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Relationship between myosin heavy chain IId isoform and fibre types in soleus muscle of the rat after hindlimb suspension.
Eur J Appl Physiol Occup Physiol. 1993; 66(5):451-4.EJ

Abstract

The relationship between the myosin heavy chain (HC) IId isoform and histochemically defined fibre types was investigated in the rat soleus muscle after hindlimb suspension. After 4 weeks of suspension, right and left muscles were removed and fibre type composition and total fibre number were examined by histochemical myosin adenosine triphosphatase staining sections. Myosin HC isoforms were analysed by sodium dodecyl sulphate polyacrylamide gel electrophoresis. After the suspension, there was a significant decrease in the percentage of type I fibres and a concomitant increase in that of type IIa fibres. However, the total number of fibres was not affected by suspension. The synthesis of HC IId isoform, which was not found in the control, and the decrease in the ratio of slow type myosin heavy chain isoform (HC I) were observed after suspension. These results would may suggest that the change of fibre type composition was caused by a shift from type I to IIa fibres after suspension. Furthermore, it could be suggested that the synthesis of HC IId isoform occurred during the stage of type shift from type I to IIa fibres.

Authors+Show Affiliations

Faculty of General Education, Kumamoto University, Japan.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

8330615

Citation

Oishi, Y. "Relationship Between Myosin Heavy Chain IId Isoform and Fibre Types in Soleus Muscle of the Rat After Hindlimb Suspension." European Journal of Applied Physiology and Occupational Physiology, vol. 66, no. 5, 1993, pp. 451-4.
Oishi Y. Relationship between myosin heavy chain IId isoform and fibre types in soleus muscle of the rat after hindlimb suspension. Eur J Appl Physiol Occup Physiol. 1993;66(5):451-4.
Oishi, Y. (1993). Relationship between myosin heavy chain IId isoform and fibre types in soleus muscle of the rat after hindlimb suspension. European Journal of Applied Physiology and Occupational Physiology, 66(5), 451-4.
Oishi Y. Relationship Between Myosin Heavy Chain IId Isoform and Fibre Types in Soleus Muscle of the Rat After Hindlimb Suspension. Eur J Appl Physiol Occup Physiol. 1993;66(5):451-4. PubMed PMID: 8330615.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Relationship between myosin heavy chain IId isoform and fibre types in soleus muscle of the rat after hindlimb suspension. A1 - Oishi,Y, PY - 1993/1/1/pubmed PY - 1993/1/1/medline PY - 1993/1/1/entrez SP - 451 EP - 4 JF - European journal of applied physiology and occupational physiology JO - Eur J Appl Physiol Occup Physiol VL - 66 IS - 5 N2 - The relationship between the myosin heavy chain (HC) IId isoform and histochemically defined fibre types was investigated in the rat soleus muscle after hindlimb suspension. After 4 weeks of suspension, right and left muscles were removed and fibre type composition and total fibre number were examined by histochemical myosin adenosine triphosphatase staining sections. Myosin HC isoforms were analysed by sodium dodecyl sulphate polyacrylamide gel electrophoresis. After the suspension, there was a significant decrease in the percentage of type I fibres and a concomitant increase in that of type IIa fibres. However, the total number of fibres was not affected by suspension. The synthesis of HC IId isoform, which was not found in the control, and the decrease in the ratio of slow type myosin heavy chain isoform (HC I) were observed after suspension. These results would may suggest that the change of fibre type composition was caused by a shift from type I to IIa fibres after suspension. Furthermore, it could be suggested that the synthesis of HC IId isoform occurred during the stage of type shift from type I to IIa fibres. SN - 0301-5548 UR - https://www.unboundmedicine.com/medline/citation/8330615/Relationship_between_myosin_heavy_chain_IId_isoform_and_fibre_types_in_soleus_muscle_of_the_rat_after_hindlimb_suspension_ DB - PRIME DP - Unbound Medicine ER -