Accumulation of Newly Synthesized Myosin Heavy Chain during Thyroxine-Induced Myofiber Type Transition

Ce, Carpenter; Ml, Greaser; Rg, Cassens

doi:10.2527/jas1987.6451574x

Cited by 7 publications

(2 citation statements)

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“…A uniform emergence of newly-synthesized heavy chain throughout already existing myofbrils has been reported in slow-to-fast fibre type transitions in adult muscle induced by either electrical stimulation (rabbit) or by thyroxine (chicken) indicating that such mechanisms do exist (Franchi et al, 1990;Carpenter et al, 1987). It should be noted, however, that the experimentallyinduced transitions occurred over many weeks and were thus much slower that the first two developmental transitions described in the present study.…”

Section: Discussioncontrasting

confidence: 49%

Developmental myosin heavy chain progression in avian type IIB muscle fibres

Rushbrook

Weiss

Yao

1991

J Muscle Res Cell Motil

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Myosin heavy chain species were investigated during development in avian pectoralis major muscles (type IIB fibres) by high resolution anion-exchange chromatography of the myosin head region, subfragment-1. At 15 days in ovo four distinct fast-type heavy chain species, I, II, III and IV, in order of elution, were identified. By 19 days in ovo, form IV had become predominant and remained the major species through 3-days post-hatch. This form has been named the peri-hatch form. Between 3 and 5 days post-hatch, a second massive change occurred such that by 5 days post-hatch a new species, V, apparent at 19 days in ovo in small amounts, dominated and at 8 days post-hatch was the only heavy chain species present. Form V, which corresponds to that previously identified as the post-hatch form, continued as the major species through 20 days post-hatch and was replaced slowly by the adult form. N-terminal sequencing of CNBr peptides from three subfragment-1 heavy chain species, the peri-hatch (form IV), the post-hatch (form V) and adult, revealed differences in amino acid sequence consistent with the three being products of different genes. These results confirm and extend recent reports of complexity in fast heavy chain expression prior to hatching in the chicken (Hofmann et al., 1988; Van Horn & Crow, 1989).

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Section: Discussioncontrasting

confidence: 49%

Developmental myosin heavy chain progression in avian type IIB muscle fibres

Rushbrook

Weiss

Yao

1991

J Muscle Res Cell Motil

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“…We observed a fast-to slow-myosin light chain transition with AIM-V after the formation of a myooid. It is well known that muscle fiber type conversion occurs with a stimulation pattern (Salmons and Sreter, 1976), or chemicals such as a b 2 -receptor agonist (Zeman et al, 1988) and thyroxine (Carpenter et al, 1987). Although the ingredients of AIM-V are disclosed, insulin and purified noncytokine factors as well as proteins such as albumin and transferrin are present in the medium (Helinski et al, 1988).…”

Section: Discussionmentioning

confidence: 99%

Novel method for fabrication of skeletal muscle construct from the C2C12 myoblast cell line using serum‐free medium AIM‐V

Fujita

Shimizu

Nagamori

2009

Biotech & Bioengineering

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We have fabricated muscle tissue from murine myoblast cell line C2C12 by modifying the previously reported method. Fabrication of skeletal muscle tissue has been performed in many ways including the use of a biodegradable scaffold, a collagen gel-embedded culture, or cell sheet tissue engineering, but the extent of tension generation remains low. Recently, a new skeletal muscle tissue engineering technique involving self-dissociation of a cell sheet from a laminin-coated polydimethylsiloxane surface was reported which mostly involved a primary cell culture or co-culture of C2C12 and 10T1/2 cells. In this study, we succeeded in fabricating muscle tissue using C2C12 cells alone by enhancing cell-cell attachment by the use of serum-free medium AIM-V. C2C12 cells were seeded on to a laminin-coated PDMS surface in a 35 mm culture dish with two silk sutures of 5 mm in length each pinned at two places 18 mm apart. Then, cells were allowed to differentiate in AIM-V, and the cells started to dissociate in a sheet-like manner after 5-8 days of differentiation. The cells remained attached to the silk sutures, and tissue having a cylindrical morphology was fabricated. After the cylindrical morphology had been obtained, the medium was changed to DMEM supplemented with 2% horse serum, followed by culture for an additional 5-8 days for maturation. Tissue fabricated using this method was excitable with electric pulse stimulation and the generated active tension was approximately 1.4x greater than that reported previously for a co-culture of C2C12 and 10T1/2 cells. Immuno-fluorescence study revealed the presence of a sarcomere structure within the fabricated tissue, and Western blotting confirmed the expression of muscle specific-proteins. The increased active tension generation compared to that with the previously reported method is probably attributable to the increased proportion of myogenic cells in the tissue. Myooid fabricated from mono-culture of C2C12 will be useful in the muscle study, especially in the area where gene modification is needed.

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