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Identification of myosin heavy chain I, IIa and IIx in canine skeletal muscles by an electrophoretic and immunoblotting study.
Cells Tissues Organs. 2005; 180(2):106-16.CT

Abstract

To determine which myosin heavy chain (MHC) isoforms are expressed in canine skeletal muscles, different muscle samples of five mixed-breed dogs were analysed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The separated MHC isoforms were identified by immunoblotting technique using a set of specific monoclonal antibodies. To compare the results of the electrophoretic and immunoblotting study, the pattern of MHC isoform expression and histochemical profiles of canine fibres were additionally demonstrated on serial muscle sections by immunohistochemistry and myofibrillar adenosine triphosphatase (mATPase) histochemistry. Not more than three MHC isoforms were demonstrated by SDS-PAGE in the analysed canine muscles. By the immunoblotting technique, the fastest migrating MHC band was identified as slow or MHC-I, the intermediate one as MHC-IIx and the slowest migrating band as MHC-IIa isoform. Since none of the three MHC bands and none of the analysed fibres were recognized by the antibody specific to MHC-IIb of rats, we concluded that MHC-IIb is not expressed in large skeletal muscles of dogs. Similarly, only three major fibre types, i.e. I, IIA and IIX, were revealed according to the pattern of MHC immunohistochemistry and mATPase reaction. Type IIA fibres were more alkali- and acid-stable than type IIX fibres after mATPase histochemistry; hence, the latter corresponded to type IIDog fibres. However, beside the three major fibre types, scarce hybrid fibres co-expressing two MHC isoforms (I/IIA and IIA/IIX) were demonstrated by immunohistochemistry.

Authors+Show Affiliations

Institute of Anatomy, Medical Faculty, University in Ljubljana, Ljubljana, Slovenia. vika.smerdu@mf.uni-lj.siNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

16113539

Citation

Smerdu, V, et al. "Identification of Myosin Heavy Chain I, IIa and IIx in Canine Skeletal Muscles By an Electrophoretic and Immunoblotting Study." Cells, Tissues, Organs, vol. 180, no. 2, 2005, pp. 106-16.
Smerdu V, Strbenc M, Meznaric-Petrusa M, et al. Identification of myosin heavy chain I, IIa and IIx in canine skeletal muscles by an electrophoretic and immunoblotting study. Cells Tissues Organs. 2005;180(2):106-16.
Smerdu, V., Strbenc, M., Meznaric-Petrusa, M., & Fazarinc, G. (2005). Identification of myosin heavy chain I, IIa and IIx in canine skeletal muscles by an electrophoretic and immunoblotting study. Cells, Tissues, Organs, 180(2), 106-16.
Smerdu V, et al. Identification of Myosin Heavy Chain I, IIa and IIx in Canine Skeletal Muscles By an Electrophoretic and Immunoblotting Study. Cells Tissues Organs. 2005;180(2):106-16. PubMed PMID: 16113539.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Identification of myosin heavy chain I, IIa and IIx in canine skeletal muscles by an electrophoretic and immunoblotting study. AU - Smerdu,V, AU - Strbenc,M, AU - Meznaric-Petrusa,M, AU - Fazarinc,G, PY - 2005/04/18/accepted PY - 2005/8/23/pubmed PY - 2005/10/29/medline PY - 2005/8/23/entrez SP - 106 EP - 16 JF - Cells, tissues, organs JO - Cells Tissues Organs VL - 180 IS - 2 N2 - To determine which myosin heavy chain (MHC) isoforms are expressed in canine skeletal muscles, different muscle samples of five mixed-breed dogs were analysed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The separated MHC isoforms were identified by immunoblotting technique using a set of specific monoclonal antibodies. To compare the results of the electrophoretic and immunoblotting study, the pattern of MHC isoform expression and histochemical profiles of canine fibres were additionally demonstrated on serial muscle sections by immunohistochemistry and myofibrillar adenosine triphosphatase (mATPase) histochemistry. Not more than three MHC isoforms were demonstrated by SDS-PAGE in the analysed canine muscles. By the immunoblotting technique, the fastest migrating MHC band was identified as slow or MHC-I, the intermediate one as MHC-IIx and the slowest migrating band as MHC-IIa isoform. Since none of the three MHC bands and none of the analysed fibres were recognized by the antibody specific to MHC-IIb of rats, we concluded that MHC-IIb is not expressed in large skeletal muscles of dogs. Similarly, only three major fibre types, i.e. I, IIA and IIX, were revealed according to the pattern of MHC immunohistochemistry and mATPase reaction. Type IIA fibres were more alkali- and acid-stable than type IIX fibres after mATPase histochemistry; hence, the latter corresponded to type IIDog fibres. However, beside the three major fibre types, scarce hybrid fibres co-expressing two MHC isoforms (I/IIA and IIA/IIX) were demonstrated by immunohistochemistry. SN - 1422-6405 UR - https://www.unboundmedicine.com/medline/citation/16113539/Identification_of_myosin_heavy_chain_I_IIa_and_IIx_in_canine_skeletal_muscles_by_an_electrophoretic_and_immunoblotting_study_ L2 - https://www.karger.com?DOI=10.1159/000086751 DB - PRIME DP - Unbound Medicine ER -