Developmental appearance of myosin heavy and light chain isoforms in vivo and in vitro in chicken skeletal muscle

Bandman, Everett; Matsuda, Ryoichi; Strohman, Richard C.

doi:10.1016/0012-1606(82)90138-5

Cited by 178 publications

(85 citation statements)

References 39 publications

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“…Thus, the epitopes recognized by S58 and F59 define slow and fast classes of MHC isoforms that are found at all developmental ages. Each class of MHC contains an unknown number of developmentally regulated isoforms (5,(28)(29)(30)(31)(32). In the discussion that follows, therefore, designation of a MHC as either fast class or slow class is understood to mean specifically that the MHC under consideration has a particular electrophoretic mobility and immunological reactivity that is shared by a number of isoforms within the class.…”

Section: Methodsmentioning

confidence: 99%

Developmental origins of skeletal muscle fibers: clonal analysis of myogenic cell lineages based on expression of fast and slow myosin heavy chains.

Miller¹,

Stockdale²

1986

Proc. Natl. Acad. Sci. U.S.A.

148

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A clonal analysis was used to show that skeletal muscle myoblasts are committed to distinct cell lineages during development. Myoblasts taken from embryonic chicken hindlimb muscles of different ages were cultured at clonal density. The content offast and slow classes of the myosin heavy chain isoforms in the myotubes of the resulting muscle colonies was determined immunocytochemically with specific monoclonal antibodies that served as markers for the different fiber types. The muscle colonies formed by cloning myoblasts from early hindlimbs (days 4-6 in ovo) were of three types: the most numerous type, in which all myotubes in a colony contained only the fast class of myosin heavy chain; a less numerous type, in which all myotubes in a colony contained both the fast and slow classes of myosin heavy chain isoforms; and a rare type, in which all myotubes in a colony contained only the slow class of myosin heavy chain. The muscle colonies formed by cloning myoblasts from later hindlimbs (days 10-12 in ovo) were, however, all of one type, in which every myotube in a colony contained only fast myosin heavy chain. Thus, myoblasts in the early embryo (days 4-6 in ovo) were a heterogeneous population committed to three myogenic lineages: fast, mixed fast/slow, and slow, whereas myoblasts from the later embryo (days 10-12 in ovo) were only in the fast myogenic lineage. These results suggest that muscle fiber formation is rooted in two developmental phases-an early phase in which diverse fiber types are formed from intrinsically diverse populations of myoblasts and a later phase in which fibers are formed from a single population of myoblasts.The analysis of cell lineage is a central problem in developmental biology. To understand the molecular and cellular mechanisms underlying differentiation of a particular cell type, it is necessary to identify and isolate the immediate precursors ofthe differentiated cell of interest. One system in which the analysis of cell lineage has presented a long-standing problem is the formation of the three muscle cell types of skeletal muscle: the fast, mixed fast/slow, and slow muscle fibers which are described below. Two models-one requiring a single myogenic lineage and a second requiring multiple myogenic lineages-could explain muscle fiber diversification (1). It has usually been assumed that all muscle fibers arise from a single myoblast population, with diversification specified later by the type of innervation the fibers received. The experimental justification for this assumption has not, however, been compelling, and the alternative model, that fast, mixed fast/slow, and slow fibers form from separate myoblast populations, has remained an open possibility (1). Recent results led us to reexamine myogenic lineages in muscle fiber diversification.Adult muscles in birds and mammals contain a heterogeneous population of muscle fibers with fast, mixed, and slow properties. Although first defined physiologically, these fiber types can now be defined biochemically by the presence...

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Section: Methodsmentioning

confidence: 99%

Developmental origins of skeletal muscle fibers: clonal analysis of myogenic cell lineages based on expression of fast and slow myosin heavy chains.

Miller¹,

Stockdale²

1986

Proc. Natl. Acad. Sci. U.S.A.

148

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“…The frozen bacterial pellets were thawed on ice, resuspended in low salt buffer (20 mM KCl, 2 mM KH 2 PO 4 , 1 mM EGTA, pH 6.8), 10 mM DTT, 0.1 mM phenylmethylsulfonyl fluoride in 1/40 of the volume of the bacterial culture, and sonicated on ice to decrease viscosity. The LMM proteins were purified according to the method previously described to purify myosin from chicken muscle (34), and further purified by gel permeation chromatography under denaturing conditions. The LMM preparations were denatured by dialysis against 4 M (or 6 M) GdmCl, 40 mM NaPP i , pH 7.5, 10 mM DTT, centrifuged (14,000 ϫ g, 15 min., 4°C), and the supernatant loaded onto a Bio-Gel A-15m (Bio-Rad) column (2 ϫ 50 cm) equilibrated with the same buffer.…”

Section: Cloning Of Recombinant Lmms-recombinantmentioning

confidence: 99%

Regulation of α-Helical Coiled-coil Dimerization in Chicken Skeletal Muscle Light Meromyosin

Arrizubieta

Bandman

1999

Journal of Biological Chemistry

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The dimerization specificity of the light meromyosin (LMM) domain of chicken neonatal and adult myosin isoforms was analyzed by metal chelation chromatography. Our results show that neonatal and adult LMMs associate preferentially, although not exclusively, as homodimeric coiled-coils. Using chimeric LMM constructs combining neonatal and adult sequences, we observed that a stretch of 183 amino acids of sequence identity at the N terminus of the LMM was sufficient to allow the adult LMM to dimerize in a non-selective manner. In contrast, sequence identity in the remaining C-terminal 465 amino acids had only a modest effect on the dimerization selectivity of the adult isoform. Sequence identity at the N terminus also promoted dimerization of the neonatal LMM to a greater degree than sequence identity at the C terminus. However, the N terminus had only a partial effect on the dimerization specificity of the neonatal sequence, and residues distributed throughout the LMM were capable of affecting dimerization selectivity of this isoform. These results indicated that dimerization preference of the neonatal and adult isoforms was affected to a different extent by sequence identity at a given region of the LMM.

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“…The most detailed results have been obtained in birds (Bandman et al, 1982;Crow and Stockdale, 1986;Miller and Stockdale, 1986; for reviews, see Stockdale and Miller, 1987, and Stockdale, 1990), in small mammals, such as mice (Rubinstein and Kelly, 1981;Whalen et al, 1981;Lyons et al 1983;Vivarelli et al, 1988) and cats (Hoh and Hughes, 1989). Studies have also been made on the human fetus (Pons et al, 1986;Draeger et al, 1987 39,53,64,84,98,122,143,180,224 Pons et al (1986).…”

mentioning

confidence: 99%

Myosin expression in semitendinosus muscle during fetal development of cattle: immunocytochemical and electrophoretic analyses

Robelin¹,

Picard²,

Listrat³

et al. 1993

Reprod. Nutr. Dev.

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Developmental appearance of myosin heavy and light chain isoforms in vivo and in vitro in chicken skeletal muscle

Cited by 178 publications

References 39 publications

Developmental origins of skeletal muscle fibers: clonal analysis of myogenic cell lineages based on expression of fast and slow myosin heavy chains.

Developmental origins of skeletal muscle fibers: clonal analysis of myogenic cell lineages based on expression of fast and slow myosin heavy chains.

Regulation of α-Helical Coiled-coil Dimerization in Chicken Skeletal Muscle Light Meromyosin

Myosin expression in semitendinosus muscle during fetal development of cattle: immunocytochemical and electrophoretic analyses

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