Myofibrillogenesis pp 225-235 | Cite as
The Function of Normal and Familial Hypertrophic Cardiomyopathy-Associated Tropomyosin
Chapter
Abstract
This review will focus on the role of sarcomeric tropomyosin during the assembly and function of thin filaments in striated muscle. Particular emphasis will be devoted to how mutations in familial hypertrophic cardiomyopathy influence these processes. Due to the complex and extensive nature of this topic, this review will not address the role of tropomyosin in the cytoskeleton; however, excellent articles on this topic have addressed this area (Lin et al., 1988; Hegmann et al., 1989).
Keywords
Thin Filament Indirect Flight Muscle Nemaline Myopathy Troponin Complex Mutant Heart
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
Preview
Unable to display preview. Download preview PDF.
References
- Beall, C., Sepanski, M., and Fyrberg, E. 1989. Genetic dissection of Drosophila myofibril formation: effects of actin and myosin heavy chain null alleles. Genes Dev. 3:131–140.PubMedCrossRefGoogle Scholar
- Bing, W., Redwood, C., Purcell, I., Esposito, G., Watkins, H., and Marston, S. 1997. Effects of two hypertrophie cardiomyopathy mutations in a-tropomyosin, asp175asn and glu180gly, on Ca“ regulation of thin filament motility. Biochem. Biophys. Res. Commun. 236:760–764.PubMedCrossRefGoogle Scholar
- Bonne, G., Carrier, L., Richard, P., Hainque, B., and Schwartz, K. 1998. Familial hypertrophic cardiomyopathy. Circ. Res. 83:580–593.PubMedCrossRefGoogle Scholar
- Bottinelli, R., Coviello, D., Redwood, C., Pellegrino, M., Maron, B., Spirito, P., Watkins, H., and Reggiani, C. 1998. A mutant tropomyosin that causes hypertrophic cardiomyopathy is expressed in vivo and associated with an increased calcium sensitivity. Circ. Res. 82:106–115.PubMedCrossRefGoogle Scholar
- Butters, C., Willadsen, K., and Tobacman, L. 1993. Cooperative interactions between adjacent troponin—tropomyosin complexes may be transmitted through the actin filament. J. Biol. Chem. 268:15565–15570.PubMedGoogle Scholar
- Cho, Y., Liu, J., and Hitchcock-DeGregori, S. 1990. The amino terminus of muscle tropomyosin is a major determinant for function. J. Biol. Chem 265:538–545.PubMedGoogle Scholar
- Dufour, C., Weinberger, R., and Gunning, P. 1998. Tropomyosin isoform diversity and neuronal morphogenesis Immunol. Cell Biol 76:424–429.PubMedCrossRefGoogle Scholar
- Fyrberg, E. 1989. Study of contractile and cytoskeletal proteins using Drosophila genetics. Cell Motil. Cytoskel. 14:118–127.CrossRefGoogle Scholar
- Geeves, M. and Lehrer, S. 1994. Dynamics of the muscle thin filament regulatory switch: the size of the cooperative unit. Biophys. J. 67:273–282.PubMedCrossRefGoogle Scholar
- Gunning, P., Hardeman, E., Jeffrey, P., and Weinberger, R. 1998. Creating intracellular structural domains: spatial segregation of actin and tropomyosin isoforms in neurons. Bioessays 20:892–900.PubMedCrossRefGoogle Scholar
- Hammell, R. and Hitchcock-DeGregori, S. 1996. Mapping the functional domains within the carboxyl terminus of a-tropomyosin encoded by the alternatively spliced ninth exon. J. Biol. Chem. 271:4236–4242.PubMedCrossRefGoogle Scholar
- Hegmann, T., Lin, J., and Lin, J. 1989. Probing the role of nonmuscle tropomyosin isoforms in intracellular granule movement by microinjection of monoclonal antibodies. J. Cell Biol. 109:1141–1152.PubMedCrossRefGoogle Scholar
- Izumo, S., Nadal-Ginard, B., and Mandavi, V. 1988. Protooncogene induction and reprogramming of cardiac gene expression produced by pressure overload. Proc. Natl. Acad. Sci. USA 85:339–343.PubMedCrossRefGoogle Scholar
