Myosin Heavy Chain Expression in Respiratory Muscles of the Rat
- 1 March 1992
- journal article
- Published by American Thoracic Society in American Journal of Respiratory Cell and Molecular Biology
- Vol. 6 (3) , 335-339
- https://doi.org/10.1165/ajrcmb/6.3.335
Abstract
Myosin heavy chain (MHC) isoforms of hind limb adult rat muscles and muscles with a range of respiratory activities were analyzed by a sodium dodecyl sulfate polyacrylamide gel electrophoresis technique that allowed electrophoretic separation of the three fast and one slow MHC isoform found in typical rat muscle. Costal and crural diaphragm muscle samples expressed a mixture of MHC beta/slow, MHC2A, and MHC2X but little MHC2B. In contrast, MHC2B was the dominant MHC isoform in the genioglossus, intercostal, and three abdominal muscles, all of which exhibited minimal expression of MHC beta/slow. The amount of MHC2X (relative to total MHC composition) was similar in the diaphragm, genioglossus, and transversus abdominis muscles, while considerably less was detected in the rectus abdominis and external oblique muscles. These results indicate that MHC2X is broadly and variably distributed among respiratory muscles. Furthermore, these data suggest that a large portion of 2X fibers (containing MHC2X), which cannot be detected by standard histochemical analysis, may be present in the genioglossus and transversus abdominis muscles as has been demonstrated for the diaphragm muscle. We speculate that an association exists between the level of MHC2X expression and frequency of respiratory recruitment.Keywords
This publication has 30 references indexed in Scilit:
- Emergence of the mature myosin phenotype in the rat diaphragm muscleDevelopmental Biology, 1991
- Localization of the ATP‐binding site in the 23‐kDa and 20‐kDa regions of the heavy chain of the skeletal muscle myosin headEuropean Journal of Biochemistry, 1989
- MOLECULAR GENETICS OF MYOSINAnnual Review of Biochemistry, 1987
- Type 1, 2A, and 2B myosin heavy chain electrophoretic analysis of rat muscle fibersBiochemical and Biophysical Research Communications, 1986
- MYOSINAnnual Review of Biochemistry, 1984
- Myosin isozyme transitions occurring during the postnatal development of the rat soleus muscleDevelopmental Biology, 1984
- A sensitive SDS-page method separating myosin heavy chain isoforms of rat skeletal muscles reveals the heterogeneous nature of the embryonic myosinBiochemical and Biophysical Research Communications, 1983
- Chronic denervation of rat diaphragm: Selective maintenance of adult fast myosin heavy chainsMuscle & Nerve, 1982
- The contractile properties, histochemistry, ultrastructure and electrophysiology of the cricothyroid and posterior cricoarytenoid muscles in the ratJournal of Muscle Research and Cell Motility, 1982
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970