Journal of muscle research and cell motility.
Publisher:
Chapman and Hall.. Dordrecht : Springer Netherlands
Frequency: 8 no. a year, 1999-
Country: Netherlands
Language: English
Start Year:1980 -
ISSN:
0142-4319 (Print)
1573-2657 (Electronic)
0142-4319 (Linking)
1573-2657 (Electronic)
0142-4319 (Linking)
Impact Factor
2
2022
| NLM ID: | 8006298 |
| (DNLM): | J30550000(s) |
| (OCoLC): | 06517602 |
| Coden: | JMRMD3 |
| LCCN: | sn 81001723 |
| Classification: | W1 JO775R |
Therapeutic clenbuterol treatment does not alter Ca2+ sensitivity of permeabilized fast muscle fibres from exercise trained or untrained horses. Clenbuterol is a beta2-adrenoceptor agonist primarily used for treating bronchospasm and alleviating the symptoms of chronic obstructive pulmonary disease (COPD) in the horse. In other species (rats, mice, sheep, and cattle), chronic high doses of clenbuterol (typically in the milligram per kilogram body weight range) has been shown to cause a muscle directed protein anabolic response. Clenbuterol can also modify muscle fibre composition and therefore potentially affect muscle function. This has implications for the performance of exercising horses being treated with therapeutic doses of clenb...
Myosin heavy chain profile of equine gluteus medius muscle following prolonged draught-exercise training and detraining. Fourteen 4-year old Andalusian mares were used to examine the plasticity of myosin heavy chain (MHC) composition in horse skeletal muscle with heavy draught-exercise training and detraining. Seven horses underwent a training programme based on carriage exercises for 8 months. Afterwards, they were kept in paddocks for 3 months. The remaining seven animals were used as control horses. Three gluteus medius muscle biopsies were removed at depths of 20, 40 and 60 mm from each horse before (month 0), during the training (months 3 and 8) and after detraining (month 11). Myosin heavy chain compositio...
Analysis of myosin heavy chains at the protein level in horse skeletal muscle. Combined methodologies of enzyme-linked immunosorbent assay (ELISA), sodium dodecyl sulphate polyacrilamide gel electrophoresis (SDS-PAGE), immunoblotting, traditional myofibrillar ATPase (mATPase) histochemistry and immunocytochemistry of whole biopsied samples were used to study myosin heavy chain (MHC) isoforms in the equine gluteus medius muscle. The ELISA technique allowed the quantification of the three MHC isoforms known to be present in different horse muscles: slow (MHC-I) and two fast (termed MHC-IIA and MCH-IIX). The SDS-PAGE method resolved MHCs in three bands: MHC-I, MHC-IIX and M...