Regenerated rat fast muscle transplanted to the slow muscle bed and innervated by the slow nerve, exhibits an identical myosin heavy chain repertoire to that of the slow muscle

The myosin heavy-chain (MHC) isoform pattern was studied by biochemical methods in the slow-twitch (soleus) and fast-twitch (gastrocnemius) muscles of adult rats during atrophy after tenotomy and recovery after tendon regeneration. The tenotomized slow muscle atrophied more than the tenotomized fast muscle. During the 12 days after tenotomy the total MHC content decreased by about 85% in the slow muscle, and only by about 35% in the fast muscle. In the slow muscle the ratio of MHC-1 to MHC-2A(2S) remained almost unchanged, showing that similar diminution of both isoforms occurs. In the fast muscle the MHC-2A/MHC-2B ratio decreased, showing the loss of MHC-2A mainly. After tendon regeneration, the slow muscle recovered earlier than the fast muscle. Full recovery of the muscles was not observed until up to 4 months later. The embryonic MHC, which seems to be expressed in denervated adult muscle fibres, was not detected by immunoblotting in the tenotomized muscles during either atrophy or recovery after tendon regeneration. The influence of tenotomy and denervation on expression of the MHC isoforms is compared. The results show that: (a) MHC-1 and MHC-2A(2S) are very sensitive to tenotomy, whereas MHC-2B is much less sensitive; (b) expression of the embryonic MHC in adult muscle seems to be inhibited by the intact neuromuscular junction.

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Red and white muscle development in the trout (Oncorhynchus mykiss) as shown by in situ hybridisation of fast and slow myosin heavy chain transcripts

Journal of Experimental Biology ◽

10.1242/jeb.204.12.2097 ◽

2001 ◽

Vol 204 (12) ◽

pp. 2097-2101 ◽

Cited By ~ 3

Author(s):

Pierre-Yves Rescan ◽

Bertrand Collet ◽

Cecile Ralliere ◽

Chantal Cauty ◽

Jean-Marie Delalande ◽

...

Keyword(s):

Myosin Heavy Chain ◽

Heavy Chain ◽

In Situ Hybridisation ◽

Slow Muscle ◽

Fast Muscle ◽

Slow Myosin ◽

Slow Myosin Heavy Chain ◽

And Migration ◽

Slow Myhc

SUMMARY The axial muscle of most teleost species consists of a deep bulk of fast-contracting white fibres and a superficial strip of slow-contracting red fibres. To investigate the embryological development of fast and slow muscle in trout embryos, we carried out single and double in situ hybridisation with fast and slow myosin heavy chain (MyHC)-isoform-specific riboprobes. This showed that the slow-MyHC-positive cells originate in a region of the somite close to the notochord. As the somite matures in a rostrocaudal progression, the slow-MyHC-positive cells appear to migrate radially away from the notochord to the lateral surface of the myotome, where they form the superficial strip of slow muscle. Surprisingly, the expression pattern of the fast MyHC showed that the differentiation of fast muscle commences in the medial domain of the somite before the differentiation and migration of the slow muscle precursors. Later, as the differentiation of fast muscle progressively spreads from the inside to the outside of the myotome, slow-MyHC-expressing cells become visible medially. Our observations that the initial differentiation of fast muscle takes place in proximity to axial structures and occurs before the differentiation and migration of slow muscle progenitors are not in accord with the pattern of muscle formation in teleosts previously described in the zebrafish Danio rerio, which is often used as the model organism in fishes.

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PLASTICITY OF SKELETAL MUSCLE STUDIED BY STEREOLOGY

Image Analysis & Stereology ◽

10.5566/ias.v23.p143-152 ◽

2011 ◽

Vol 23 (3) ◽

pp. 143

Author(s):

Ida Eržen

Keyword(s):

