Literature DB >> 3631252

Myofibrillar M-band structure and composition of physiologically defined rat motor units.

L E Thornell, E Carlsson, E Kugelberg, B K Grove.   

Abstract

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.

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Year:  1987        PMID: 3631252     DOI: 10.1152/ajpcell.1987.253.3.C456

Source DB:  PubMed          Journal:  Am J Physiol        ISSN: 0002-9513


  9 in total

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2.  Fiber type-specific distribution of parvalbumin in rabbit skeletal muscle. A quantitative microbiochemical and immunohistochemical study.

Authors:  T L Schmitt; D Pette
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Authors:  H T Pask; K L Jones; P K Luther; J M Squire
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4.  Diversity in expression of myosin heavy chain isoforms and M-band proteins in rat muscle spindles.

Authors:  F Pedrosa; G S Butler-Browne; G K Dhoot; D A Fischman; L E Thornell
Journal:  Histochemistry       Date:  1989

5.  Myofibrillar M-band proteins in rat skeletal muscles during development.

Authors:  E Carlsson; B K Grove; T Wallimann; H M Eppenberger; L E Thornell
Journal:  Histochemistry       Date:  1990

6.  Protein differences between human trapezius and vastus lateralis muscles determined with a proteomic approach.

Authors:  Jenny Hadrévi; Fredrik Hellström; Thomas Kieselbach; Christer Malm; Fatima Pedrosa-Domellöf
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7.  Isoenzyme-specific interaction of muscle-type creatine kinase with the sarcomeric M-line is mediated by NH(2)-terminal lysine charge-clamps.

Authors:  T Hornemann; M Stolz; T Wallimann
Journal:  J Cell Biol       Date:  2000-06-12       Impact factor: 10.539

Review 8.  Fibre typing of intrafusal fibres.

Authors:  Lars-Eric Thornell; Lena Carlsson; Per-Olof Eriksson; Jing-Xia Liu; Catharina Österlund; Per Stål; Fatima Pedrosa-Domellöf
Journal:  J Anat       Date:  2015-08       Impact factor: 2.610

9.  Comparative analysis of the transcriptomes of EDL, psoas, and soleus muscles from mice.

Authors:  Pabodha Hettige; Uzma Tahir; Kiisa C Nishikawa; Matthew J Gage
Journal:  BMC Genomics       Date:  2020-11-19       Impact factor: 3.969

  9 in total

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