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Pattern of myosin heavy chain isoforms in different fibre types of canine trunk and limb skeletal muscles.
Cells Tissues Organs. 2004; 176(4):178-86.CT

Abstract

The aim of this study was to determine the pattern of myosin heavy chain (MHC) isoform expressions within the muscle fibres of functionally diverse trunk and limb dog muscles using monoclonal antibodies that are specific to MHC isoforms. We found that three MHC isoforms are expressed in dog skeletal muscles. The pattern of their expressions determined the existence of 'pure' fibres, i.e. I and IIa, both expressing only one MHC isoform, and 'hybrid' fibres, i.e. I/IIa and IIa/x, that co-expressed two MHC isoforms. While the MHCI, MHCIIa and MHCI/IIa fibres corresponded to the myofibrillar ATPase type fibres I, IIA and IIC, respectively, the hybrid MHCIIa/x fibres mostly behaved like the IIDog fibre type in myofibrillar ATPase reaction as described by Latorre et al. No pure MHCIIx fibres were found. Though MHCIIa/x fibres were quite numerous, their presence varied not only within different muscles but within the same muscle of different animals as well. We suggest that the discrepancies in the classification of fibre types according to their myofibrillar ATPase activity between different studies of dog skeletal muscles are probably a consequence of the variable content of the MHCIIa and MHCIIx isoforms in the MHCIIa/x hybrid fibres. Estimating the histochemical metabolic profile of fibres we found that in all fast fibres oxidative-glycolytic metabolism prevailed, whereas in slow fibres oxidative metabolism was more pronounced.

Authors+Show Affiliations

Institute for Anatomy, Histology and Embryology, Veterinary Faculty, University of Ljubljana, Ljubljana, Slovenia.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

15118397

Citation

Strbenc, M, et al. "Pattern of Myosin Heavy Chain Isoforms in Different Fibre Types of Canine Trunk and Limb Skeletal Muscles." Cells, Tissues, Organs, vol. 176, no. 4, 2004, pp. 178-86.
Strbenc M, Smerdu V, Zupanc M, et al. Pattern of myosin heavy chain isoforms in different fibre types of canine trunk and limb skeletal muscles. Cells Tissues Organs. 2004;176(4):178-86.
Strbenc, M., Smerdu, V., Zupanc, M., Tozon, N., & Fazarinc, G. (2004). Pattern of myosin heavy chain isoforms in different fibre types of canine trunk and limb skeletal muscles. Cells, Tissues, Organs, 176(4), 178-86.
Strbenc M, et al. Pattern of Myosin Heavy Chain Isoforms in Different Fibre Types of Canine Trunk and Limb Skeletal Muscles. Cells Tissues Organs. 2004;176(4):178-86. PubMed PMID: 15118397.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Pattern of myosin heavy chain isoforms in different fibre types of canine trunk and limb skeletal muscles. AU - Strbenc,M, AU - Smerdu,V, AU - Zupanc,M, AU - Tozon,N, AU - Fazarinc,G, PY - 2003/12/04/accepted PY - 2004/5/1/pubmed PY - 2004/12/16/medline PY - 2004/5/1/entrez SP - 178 EP - 86 JF - Cells, tissues, organs JO - Cells Tissues Organs VL - 176 IS - 4 N2 - The aim of this study was to determine the pattern of myosin heavy chain (MHC) isoform expressions within the muscle fibres of functionally diverse trunk and limb dog muscles using monoclonal antibodies that are specific to MHC isoforms. We found that three MHC isoforms are expressed in dog skeletal muscles. The pattern of their expressions determined the existence of 'pure' fibres, i.e. I and IIa, both expressing only one MHC isoform, and 'hybrid' fibres, i.e. I/IIa and IIa/x, that co-expressed two MHC isoforms. While the MHCI, MHCIIa and MHCI/IIa fibres corresponded to the myofibrillar ATPase type fibres I, IIA and IIC, respectively, the hybrid MHCIIa/x fibres mostly behaved like the IIDog fibre type in myofibrillar ATPase reaction as described by Latorre et al. No pure MHCIIx fibres were found. Though MHCIIa/x fibres were quite numerous, their presence varied not only within different muscles but within the same muscle of different animals as well. We suggest that the discrepancies in the classification of fibre types according to their myofibrillar ATPase activity between different studies of dog skeletal muscles are probably a consequence of the variable content of the MHCIIa and MHCIIx isoforms in the MHCIIa/x hybrid fibres. Estimating the histochemical metabolic profile of fibres we found that in all fast fibres oxidative-glycolytic metabolism prevailed, whereas in slow fibres oxidative metabolism was more pronounced. SN - 1422-6405 UR - https://www.unboundmedicine.com/medline/citation/15118397/Pattern_of_myosin_heavy_chain_isoforms_in_different_fibre_types_of_canine_trunk_and_limb_skeletal_muscles_ L2 - https://www.karger.com?DOI=10.1159/000077034 DB - PRIME DP - Unbound Medicine ER -