Structure-function relationship of soleus muscle fibres from the rhesus monkey
โ Scribed by C. Cordonnier; L. Stevens; F. Picquet; Y. Mounier
- Publisher
- Springer
- Year
- 1995
- Tongue
- English
- Weight
- 1014 KB
- Volume
- 430
- Category
- Article
- ISSN
- 0031-6768
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โฆ Synopsis
Functional and structural properties of rhesus monkey skinned fibres were studied in order to examine the relationship between calcium/strontium (Ca/St) activation characteristics and protein composition. The fibres were classified according to their Ca/Sr affinity into slow (61%) and fast groups (39%). According to the myosin isoform composition, two additional hybrid types were defined. Thus, four profiles were characterized: two corresponding to slow (S) and fast (F) isoforms and two corresponding to a mixed proportion of slow and fast isoforms. They were called hybrid slow (HS) or hybrid fast (HF) based on the predominant myosin isoform. Tension/pCa parameters and maximal shortening velocities were determined. S fibres showed a higher pCa threshold and affinity as well as shallower slopes of their tension/pCa curve than did F fibres. HS and HF fibres exhibited tension/pCa curves which were positioned close to those of S and F fibres, respectively. No significant difference was observed between S and HS fibres or between F and HF fibres. Maximal shortening velocity values were higher for fibres expressing predominantly fast myosin isoforms. We suggest than when both S and F isoforms of myofibrillar proteins are expressed in a muscle fibre, the functional properties are mainly governed by the predominant isoform.
๐ SIMILAR VOLUMES
## C T I O N Src Homology 2 (SH2) domains are protein modules of about 100 amino acids in size which are found in a large number of proteins involved in signal transduction. The function of SH2 domains is to specifically recognize the phosphorylated state of tyrosine residues, thereby allowing SH