Skeletal Muscle ◽

Myosin Heavy Chain ◽

Satellite Cell ◽

Satellite Cells ◽

Heavy Chain ◽

Myosin Heavy Chain Isoforms ◽

Slow Muscle ◽

Fast Muscle ◽

Fast Muscles ◽

Slow And Fast Muscles

The present contribution provides an overview of stereological methods applied in the skeletal muscle research at the Institute of Anatomy of the Medical Faculty in Ljubljana. Interested in skeletal muscle plasticity we studied three different topics: (i) expression of myosin heavy chain isoforms in slow and fast muscles under experimental conditions, (ii) frequency of satellite cells in young and old human and rat muscles and (iii) capillary supply of rat fast and slow muscles. We analysed the expression of myosin heavy chain isoforms within slow rat soleus and fast extensor digitorum longus muscles after (i) homotopic and heterotopic transplantation of both muscles, (ii) low frequency electrical stimulation of the fast muscle and (iii) transposition of the fast nerve to the slow muscle. The models applied were able to turn the fast muscle into a completely slow muscle, but not vice versa. One of the indicators for the regenerative potential of skeletal muscles is its satellite cell pool. The estimated parameters, number of satellite cells per unit fibre length, corrected to the reference sarcomere length (Nsc/Lfib) and number of satellite cells per number of nuclei (myonuclei and satellite cell nuclei) (Nsc/Nnucl) indicated that the frequency of M-cadherin stained satellite cells declines in healthy old human and rat muscles compared to young muscles. To access differences in capillary densities among slow and fast muscles and slow and fast muscle fibres, we have introduced Slicer and Fakir methods, and tested them on predominantly slow and fast rat muscles. Discussing three different topics that require different approach, the present paper reflects the three decades of the development of stereological methods: 2D analysis by simple point counting in the 70's, the disector in the 80's and virtual spatial probes in the 90's. In all methods the interactive computer assisted approach was utilised.

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Regenerated rat fast muscle transplanted to the slow muscle bed and innervated by the slow nerve, exhibits an identical myosin heavy chain repertoire to that of the slow muscle

Histochemistry and Cell Biology ◽

10.1007/bf02473309 ◽

1996 ◽

Vol 106 (5) ◽

pp. 473-479 ◽

Cited By ~ 13

Author(s):

Erika Snoj-Cvetko ◽

Janez Sketelj ◽

Igor Dolenc ◽

Slavko Obreza ◽

Chantal Janmot ◽

...

Keyword(s):

Myosin Heavy Chain ◽

Heavy Chain ◽

Slow Muscle ◽

Fast Muscle

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The thermal acclimation of burst escape performance in fish: an integrated study of molecular and cellular physiology and organismal performance

Journal of Experimental Biology ◽

10.1242/jeb.198.10.2165 ◽

1995 ◽

Vol 198 (10) ◽

pp. 2165-2175 ◽

Cited By ~ 9

Author(s):

T Johnson ◽

A Bennett

Keyword(s):

Myosin Heavy Chain ◽

Heavy Chain ◽

Thermal Acclimation ◽

Fast Muscle ◽

Acclimation Temperature ◽

Myofibrillar Atpase ◽

Escape Performance ◽

Physiological Properties ◽

Isoform Expression ◽

Fast Twitch

Goldfish (Family Cyprinidae, Carassius auratus) and killifish (Family Cyprinodontidae, Fundulus heteroclitus) were acclimated to 10, 20 and 35 °C for 4 weeks. The thermal acclimation of C-start (escape swimming) performance and the physiological properties of fast twitch muscle fibres that underlie it were investigated in these species at the molecular (myosin isoform expression), biochemical (myofibrillar ATPase activity), cellular (contractile kinetics) and organismal levels of organisation. Peptide maps were obtained for fast muscle myosin heavy chains, isolated from 10 °C- and 35 °C-acclimated fish. Different myosin heavy chain isoforms were expressed in response to a change in acclimation temperature in goldfish, but myosin heavy chain isoform expression was unaffected by acclimation temperature in killifish. Compared with fish acclimated to 35 °C, acclimation to 10 °C increased the activity of fast muscle myofibrillar ATPase assayed at 10 °C fivefold in goldfish and only 50 % in killifish. Muscle twitch contraction time at 10 °C decreased significantly in response to acclimation to 10 °C in both species; however, the magnitude of this response was much greater in goldfish (100 %) than in killifish (30 % or less). In goldfish, these changes in the physiological properties of fast twitch fibres during 10 °C acclimation resulted in a six- to eightfold increase in the speed and turning velocity of fish performing C-starts at 10 °C. By comparison, the somewhat smaller acclimatory response of killifish fast muscle properties was accompanied by only a minor (50 % or less) adjustment in locomotor performance. Thermal acclimatory responses of fast muscle at the molecular, biochemical and cellular levels of organisation are clearly reflected in alterations in organismal escape performance.

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