Abstract
The presence of developmentally regulated myosin isoforms in muscle tissues is well established (1–9). Cardiac myosin has been studied extensively, and three different isoforms have been identified (4,5). These myosin isoforms differ with respect to (a) their mobilities on nondenaturing Polyacrylamide gels (3), (b) subunit composition (3,4), and (c) actomyosin ATPase activities (4). Moreover, specific cardiac myosin isoforms are expressed following volume overload of the heart (2) and change depending upon thyroid hormone levels (5). Similarly, fiberspecific myosin isoforms are expressed in skeletal muscle, and the myosin isoform correlates with both the type of innervation and the sequence of electrical stimulation (6).
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
H. Takano-Ohmuro, T. Obinata, M. Kawashima, T. Masaki, and T. Tanaka, Embryonic Chicken Skeletal, Cardiac, and Smooth Muscles Express a Common Embryo-specific Myosin Light Chain. J. Cell Biol. 100:2025–2030 (1985).
A.M. Lompre, 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).
J.F.Y. Hoh, P.A. McGrath, and R.I. White, Electrophoretic Analysis of Multiple Forms of Myosin in Fast-Twitch and Slow-Twitch Muscles of the Chick. Biochem. J. 157:87–95 (1976).
J.J. Schier and R.S. Adelstein, Structural and Enzymatic Comparison of Human Cardiac Muscle Myosins Isolated from Infants, Adults, and Patients with Hypertrophic Cardiomyopathy. J. Clin. Invest. 69:816–825 (1982).
I.L. Flink, J.H. Rader, and E. Morkin, Thyroid Hormone Stimulates Synthesis of a Cardiac Myosin Isozyme. J. Biol. Chem. 254:3105–3110 (1979).
S. Salmons, and F.A. Sreter, Significance of Impulse Activity in the Transformation of Skeletal Muscle Type. Nature 263:30–34 (1976).
D.A. Winkelmann, S. Lowey, and J.L. Press, Monoclonal Antibodies Localize Changes on Myosin Heavy Chain Isozymes during Avian Myogenesis. Cell 34:295–306 (1983).
N. Katoh, and S. Kubo, Purfication and Some Properties of Rabbit Stomach Myosin. J. Biochem. 81:1497–1503 (1977).
H. Takano-Ohmuro, T. Obinata, T. Mikawa, and T. Masaki, Changes in Myosin Isozymes during Development of Chicken Gizzard Muscle. J. Biochem. 93:903–908 (1983).
M. Kawashima, Y. Nabeshima, T. Obinata, and Y. Fujii-Kuriyama, A Common Myosin Light Chain is Expressed in Chicken Embryonic Skeletal, Cardiac, and Smooth Muscles and in Brain Continuously from Embryo to Adult. J. Biol. Chem. 262:14408–14414 (1987).
R.S. Adelstein and C.B. Klee, Purification and Characterization of Smooth Muscle Myosin Light Chain Kinase. J. Biol. Chem. 256:7501–7509 (1981).
M. Nishikawa, S. Shirakawa, and R.S. Adelstein, Phosphorylation of Smooth Muscle Myosin Light Chain Kinase by Protein Kinase C. J. Biol. Chem. 260:8978–8983 (1985).
P. de Lanerolle, R.S. Adelstein, J.R. Feramisco, and K. Burridge, Characterization of Antibodies to Smooth Muscle Myosin Kinase and their use in Localizing Myosin Kinase in Nonmuscle Cells. Proc. Natl. Acas. Sci. USA 78:4738–4742 (1981).
D.R. Hathaway and J.R. Haeberle, A Radioimmunoblotting Method for Measuring Myosin Light Chain Phosphorylation Levels in Smooth Muscle. Am. J. Physiol. 249: C345–C351 (1985).
J.R. Sellers, M.D. Pato, and R.S. Adelstein, Reversible Phosphorylation of Smooth Muscle Myosin, Heavy Meromyosin, and Platelet Myosin. J. Biol. Chem. 256:13137–13142 (1981).
