Myosin types and fiber types in cardiac muscle. I. Ventricular myocardium.
Open Access
- 1 January 1981
- journal article
- research article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 88 (1), 226-233
- https://doi.org/10.1083/jcb.88.1.226
Abstract
Antisera against bovine atrial myosin were raised in rabbits, purified by affinity chromatography, and absorbed with insolubilized ventricular myosin. Specific anti-bovine atrial myosin (anti-bAm) antibodies reacted selectively with atrial myosin heavy chains, as determined by enzyme immunoassay combined with SDS-gel electrophoresis. In direct and indirect immunofluorescence assay, anti-bAm was found to stain all atrial muscle fibers and a minor proportion of ventricular muscle fibers in the right ventricle of the bovine heart. In contrast, almost all muscle fibers in the left ventricle were unreactive. Purkinje fibers showed variable reactivity. In the rabbit heart, all atrial muscle fibers were stained by anti-bAm, whereas ventricular fibers showed a variable response in both the right and left ventricle, with a tendency for reactive fibers to be more numerous in the right ventricle and in subepicardial regions. Diversification of fiber types with respect to anti-bAm reactivity was found to occur during late stages of postnatal development in the rabbit heart and to be influenced by thyroid hormone. All ventricular muscle fibers became strongly reactive after thyroxine treatment, whereas they became unreactive or poorly reactive after propylthiouracil treatment. These findings are consistent with the existence of different ventricular isomyosins whose relative proportions can vary according to the thyroid state. Variations in ventricular isomyosin composition can account for the changes in myosin Ca2+-activated ATPase activity previously observed in cardiac muscle from hyper- and hypothyroid animals and may be responsible for the changes in the velocity of contraction of ventricular myocardium that occur under these conditions. The differential distribution of ventricular isomyosins in the normal heart suggests that fiber types with different contractile properties may coexist in the ventricular myocardium.Keywords
This publication has 36 references indexed in Scilit:
- An immunochemical approach to the structure of myosin and the thick filamentJournal of Molecular Biology, 1972
- The transformation of myosin in cross-innervated rat musclesThe Journal of Physiology, 1971
- Species Differences in Intrinsic Myocardial ContractilityExperimental Biology and Medicine, 1970
- The Reliability of Molecular Weight Determinations by Dodecyl Sulfate-Polyacrylamide Gel ElectrophoresisJournal of Biological Chemistry, 1969
- CARDIAC MUSCLEThe Journal of cell biology, 1968
- Influence of the Thyroid State on the Intrinsic Contractile Properties and Energy Stores of the Myocardium*Journal of Clinical Investigation, 1967
- Contractile State of Cardiac Muscle Obtained from Cats with Experimentally Produced Ventricular Hypertrophy and Heart FailureCirculation Research, 1967
- ATPase Activity of Myosin Correlated with Speed of Muscle ShorteningThe Journal of general physiology, 1967
- Chromatography of Myosin on Diethylaminoethyl-Sephadex A-50*Biochemistry, 1967
- STUDIES ON MYOSIN FROM RED AND WHITE SKELETAL MUSCLES OF RABBIT .I. ADENOSINE TRIPHOSPHATASE ACTIVITY1966