Effects of ammonium ions on the depolarization-induced and direct activation of the contractile apparatus in mechanically skinned fast-twitch skeletal muscle fibres of the rat

1996 ◽  
Vol 17 (6) ◽  
pp. 611-616 ◽  
Author(s):  
Gabriela M. M. Stephenson ◽  
D. George Stephenson
1998 ◽  
Vol 435 (6) ◽  
pp. 753-761 ◽  
Author(s):  
C. Veigel ◽  
R. D. von Maydell ◽  
K.R. Kress ◽  
J. E. Molloy ◽  
R. H. A. Fink

1984 ◽  
Vol 222 (1228) ◽  
pp. 401-408 ◽  

An analysis has been performed of the native myosin isoenzyme com position of isolated skeletal muscle fibres from Xenopus laevis with welldefined isotonic contraction properties. Fast twitch ‘ white ’ (type 1) fibres contained three isomyosins; fast twitch ‘red ’ (type 2) fibres showed two major myosin bands with migration velocities very similar to those of the two slower bands in type 1. Slow twitch (type 3) fibres yielded a single, slowly migrating band as did slow tonic (type 5) fibres, whereas the myosin from type 4 (very slow twitch, ‘intermediate’) fibres migrated with a somewhat higher mobility. The results suggest that amphibian skeletal muscle may possess the principal fibre types found in mammals and birds.


2009 ◽  
Vol 459 (4) ◽  
pp. 631-644 ◽  
Author(s):  
Norbert Weiss ◽  
Tina Andrianjafiniony ◽  
Sylvie Dupré-Aucouturier ◽  
Sandrine Pouvreau ◽  
Dominique Desplanches ◽  
...  

2005 ◽  
Vol 53 (4) ◽  
pp. 237
Author(s):  
Anthony J. Bakker ◽  
Ann L. Parkinson ◽  
Stewart I. Head

Eutherian mammal fast-twitch muscle fibres share similar contractile activation properties, suggesting that these properties are highly conserved in mammals. To investigate this hypothesis, we examined the contractile properties of skeletal muscle from the order Monotremata, a mammalian order that separated from eutherians 150 million years ago. The Ca2+- and Sr2+-activation properties of single mechanically skinned skeletal muscle fibres from the extensor digitorum longus (EDL) muscle of the short-nosed echidna were determined. Sigmoidal curves fitted to force response data plotted as a function of pCa (–log[Ca2+]), had a mean slope of 4.32 ± 0.28 and a mean pCa50 and pCa10 value of 6.18 ± 0.01 and 6.41 ± 0.02 respectively (n = 20). The mean pSr50, pSr10 and slope values of curves fitted to the force-response data after activation with Sr2+ were 4.80 ± 0.03, 5.29 ± 0.07 and 2.75 ± 0.18 respectively (n = 20). The mean pCa50–pSr50 value for the echidna EDL fibres was 1.37 ± 0.04. In five of the echidna fibres, exposure to submaximal Ca2+ concentrations produced myofibrillar force oscillations (mean frequency, 0.13 ± 0.01 Hz), a phenomenon found only in eutherian slow and intermediate muscle fibres. These results show that echidna EDL fibres generally have similar contractile properties to eutherian fast-twitch skeletal muscle fibres, such as those found in the EDL of the rat.


2004 ◽  
Vol 378 (1) ◽  
pp. 269-274 ◽  
Author(s):  
Brett O'CONNELL ◽  
Long T. NGUYEN ◽  
Gabriela M. M. STEPHENSON

In the present study, we investigated the possibility that MHC (myosin heavy chain) and TnC (troponin C) isoforms exist in specific combinations in rat-skeletal-muscle fibres. Single fibres (numbering 245) from soleus (predominantly slow-twitch) and sternomastoid (predominantly fast-twitch) muscles of adult rats were analysed for MHC and TnC isoform composition, using alanine-SDS/PAGE for separating MHC isoforms, and a novel method (based on the previously reported influence of Ca2+ on the mobility of Ca2+-binding proteins in SDS gels) for unequivocal identification of TnC isoforms in single-fibre segments. In this study, all fibres that contained only one MHC isoform (slow or fast) contained only the matching TnC isoform and all fibres that contained multiple fast MHC isoforms contained only the fast TnC isoform. Fibres expressing both slow and fast MHC isoforms displayed either both TnC isoforms or only one TnC isoform of a type depending on the relative proportion of fast/slow MHC present. Our results suggest a close relationship between MHC and TnC isoform composition in non-transforming skeletal muscles of adult rat.


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