M. Nishikawa, H. Hidaka, and R.S. Adelstein, Phosphorylation of Smooth Muscle Heavy Meromyosin by Calcium-activated, Phospholipid-dependent Protein Kinase. J. Biol. Chem. 258:14069–14072 (1983).
J.A. Spudich, and S. Watt, The Regulation of Rabbit Skeletal Muscle Contraction. J. Biol. Chem. 246:1866–1871, (1971).
O.H. Lowry, N.J. Rosenbrough, A.L. Farr, and R.J. Randall, Protein Measurement with the Folin Phenol Reagent. J. Biol. Chem. 193:265–275 (1951).
U.K. Laemmli, Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4. Nature 227:680–685 (1970).
P. de Lanerolle, M. Nishikawa, R. Felsen, and R.S. Adelstein, Immunological Properties of Myosin Light-Chain Kinases. Biochimica et Biophysica Acta 914:74–82 (1987).
J.C. Seidel, N. Nath, and S. Nag, Ca2+ Dependence of the ATPase Activity of Phosphorylated Smooth Muscle Myosin: Effects of Tropomyosin and Actin. Biochimica et Biophysica Acta 871:93–100 (1986).
M. Ikebe, D.J. Hartshorne, and M. Elzinga, Phosphorylation of the 20,000-Dalton Light Chain of Smooth Muscle Myosin by the Calcium-Activated, Phospholipid-Dependent Protein Kinase. J. Biol. Chem. 262:9569–9573 (1987).
P. de Lanerolle, and M. Nishikawa, Regulation of Embryonic Smooth Muscle Myosin by Protein Kinase C. J. Biol. Chem. 263:9071–9074 (1988).
R.S. Adelstein, Regulation of Contractile Proteins by Phosphorylation. J. Clin. Invest. 72:1863–1866 (1983).
P. de Lanerolle, and J.T. Stull, Myosin Phosphorylation during Contraction and Relaxation of Tracheal Smooth Muscle. J. Biol. Chem. 255:9993–10000 (1980).
L. Donner, P. de Lanerolle, and J. Costa, Immunoreactivity of Paraffin-embedded Normal Tissues and Mesenchymal Tumors for Smooth Muscle Myosin. Am. J. Clin. Path. 80:677–681 (1983).
R.M. Medford, R.M. Wydro, H.T. Nguyen, and B. Nadal-Ginard, Cytoplasmic Processing of Myosin Heavy Chain Messenger RNA: Evidence Provided by using a Recombinant DNA Plasmid. Proc. Natl. Acad. Sci. USA 77:5749–5753 (1980).
A.R. Bengur, E.A. Robinson, E. Appella, and J.R. Sellers, Sequence of the Sites Phosphorylated by Protein Kinase C in the Smooth Muscle Myosin Light Chain. J. Biol. Chem. 262:7613–7617 (1987).
I. Mabuchi, and M. Okuno, The Effect of Myosin Antibody on the Division of Starfish Blastomeres. J. Cell Biol. 74:251–263 (1977).
D.A. Knecht and W.F. Loomis, Antisense RNA Inactivation of Myosin Heavy Chain Gene Expression in Dictyostelium discoideum. Science 236:1081–1086 (1987).
A. De Lozanne and J.A. Spudich, Disruption of the Dictyostelium Myosin Heavy Chain Gene by Homologous Recombination. Science 236:1086–1091 (1987).
Y. Nishizuka, Studies and Perspectives of Protein Kinase C. Science 233:305–312 (1986).
E. Rozengurt, Early Signals in the Mitogenic Response. Science 234:161–166 (1986).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1989 Plenum Press, New York
About this chapter
Cite this chapter
de Lanerolle, P. (1989). Regulation of Embryonic Smooth Muscle Myosin by Myosin Light Chain Kinase and by Protein Kinase C. In: Hidaka, H., Carafoli, E., Means, A.R., Tanaka, T. (eds) Calcium Protein Signaling. Advances in Experimental Medicine and Biology, vol 255. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5679-0_34
Download citation
DOI: https://doi.org/10.1007/978-1-4684-5679-0_34
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-5681-3
Online ISBN: 978-1-4684-5679-0
eBook Packages: Springer Book Archive