The fibre type composition of the striated muscle of the oesophagus in ruminants and carnivores
- 1 May 1984
- journal article
- research article
- Published by Springer Nature in Histochemistry and Cell Biology
- Vol. 80 (3) , 277-288
- https://doi.org/10.1007/bf00495778
Abstract
The fibre type composition of the striated muscle layer of the oesophagus of the cow, sheep, donkey, dog and cat was examined with standard histochemical methods and immunohistochemical staining using type-specific antimyosin sera. The heavy chain and light chain composition of oesophageal myosin was also examined using electrophoretic peptide mapping and 2-dimensional gel electrophoresis respectively. In the ruminants and donkey the oesophagus was composed of fibre types I, IIA and IIC with immunohistochemical characteristics identical to those of the same fibre types found in control skeletal muscle. In the ruminants there was a gradient in the proportion of type I fibres from 1% (at the cervical end) to about 30% (at the caudal end). In the carnivores the oesophageal muscle was composed of a very small percentage of type I and IIC fibres, but the predominant type was very different hisotchemically and immunohistochemically from all the fibre types (I, IIA, IIB, IIC) present in the control muscles. This oesophageal fibre type (IIoes) had an acid- and alkaline-stable m-ATP-ase activity, a moderate histochemical Ca-Mg actomyosin ATPase activity, and reacted weakly with anti-IIA and antiIIB myosin sera. Although the light chains of the IIoes myosin were the same as the light chains of a mixture of IIA and IIB myosins, their respective heavy chains gave different peptide maps. Greater differences were obtained between the heavy chains of IIoes and other striated muscle myosins. These observations lead us to conclude that this predominant fibre type of the carnivore oesophageal striated muscle is of the ‘fast’ type, and contains a distinct isoform of myosin similr but not identical to the other fast type myosins.Keywords
This publication has 60 references indexed in Scilit:
- Myosin heavy chains from two different adult fast-twitch muscles have different peptide maps but identical mRNAsCell, 1982
- "Fast" isomyosins and fiber types in mammalian skeletal muscle.Journal of Histochemistry & Cytochemistry, 1981
- Fast-white and fast-red isomyosins in guinea pig musclesBiochemical and Biophysical Research Communications, 1980
- "Slow" myosins in vertebrae skeletal muscle. An immunofluorescence study.The Journal of cell biology, 1980
- Transitions in contractile protein isozymes during muscle cell differentiationBiochimie, 1979
- Histochemical fibre types in striated muscle from the guinea-pig oesophagusCellular and Molecular Life Sciences, 1978
- Myosin from cross‐reinnervated cat muscles. Evidence for reciprocal transformation of heavy chainsFEBS Letters, 1975
- Quantitative Film Detection of 3H and 14C in Polyacrylamide Gels by FluorographyEuropean Journal of Biochemistry, 1975
- Histochemical and mechanical properties of the jaw muscles of the catExperimental Neurology, 1973
- Light Chains from Fast and Slow Muscle MyosinsNature, 1971