Differences in myosin composition between human oro-facial,masticatory and limb muscles: enzyme-, immunohisto-and biochemical studies |
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| Authors: | P. Stål P.-O. Eriksson S. Schiaffino G. S. Butler-Browne L.-E. Thornell |
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| Affiliation: | (1) Department of Anatomy, Umeå University, Umeå, Sweden;(2) Department of Clinical Oral Physiology, Umeå University, Umeå, Sweden;(3) Department of Biomedical Sciences, University of Padova, 35100 Padova, Italy;(4) CNR Unit for Muscle Biology and Physiology, University of Padova, 35100 Padova, Italy;(5) CNRS URA 1448, UFR Biomedicale, Rue des St-Peres, Paris, France |
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| Abstract: | Summary Immunohistochemistry was used to determine the myosin composition of defined fibre types of three embryologically different adult muscles, the oro-facial, masseter and limb muscles. In addition, the myosin composition in whole muscle specimens was analysed with biochemical methods. Both similarities and differences between muscles in the content of myosin heavy chains and myosin light chains were found. Nevertheless, each muscle had its own distinct identity. Our results indicated the presence of a previously undetected fast myosin heavy chain isoform in the oro-facial type II fibre population, tentatively termed  fast F . The masseter contained aberrant myosin isoforms, such as foetal myosin heavy chain and  -cardiac myosin heavy chain and unique combinations of myosin heavy chain isoforms which were not found in the limb or oro-facial muscles. The type IM and IIC fibres coexpressed slow and fast A myosin heavy chains in the oro-facial and limb muscles but slow and a fast B like myosin heavy chain in the masseter. While single oro-facial and limb muscle fibres contained one or two myosin heavy chain types, single masseter fibres coexpressed up to four different myosin heavy chain isoforms. Describing the fibres according to their expression of myosin heavy chain isozymes, up to five fibre types could be distinguished in the oro-facial and limb muscles and eight in the masseter. Oro-facial and limb muscles expressed five myosin light chains, MLC1S, MLC2S, MLC1F, MLC2F and MLC3F, and the masseter four, MLC1S, MLC2S, MLC1F, and, in addition, an embryonic myosin light chain, MLCtemb, which is usually not present in normal adult skeletal muscle. These results probably reflect the way the muscles have evolved to meet the specialized functional requirements imposed upon them and are in agreement with the previously proposed concept that jaw and limb muscles belong to two distinct allotypes. |
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