|
|
||||||||
AJP - Cell Physiology, Vol 253, Issue 3 C456-C468, Copyright © 1987 by American Physiological Society
ARTICLES |
L. E. Thornell, E. Carlsson, E. Kugelberg and B. K. Grove
The isometric contraction time of 19 fast and slow rat motor units in the soleus and the anterior tibial muscles were recorded. The motor unit fibers, subsequently distinguished by glycogen depletion, were histochemically differentiated into fiber types and analyzed immunohistochemically for high molecular weight M-band proteins, as well as ultrastructurally for M-band fine structure, Z-disc width, and volume density of mitochondria. All fibers belonging to slow-twitch motor units in both the anterior tibialis and soleus muscles were histochemically classed as type 1. They lacked the Mr 165,000 M-protein, showed ultrastructurally a four-line M-band pattern, and had broad Z-discs, whereas the volume density of the mitochondria varied considerably. Muscle fibers belonging to the fast-twitch motor units were histochemically classed as types 2A and 2B in anterior tibialis and type 2A in soleus. They contained a three- or a five-line M-band pattern and medium-to-thin Z-discs in the anterior tibialis and a five-line M-band pattern and broad Z-discs in the soleus. Furthermore, the volume density of mitochondria showed considerable variation within and in between soleus and anterior tibialis type 2 fibers. As the differences in M-band composition and structure between fiber types overrode the intragroup variability in contraction times of slow and fast units within and between the two muscles, it is concluded that the M-band composition and structure is fundamentally related to whether the fiber is innervated by a slow or fast motor neuron, whereas other parameters such as contraction time, Z-disc width, and mitochondrial content of fibers of fast and slow units are relative and vary between muscles. Thus the M-band appearance can be used as a reliable marker to distinguish between fibers of slow- and fast-twitch motor units in rat leg muscles.
This article has been cited by other articles:
![]() |
R. Willmann, J. Kusch, K. R. Sultan, A. G. Schneider, and D. Pette Muscle LIM protein is upregulated in fast skeletal muscle during transition toward slower phenotypes Am J Physiol Cell Physiol, February 1, 2001; 280(2): C273 - C279. [Abstract] [Full Text] [PDF] |
||||
![]() |
T. Hornemann, M. Stolz, and T. Wallimann Isoenzyme-specific Interaction of Muscle-type Creatine Kinase with the Sarcomeric M-Line Is Mediated by NH2-terminal Lysine Charge-Clamps J. Cell Biol., June 12, 2000; 149(6): 1225 - 1234. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| Visit Other APS Journals Online |