Embryonic myosin heavy chain as a differentiation marker of developing human skeletal muscle and rhabdomyosarcoma

Schiaffino, Stefano; Gorza, Luisa; Sartore, Saverio; Saggin, Leopoldo; Carli, Modesto

doi:10.1016/0014-4827(86)90574-4

Cited by 89 publications

(54 citation statements)

References 20 publications

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“…b ϩ , Positive reaction for that MAb with that specific MHC isoform; Ϫ , no reaction between MAb and MHC isoform. c Antibody BF-G6 reacts primarily with the embryonic MHC isoform, but it also binds MHC IIB at a lower affinity (Schiaffino et al 1986). …”

Section: Methodsmentioning

confidence: 99%

Evidence for Three Fast Myosin Heavy Chain Isoforms in Type II Skeletal Muscle Fibers in the Adult Llama (Lama glama)

Graziotti

Ríos

Rivero

2001

J Histochem Cytochem.

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(J-LLR)S U M M A R Y Skeletal muscle fiber types classified on the basis of their content of different myosin heavy chain (MHC) isoforms were analyzed in samples from hindlimb muscles of adult sedentary llamas ( Lama glama ) by correlating immunohistochemistry with specific anti-MHC monoclonal antibodies, myofibrillar ATPase (mATPase) histochemistry, and quantitative histochemistry of fiber metabolic and size properties. The immunohistochemical technique allowed the separation of four pure (i.e., expressing a unique MHC isoform) muscle fiber types: one slow-twitch (Type I) and three fast-twitch (Type II) phenotypes. The same four major fiber types could be objectively discriminated with two serial sections stained for mATPase after acid (pH 4.5) and alkaline (pH 10.5) preincubations. The three fast-twitch fiber types were tentatively designated as IIA, IIX, and IIB on the basis of the homologies of their immunoreactivities, acid denaturation of their mATPase activity, size, and metabolic properties expressed at the cellular level with the corresponding isoforms of rat and horse muscles. Acid stability of their mATPase activity increased in the rank order IIA Ͼ IIX Ͼ IIB. The same was true for size and glycolytic capacity, whereas oxidative capacity decreased in the same rank order IIA Ͼ IIX Ͼ IIB. In addition to these four pure fibers (I, IIA, IIX, and IIB), four other fiber types with hybrid phenotypes containing two (I ϩ IIA, IIAX, and IIXB) or three (IIAXB) MHCs were immunohistochemically delineated. These frequent phenotypes (40% of the semitendinosus muscle fiber composition) had overlapped mATPase staining intensities with their corresponding pure fiber types, so they could not be delineated by mATPase histochemistry. Expression of the three fast adult MHC isoforms was spatially regulated around islets of Type I fibers, with concentric circles of fibers expressing MHC-IIA, then MHC-IIX, and peripherally MHC-IIB. This study demonstrates that three adult fast Type II MHC isoproteins are expressed in skeletal muscle fibers of the llama. The general assumption that the very fast MHC-IIB isoform is expressed only in small mammals can be rejected.

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Section: Methodsmentioning

confidence: 99%

Evidence for Three Fast Myosin Heavy Chain Isoforms in Type II Skeletal Muscle Fibers in the Adult Llama (Lama glama)

Graziotti

Ríos

Rivero

2001

J Histochem Cytochem.

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“…Sectioning of frozen tissue and immunostaining with anti-MHC antibodies was performed as described (Schiaffino et al 1986). Sections 10 tzm thick were stained with the following antibodies: anti-MHC-2A (antibody SC71; Schiaffino et al 1989), anti-MHC-2B (antibody BF-F3; Schiaffino et al 1989), and anti-slow MHC (antibody BAF8; Maier et al 1988).…”

Section: Histologymentioning

confidence: 99%

Inactivation of the myogenic bHLH gene MRF4 results in up-regulation of myogenin and rib anomalies.

Zhang¹,

Behringer²,

Olson³

1995

Genes Dev.

282

173

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The myogenic basic helix-loop--helix (bHLH) proteins MyoD, myf5, myogenin, and MRF4 can initiate myogenesis when expressed in nonmuscle cells. During embryogenesis, each of the myogenic bHLH genes is expressed in a unique temporospatial pattern within the skeletal muscle lineage, suggesting that they play distinct roles in muscle development. Gene targeting has shown that MyoD and myf5 play partially redundant roles in the genesis of myoblasts, whereas myogenin is required for terminal differentiation. MRF4 is expressed transiently in the somite myotome during embryogenesis and then becomes up-regulated during late fetal development to eventually become the predominant myogenic bHLH factor expressed in adult skeletal muscle. On the basis of its expression pattern, it has been proposed that MRF4 may regulate skeletal muscle maturation and aspects of adult myogenesis. To determine the function of MRF4, we generated mice carrying a homozygous germ-line mutation in the MRF4 gene. These mice showed only a subtle reduction in expression of a subset of muscle-specific genes but showed a dramatic increase in expression of myogenin, suggesting that it may compensate for the absence of MRF4 and demonstrating that MRF4 is required for the down-regulation of myogenin expression that normally occurs in postnatal skeletal muscle. Paradoxically, MRF4--null mice exhibited multiple fib anomalies, including extensive bifurcations, fusions, and supernumerary processes. These results demonstrate an unanticipated regulatory relationship between myogenin and MRF4 and suggest that MRF4 influences fib outgrowth through an indirect mechanism.

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“…Laboratory Investigation • May 2003 • Volume 83 • Number 5 (LaFramboise et al, 1990;Schiaffino et al, 1986), was detectable in small regenerating fibers 3 days after bupivacaine injection (Fig. 3a, B1 to B3).…”

Section: Expression Of Carp In Muscular Dystrophymentioning

confidence: 98%

Cardiac-Restricted Ankyrin-Repeated Protein Is Differentially Induced in Duchenne and Congenital Muscular Dystrophy

Nakada

Tsukamoto

Oka

et al. 2003

Laboratory Investigation

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Embryonic myosin heavy chain as a differentiation marker of developing human skeletal muscle and rhabdomyosarcoma

Cited by 89 publications

References 20 publications

Evidence for Three Fast Myosin Heavy Chain Isoforms in Type II Skeletal Muscle Fibers in the Adult Llama (Lama glama)

Evidence for Three Fast Myosin Heavy Chain Isoforms in Type II Skeletal Muscle Fibers in the Adult Llama (Lama glama)

Inactivation of the myogenic bHLH gene MRF4 results in up-regulation of myogenin and rib anomalies.

Cardiac-Restricted Ankyrin-Repeated Protein Is Differentially Induced in Duchenne and Congenital Muscular Dystrophy

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