H, Becker, AE. The conduction bundle at the atrioventricular junction: an anatomical study. Eur J Cardiothorac Surg 1989; 3: 283–287.Google Scholar
54.Anderson, RH. The disposition and innervation of atrioventricularring specialized tissue in rats and rabbits. J Anat 1972; 113: 197–211.Google ScholarPubMed
55.Anderson, RH. The disposition, morphology and innervation of cardiac specialized tissue in the guinea-pig. J Anat 1972; 111: 453–468.Google ScholarPubMed