- Karibe, A., Bachinski, L., Arai, A., Tripodi, D., Roberts, R., and Fananapazir, L. 1999. Familial hypertrophic cardiomyopathy caused by a novel alpha-tropomyosin mutation (val95a1a) is associated with mild cardiac hypertrophy but a high incidence of sudden death. Circulation 100 (18):I-619a.Google Scholar
- Kronert, W., Acebes, A., Ferrus, A., and Bernstein, S. 1999. Specific myosin heavy chain mutations suppress troponin I defects in Drosophila muscles. J. Cell Biol. 144:989–1000.Google Scholar
- LaFrance, S., Fransen, M., Dube, D., Stefanu, C., Ray, T., and Lemanski, L. 1993. RNA from normal anterior endoderm/mesoderm-conditioned medium stimulates myofibrillogenesis in developing mutant axolotl hearts. Cell. Mol. Biol. Res. 39:547–560.PubMedGoogle Scholar
- Laing, N., Wilton, S., Akkari, P., Dorosz, S., Boundy, K., Kneebone, C., Blumbergs, P., White, S., Watkins, H., Love, D., and Haan, E. 1995. A mutation in the a tropomyosin gene TPM3 associated with autosomal dominant nemaline myopathy. Nat. Genetics 9:75–79.CrossRefGoogle Scholar
- Landis, C., Back, N., Homsher, E., and Tobacman, L. 1999. Effects of tropomyosin internal detections on thin filament function. J. Biol. Chem. 274:31279–31285.PubMedCrossRefGoogle Scholar
- Lees-Miller, J. and Helfman, D. 1991. The molecular basis for tropomyosin isoform diversity. Bioessays 13:429–437.PubMedCrossRefGoogle Scholar
- Lehrer, S., Golitsina, N., and Geeves, M. 1997. Actin-tropomyosin activation of myosin sub-fragment 1 ATPase and thin filament cooperativity. The role of tropomyosin flexibility and end-to-end interactions. Biochemistry 36:13449–13454.PubMedCrossRefGoogle Scholar
- Lemanski, L. 1973. Morphology of developing heart in cardiac lethal mutant Mexican axolotls, Ambystoma mexicanum. Dey. Biol. 33:312–333.CrossRefGoogle Scholar
- Lemanski, L. 1979. Role of tropomyosin in actin filament formation in embryonic salamander heart cells. J. Cell Biol. 82:227–238.PubMedCrossRefGoogle Scholar
- Lin, J., Hegmann, T., and Lin, J. 1988. Differential localization of tropomyosin isoforms in cultured nonmuscle cells. J. Cell Biol. 107:563–572.PubMedCrossRefGoogle Scholar
- Mak, A. and Smillie, L. 1981. Structural interpretation of the two-site binding of troponin on the muscle thin filament. J. Mol. Biol. 149:541–550.PubMedCrossRefGoogle Scholar
- Malhotra, A. 1994. Role of regulatory proteins (troponin-tropomyosin) in pathologic states. Mol. Cell. Biochem. 135:43–50.PubMedCrossRefGoogle Scholar
- Michele, D., Albayya, F., and Metzger, J. 1999. Direct, convergent hypersensitivity of calcium-activated force generation produced by hypertrophic cardiomyopathy mutant a-tropomyosins in adult cardiac myocytes. Nat. Med. 5:1413–1417.PubMedCrossRefGoogle Scholar
- Muthuchamy, M., Boivin, G., Grupp, I., and Wieczorek, D. 1998.13-tropomyosin overexpression induces severe cardiac abnormalities. J. Mol. Cell. Cardiol. 30:1545–1557.PubMedCrossRefGoogle Scholar
- Muthuchamy, M., Grupp, I., Grupp, G., O’Toole, B., Kier, A., Boivin, G., Neumann, J., and Wieczorek, D. 1995. Molecular and physiological effects of overexpressing striated muscle 13-tropomyosin in the adult murine heart. J. Biol. Chem. 270:30593–30603.PubMedCrossRefGoogle Scholar
- Muthuchamy, M., Pajak, L., Howles, P., Doetschman, T., and Wieczorek, D. 1993. Developmental analysis of tropomyosin gene expression in embryonic stem cells and mouse embryos. Mol. Cell. Biol. 13:3311–3323.PubMedGoogle Scholar
- Muthuchamy, M., Pieples, K., Rethinasamy, P., Hoit, B., Grupp, I., Boivin, G., Wolska, B., Evans, C., Solaro, R., and Wieczorek, D. 1999. Mouse model of a familial hypertrophic cardiomyopathy mutation in a-tropomyosin manifests cardiac dysfunction. Circ. Res. 85:47–56.PubMedCrossRefGoogle Scholar
