The synthesis and distribution of desmin and vimentin during myogenesis in vitro

Gard, David L.; Lazarides, Elias

doi:10.1016/0092-8674(80)90408-0

Cited by 300 publications

(233 citation statements)

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“…Allen et al (1) have also demonstrated that the accumulation of major myofibrillar proteins--myosin, actin, tropomyosin, and a-actinin--occurs shortly after myoblast fusion. The synthesis of desmin, an intermediate filament protein located at the periphery of each Z disk, is initiate at the onset of myoblast fusion, whereas another intermediate filament protein, vimentin, is synthesized in dividing myoblasts and the two proteins continue to be synthesized in skeletal muscle culture (19). Immunofluorescent staining with anti desmin and anti vimentin also supports the above facts (19,47,48).…”

Section: Discussionsupporting

confidence: 53%

“…During the course of myogenesis of cultured skeletal muscle cells, the synthesis of many of the major structural proteins of myofibrils--myosin, a-actin, tropomyosin, troponin components, and desmin--is first detected coordinately at about the time that myoblast fusion normally takes place and then rapidly increases (11,19). Allen et al (1) have indicated that a-actinin, as well as myosin, actin, and tropomyosin, accumulates shortly after fusion.…”

mentioning

confidence: 99%

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Differential expression and distribution of chicken skeletal- and smooth-muscle-type alpha-actinins during myogenesis in culture.

Endo¹,

Takao²

1984

The Journal of Cell Biology

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Antibodies to chicken fast skeletal muscle (pectoralis) a-actinin and to smooth muscle (gizzard) a-actinin were absorbed with opposite antigens by affinity chromatography, and four antibody fractions were thus obtained: common antibodies reactive with both pectoralis and gizzard a-actinins ([C]anti-P a-An and [C]anti-G a-An), antibody specifically reactive with pectoralis a-actinin ([S]anti-P a-An), and antibody specifically reactive with gizzard a-actinin ([S]anti-G a-An). In indirect immunofluorescence microscopy, (C)anti-P aAn, (S)anti-P a-An, and (C)anti-G a-An stained Z bands of skeletal muscle myofibrils, whereas (S)anti-G a-An did not. Although (S)anti-G a-An and two common antibodies stained smooth muscle cells, (S)anti-P u-An did not. We used (S)anti-P a-An and (S)anti-G a-An for immunofluorescence microscopy to investigate the expression and distribution of skeletal-and smoothmuscle-type a-actinins during myogenesis of cultured skeletal muscle cells. Skeletal-muscletype a-actinin was found to be absent from myogenic cells before fusion but present in them after fusion, restricted to Z bodies or Z bands. Smooth-muscle-type ~-actinin was present diffusely in the cytoplasm and on membrane-associated structures of mononucleated and fused myoblasts, and then confined to membrane-associated structures of myotubes. Immunoblotting and peptide mapping by limited proteolysis support the above results that skeletalmuscle-type a-actinin appears at the onset of fusion and that smooth-muscle-type a-actinin persists throughout the myogenesis. These results indicate (a) that the timing of expression of skeletal-muscle-type a-actinin is under regulation coordinate with other major skeletal muscle proteins; (b) that, with respect to expression and distribution, skeletal-muscle-type a-actinin is closely related to a-actin, whereas smooth-muscle-type a-actinin is to 3'-and ~-actins; and (c) that skeletal-and smooth-muscle4ype a-actinins have complementary distribution and do not co-exist in situ.a-Actinin, which was discovered by Ebashi and Ebashi (12), is a structural protein of Z bands in skeletal muscle myofibrils (33). It is also located near the fascia adherens of intercalated disks as well as in Z bands in cardiac muscle (44). In smooth muscle, it is present in cytoplasmic dense bodies and membrane-associated dense plaques (21,41). Proteins immunologically and biochemically related to a-actinin have been isolated from several nonmuscle tissues or cells: bovine brain (42), Ehrlich tumor cells (36,37), plasma membranes of sarcoma 180 ascites cells (46), HeLa cells (6), human platelets (40), rat liver (29), and porcine kidney (28). Many of these proteins, if not all, are Ca 2+ sensitive, i.e., are inhibited from cross-linking actin filaments by Ca 2+, different from any of the muscle a-actinins. Immunofluorescence microscopy, immunoelectron microscopy, and microinjection using fluorescence-labeled a-actinin have revealed that a-actinin or proteins immunologically related to a-actinin are also present in cultur...

