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Differences in myosin composition between human oro-facial, masticatory and limb muscles: enzyme-, immunohisto- and biochemical studies.
J Muscle Res Cell Motil. 1994 Oct; 15(5):517-34.JM

Abstract

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 alpha-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, MLC1emb, 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.

Authors+Show Affiliations

Department of Anatomy, Umeå University, Sweden.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

7860700

Citation

Stål, P, et al. "Differences in Myosin Composition Between Human Oro-facial, Masticatory and Limb Muscles: Enzyme-, Immunohisto- and Biochemical Studies." Journal of Muscle Research and Cell Motility, vol. 15, no. 5, 1994, pp. 517-34.
Stål P, Eriksson PO, Schiaffino S, et al. Differences in myosin composition between human oro-facial, masticatory and limb muscles: enzyme-, immunohisto- and biochemical studies. J Muscle Res Cell Motil. 1994;15(5):517-34.
Stål, P., Eriksson, P. O., Schiaffino, S., Butler-Browne, G. S., & Thornell, L. E. (1994). Differences in myosin composition between human oro-facial, masticatory and limb muscles: enzyme-, immunohisto- and biochemical studies. Journal of Muscle Research and Cell Motility, 15(5), 517-34.
Stål P, et al. Differences in Myosin Composition Between Human Oro-facial, Masticatory and Limb Muscles: Enzyme-, Immunohisto- and Biochemical Studies. J Muscle Res Cell Motil. 1994;15(5):517-34. PubMed PMID: 7860700.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Differences in myosin composition between human oro-facial, masticatory and limb muscles: enzyme-, immunohisto- and biochemical studies. AU - Stål,P, AU - Eriksson,P O, AU - Schiaffino,S, AU - Butler-Browne,G S, AU - Thornell,L E, PY - 1994/10/1/pubmed PY - 1994/10/1/medline PY - 1994/10/1/entrez SP - 517 EP - 34 JF - Journal of muscle research and cell motility JO - J Muscle Res Cell Motil VL - 15 IS - 5 N2 - 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 alpha-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, MLC1emb, 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. SN - 0142-4319 UR - https://www.unboundmedicine.com/medline/citation/7860700/Differences_in_myosin_composition_between_human_oro_facial_masticatory_and_limb_muscles:_enzyme__immunohisto__and_biochemical_studies_ DB - PRIME DP - Unbound Medicine ER -