Pattern of Myosin Heavy Chain Isoforms in Different Fibre Types of Canine Trunk and Limb Skeletal Muscles

2004 ◽  
Vol 176 (4) ◽  
pp. 178-186 ◽  
Author(s):  
M. Štrbenc ◽  
V. Smerdu ◽  
M. Županc ◽  
N. Tozon ◽  
G. Fazarinc
Meat Science ◽  
2004 ◽  
Vol 67 (1) ◽  
pp. 87-94 ◽  
Author(s):  
K Chikuni ◽  
S Muroya ◽  
I Nakajima

1996 ◽  
Vol 139 (1) ◽  
pp. 15-21 ◽  
Author(s):  
Yasuharu Oishi ◽  
Hideyuki Yamamoto ◽  
Megumi Nagano ◽  
Eishichi Miyamoto ◽  
Makoto Futatsuka

1990 ◽  
Vol 68 (5) ◽  
pp. 596-602 ◽  
Author(s):  
David J. Parry ◽  
Ross S. Wilkinson

The distribution of fibre types in the tibialis anterior (TA) muscle of adult mice was examined by means of an immuno-histochemical approach, using monoclonal antibodies that recognize different myosin heavy chain isoforms. As has been reported previously, the superficial portion of TA contains almost exclusively type IIB fibres and is almost entirely glycolytic in nature. Following section of the lateral popliteal nerve and rotation of the proximal stomp to prevent rematching, it was found that the original pattern was virtually restored within 2 months. One possible explanation for this observation is that the activity pattern of peripheral and deep muscle fibres differs and that this aids in specification of muscle fibre type. Alternatively, the muscle fibres of the superficial portion of TA may be inherently resistant to an alteration of their phenotype with regard to expression of myosin heavy chain.Key words: myosin heavy chain, immunohistochemistry, plasticity, self-reinnervation, fibre types.


2002 ◽  
Vol 2002 ◽  
pp. 175-175 ◽  
Author(s):  
A. Q. Sazili ◽  
T. Parr ◽  
P. L. Sensky ◽  
S.W. Jones ◽  
R.G. Bardsley ◽  
...  

The characterisation of muscle fibres has become increasingly important as the proportion of slow and fast fibre types are known to influence the biochemical and physiological properties of muscle during postmortem tenderisation (Ouali and Talmant, 1990). Current histochemical methods are labour intensive, time consuming and hazardous, requiring rapid freezing of samples in isopentane cooled in liquid nitrogen. The purpose of this study was to investigate an alternative immunochemical approach for identifying fibre types by examining the expression of slow myosin heavy chain (MHC-s) and fast myosin heavy chain (MHC-f) and comparing the data with classical histochemical techniques. Five different ovine skeletal muscles with known differences in fibre types distribution were studied.


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