Systematic variation in myosin expression along extraocular muscle fibres of the adult rat
- 1 February 1990
- journal article
- research article
- Published by Springer Nature in Journal of Muscle Research and Cell Motility
- Vol. 11 (1) , 25-40
- https://doi.org/10.1007/bf01833323
Abstract
Monoclonal antibodies (McAB) specific for fast (C14) and slow (S58) myosin, and a myosin antigenically similar to neonatal/embryonic myosin in mammals (ALD180), were used to characterize the myosin distribution in orbital layer fibres of rat extraocular muscles (EOM) in relation to innervation patterns. The orbital layer is composed of both singly-innervated (SIF) and multiply-innervated (MIF) fibres. The SIFs have the characteristics of twitch fibres, while the MIFs, in addition to possessing many small endings characteristic of tonic fibres, also have an en-plaque-like innervation in the endplate band resembling that of the adjacent SIFs. Myosin expression in MIFs and SIFs is unusual and varies systematically along the length of the fibres. Both SIFs and MIFs label with ALD180, but this labelling is absent in both fibre types in the endplate band region, where all fibres label with C14. Distally and also proximally to the endplate band, SIFs label with both ALD180 and C14, while the MIFs, innervated by many small, superficial endings in these regions, label with ALD180 only. This pattern of myosin expression could also be demonstrated in isolated fibres. The results are discussed in relation to the hypothesis that both populations of orbital layer fibres express constitutively both fast and the neonatal-like myosin, and that superimposed on this constitutive expression twitch or tonic innervation acts locally to selectively suppress either neonatal-like or fast myosin, respectively.Keywords
This publication has 55 references indexed in Scilit:
- Complexity of myosin species in the avian posterior latissimus dorsi muscleJournal of Muscle Research and Cell Motility, 1988
- The cellular basis of myosin heavy chain isoform expression during development of avian skeletal musclesDevelopmental Biology, 1987
- Differentiation of the anterior latissimus dorsi muscle of the chicken examined by anti‐myosin monoclonal antibodiesJournal of Experimental Zoology, 1987
- Fibre types in extraocular muscles: a new myosin isoform in the fast fibresJournal of Muscle Research and Cell Motility, 1987
- Myosin isozyme transitions occurring during the postnatal development of the rat soleus muscleDevelopmental Biology, 1984
- Three myosin heavy-chain isozymes appear sequentially in rat muscle developmentNature, 1981
- Development of muscle fiber specialization in the rat hindlimb.The Journal of cell biology, 1981
- "Slow" myosins in vertebrae skeletal muscle. An immunofluorescence study.The Journal of cell biology, 1980
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Unique intrafusal and extraocular muscle fibers exhibiting dual actomyosin ATPase activityExperimental Neurology, 1969