- Nakajima-Taniguchi, C., Matsui, H., Nagata, S., Kishimoto, T., and Yamauchi-Takihara, K. 1995. Novel missense mutations in a-tropomyosin gene found in Japanese patients with hypertrophic cardiomyopathy. J. Mol. Cell. Cardiol. 27:2053–2058.PubMedCrossRefGoogle Scholar
- Pan, B., Gordon, A., and Luo, Z. 1989. Removal of tropomyosin overlap modifies cooperative binding of myosin S-1 to reconstituted thin filaments of rabbit striated muscle. J. Biol. Chem. 264:8495–8498.PubMedGoogle Scholar
- Pieples, K. and Wieczorek, D.F. 2000. Tropomyosin 3 increases striated muscle isoform diversity. Biochem. 39:8291–8297.CrossRefGoogle Scholar
- Prabhakar, R., Boivin, G., Hoit, B., Arteaga, G., Grupp, I., Solaro, R., and Wieczorek, D. 2000. a-tropomyosin mutation (Glu180Gly) causes familial hypertrophic cardiomyopathy—a mouse model for this disease of the sarcomere. Keystone Symposium: Molecular Biology of the Cardiovascular System, p. 77a, Keystone Pub., Snow Bird, UT.Google Scholar
- Prado, A., Canal, I., Barbas, J., Molley, J., and Ferrus, A. 1995. Functional recovery of troponin I in a Drosophila heldup mutant after a second site mutation. Mol. Biol. Cell 6:1433–1441.PubMedGoogle Scholar
- Reinach, F. 1995. Nemaline myopathy mechanisms. Nat. Genetics 10:8.CrossRefGoogle Scholar
- Rethinasamy, P., Muthuchamy, M., Hewett, T., Boivin, G., Wolska, B., Evans, C., Solaro, R.J., and Wieczorek, D.F. 1998. Molecular and physiological effects of a-tropomyosin ablation in the mouse. Circ. Res. 82:116–123.PubMedCrossRefGoogle Scholar
- Solaro, R. and Van Eyk, J. 1996. Altered interactions among thin filament proteins modulate cardiac function. J. Mol. Cell. Cardiol. 28:217–230.PubMedCrossRefGoogle Scholar
- Spirito, P., Seidman, C., McKenna, W., and Maron, B. 1997. The management of hypertrophic cardiomyopathy. N. Engl. J. Med. 335:775–785.CrossRefGoogle Scholar
- Thierfelder, L., Watkins, H., MacRae, C., Lamas, R., McKenna, W., Vosberg, H., Seidman, J., and Seidman, C. 1994. α tropomyosin and cardiac troponin T mutations cause familial hypertrophic cardiomyopahty: a disease of the sarcomere. Cell 77:701–712.Google Scholar
- Walsh, T., Trueblood, C., Evans, R., and Weber, A. 1984. Removal of tropomyosin overlap and the co-operative response to increasing calcium concentrations of the acto-subfragment-1 ATPase. J. Mol. Biol. 182:265–269.CrossRefGoogle Scholar
- Warmke, J., Kreuz, A., and Falkenthal, S. 1989. Co-localization to chromosome bands 99D13 of the Drosophila melanogaster myosin light chain-2 gene and a haplo-insufficient locus that affects flight behavior. Genetics 122:139–151.PubMedGoogle Scholar
- Williams, B. and Waterston, R. 1994. Genes critical for muscle development and function in Caenorhabditis elegans identified through lethal mutations. J. Cell Biol. 124:475–490.PubMedCrossRefGoogle Scholar
- Xu, C., Craig, R., Tobacman, L., Horowitz, R., and Lehman, W. 1999. Tropomyosin positions in regulated thin filaments revealed by cryoelectron microscopy. Biophys. J. 77:985–992.PubMedCrossRefGoogle Scholar
- Zajdel, R., McLean, M., Lemanski, S., Muthuchamy, M., Wieczorek, D., Lemanski, L., and Dube, D. 1998. Ectopic expression of tropomyosin promotes myofibrillogenesis in mutant axolotl hearts. Dev. Dyn. 213:412–420.PubMedCrossRefGoogle Scholar
- Zajdel R., McLean, M., Isitmangil, G., Lemanski, L., Wieczorek, D., and Dube, D. 2000. Alteration of cardiac myofibrillogenesis by liposome-mediated delivery of exogenous proteins and nucleic acids into whole embryonic hearts. Anatomy and Embryology 201:217–228.PubMedCrossRefGoogle Scholar
Copyright information
© Springer Science+Business Media New York 2002