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Section: Discussionsupporting

confidence: 53%

mentioning

confidence: 99%

Differential expression and distribution of chicken skeletal- and smooth-muscle-type alpha-actinins during myogenesis in culture.

Endo¹,

Takao²

1984

The Journal of Cell Biology

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“…The present study shows that human ciliary muscle not only stains for the musclespecific intermediate filament desmin, but also for vimentin. The same is the case for skeletal myoblasts in culture (Gard and Lazarides, 1980) and in tissue sections (Van Muijen, Ruiter and Warnaar, 1987). as baskets around the nucleus and extend in gently curved arrays towards the cells' periphery ( x 900).…”

Section: Discussionmentioning

confidence: 68%

Cell cultures of human ciliary muscle: Growth, ultrastructural and immunocytochemical characteristics

Tamm

Flügel

Baur

et al. 1991

Experimental Eye Research

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Primary ciliary muscle cell cultures derived from human donors (16-9 1 years) were established and characterized by comparing them with ciliary muscle in tissue sections using immunocytochemical and ultrastructural methods. Monoclonal antibodies against desmin, vimentin, a-actinin, smooth muscle (sm) specific a-actin and von Willebrand factor were used. In tissue sections of the ciliary body, ciliary muscle cells, vascular muscle cells, pericytes, endothelial cells and fibroblasts stain for vimentin. Both types of muscle cells and the pericytes stain for cr-sm-actin, but only ciliary muscle cells stain for desmin. For tissue cultures, explants of the meridional and partly the reticular portion of the ciliary muscle were dissected and grown directly or after digestion of the explant with collagenase. Ten primary cell cultures with a typical hill-and-valley growth pattern similar to smooth muscle cells and two with a growth pattern similar to fibroblasts were established. All cultures could be subcultured up to the fifth passage. In fibroblast-like cultures S-10% of the cells stained for z-sm-actin. Staining for desmin was not observed. In smooth muscle-like cultures, all cells stained positive for a-sm-actin. Desmin staining was not seen in growing non-confluent smooth muscle-like cultures. In confluent cultures, about 10% of the cells stained positive for desmin, preferentially in areas where the cells had formed hills. No culture stained for von Willebrand factor. Staining for a-actinin in smooth muscle-like cultures showed that the dense bands of the myofilaments were arranged in register, similar to the typical ciliary muscle cell morphology seen in tissue sections. Ultrastructurally, the smooth muscle-like cultures showed the typical morphology of cultured smooth muscle cells. We conclude that the smooth muscle-like cultures consist of ciliary muscle cells.

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“…In mature muscle, CIC-1 expression [24], like that of parvalbumin [23], is highly dependent on fiber types, innervation, and pattern of electrical activity [25]. On the other hand, desmin mRNA and protein are classical markers of early muscle differentiation; its expression is not nerve-dependent [26,27]. Furthermore, desmin is present in all three muscle types, smooth, cardiac and skeletal.…”

Section: Discussionmentioning

confidence: 99%

Expression of chloride channel 1 mRNA in cultured myogenic cells: a marker of myotube maturation

1996

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The chloride channel CIC-1 is required to maintain a normal excitability of mature muscle fibers; its blockade leads to hyperexcitability, the hallmark of the disease myotonia. In mouse and rat myotubes, representing the embryonic stage of muscle, CIC-1 mRNA is not detectable by Northern blotting. From neonatal to adult, CIC-1 expression increases at least fourfold. Using RT-PCR and hybridization on cultured myotubes we found CIC-1 mRNA at a level of 0.4-1.1% of that in mature mouse muscle, and -<0.01% in myoblasts, at stages when desmin mRNA levels are already high. The level of CIC-1 mRNA is thus a sensitive and specific indicator of the maturation of skeletal muscle cells.

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The synthesis and distribution of desmin and vimentin during myogenesis in vitro

Cited by 300 publications

References 41 publications

Differential expression and distribution of chicken skeletal- and smooth-muscle-type alpha-actinins during myogenesis in culture.

Differential expression and distribution of chicken skeletal- and smooth-muscle-type alpha-actinins during myogenesis in culture.

Cell cultures of human ciliary muscle: Growth, ultrastructural and immunocytochemical characteristics

Expression of chloride channel 1 mRNA in cultured myogenic cells: a marker of myotube maturation

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