Molecular cloning of two fast myosin heavy chain cDNAs from chicken embryo skeletal muscle.

Umeda, Patrick K.; Sinha, A M; Jakovcic, Smilja; Merten, S; Hsu, H J; Subramanian, K. N.; Zak, Radovan; Rabinowitz, Murray

doi:10.1073/pnas.78.5.2843

Cited by 46 publications

(25 citation statements)

References 39 publications

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“…Thereafter, the a form decreases and, in the old adult, the 3 form is present almost exclusively (12,14). In the young adult animals used in this study, the ( form/a form ratio was =4:1 (12 (27).Construction and Screening of cDNA Clones. Single-and double-stranded cDNA was synthesized by using standard procedures (28,29).…”

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confidence: 99%

“…Single-and double-stranded cDNA was synthesized by using standard procedures (28,29). The duplex cDNA was tailed (30) with dCMP and annealed with Pst I-linearized deoxyguanosine-tailed plasmid pBR322 (27). The hybrid plasmid was used to transform Escherichia coli X1776 (31).…”

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confidence: 99%

“…The hybrid plasmid was used to transform Escherichia coli X1776 (31). Clones containing inserts complementary to myosin HC mRNA were selected as described (27 The publication costs ofthis article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement in accordance with 18 U. S. C. §1734 solely to indicate this fact.…”

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Molecular cloning of mRNA sequences for cardiac alpha- and beta-form myosin heavy chains: expression in ventricles of normal, hypothyroid, and thyrotoxic rabbits.

Sinha¹,

Umeda²,

Kavinsky³

et al. 1982

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

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127

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We have isolated cDNA clones from thyrotoxic (pMHCa) and normal (pMHC(8) adult rabbit hearts. Restriction map analysis and DNA sequence analyses show that, although there is strong homology between overlapping regions of the two clones, they are distinctly different. The two clones exhibited 78483% homology between the derived amino acid sequences and those determined by direct amino acid sequence analysis of rabbit fast skeletal muscle myosin heavy chains. The clones specify a segment of the myosin heavy chain corresponding to subfragment 2 and the COOH-terminal portions of subfragment 1. Nuclease S1 mapping was used to compare transcription of the two clones with expression of the a and (3 forms of myosin heavy chains in the ventricles of thyrotoxic, hypothyroid (propylthiouracil-treated), and normal rabbits. Thyrotoxic ventricles contained only pMHCa transcripts whereas hypothyroid ventricles contained exclusively pMHC(3 transcripts. These data correlate well with the presence of a-and (3-form myosin heavy chains. In the normal young adult rabbit, pMHC(3 transcripts predominate, agreeing with the known (3 form/a form ratio of 4: 1. We therefore conclude that pMHCa and pMHCP contain sequences of the a-and (-form myosin heavy chain genes, respectively.Myosin, a major contractile protein of skeletal and cardiac muscle, is composed of two 200,000-dalton heavy chains (HCs) and two sets oflow molecular weight light chains. The active center of myosin ATPase resides in the globular head of the heavy chain. This enzymatic activity is correlated with contractile velocity in skeletal muscle (1) and thus appears to be an important determinant of contractile function. Numerous polymorphic forms of myosin HC exist, not only in different types of muscle-e.g., fast and slow skeletal and cardiac-but also within each muscle type (2-12). Expression of these forms follows a developmental pattern (12-18) that may be altered by changes in the physiological (19-21) and hormonal (10-13) milieu ofthe cell.Cardiac ventricular muscle contains at least two formsreferred to as a and (3 (9)-of myosin HC. Electrophoresis of myosin under nondenaturing conditions reveals three bands; V1 and V3 are homodimers containing the a and 3 forms, respectively, whereas V2 is a heterodimer (9, 13). The ATPase activity of myosin with a-form HCs has been shown to be considerably higher than that of myosin with (-form .The expression of a-and (3form myosin HCs follows a defined developmental pattern that varies in different animal species. It has been shown that in rabbit the ( form/a form ratio is =3: 1 during the last halfofthe gestational period. After birth, the relative amount of the a form increases so that, during the first 2 wk postnatally, this ratio is 1: 1 (12, 14). Thereafter, the a form decreases and, in the old adult, the 3 form is present almost exclusively (12,14). In the young adult animals used in this study, the ( form/a form ratio was =4:1 (12 (27).Construction and Screening of cDNA Clones. Single-and double-stranded cDNA wa...

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confidence: 99%

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confidence: 99%

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confidence: 99%

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Molecular cloning of mRNA sequences for cardiac alpha- and beta-form myosin heavy chains: expression in ventricles of normal, hypothyroid, and thyrotoxic rabbits.

Sinha¹,

Umeda²,

Kavinsky³

et al. 1982

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

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127

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“…The GenBank Accession Numbers for the gene sequences used to generate each primer pair are shown in parentheses. Primer sequences are derived from the following references: slow MyHC 1 and 2 (Chen et al, 1997), slow MyHC 3 (Yutzey et al, 1994), efast MyHC Umeda et al, 1983;Umeda et al, 1981), nfast MyHC (Machida et al, 2000) and cNkx 2.5 (Schultheiss et al, 1995).…”

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confidence: 99%

Regulation of myosin expression during myotome formation

et al. 2003

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The first skeletal muscle fibers to form in vertebrate embryos appear in the somitic myotome. PCR analysis and in situ hybridization with isoform-specific probes reveal differences in the temporal appearance and spatial distribution of fast and slow myosin heavy chainmRNA transcripts within myotomal fibers. Embryonic fast myosin heavy chain was the first isoform expressed, followed rapidly by slow myosin heavy chains 1 and 3, with slow myosin heavy chain 2 appearing several hours later. Neonatal fast myosin heavy chain is not expressed in myotomal fibers. Although transcripts of embryonic fast myosin heavy chain were always distributed throughout the length of myotomal fibers, the mRNA for each slow myosin heavy chain isoform was initially restricted to the centrally located myotomal fiber nuclei. As development proceeded, slow myosin heavy chain transcripts spread throughout the length of myotomal fibers in order of their appearance. Explants of segments from embryos containing neural tube, notochord and somites 7-10, when incubated overnight, become innervated by motor neurons from the neural tube and express all four myosin heavy chain genes. Removal of the neural tube and/or notochord from explants prior to incubation or addition of d-tubocurare to intact explants prevented expression of slow myosin chain 2 but expression of genes encoding the other myosin heavy chain isoforms was unaffected. Thus, expression of slow myosin heavy chain 2 is dependent on functional innervation, whereas expression of embryonic fast and slow myosin heavy chain 1 and 3are innervation independent. Implantation of sonic-hedgehog-soaked beads in vivo increased the accumulation of both fast and slow myosin heavy chain transcripts, as well as overall myotome size and individual fiber size, but had no effect on myotomal fiber phenotype. Transcripts encoding embryonic fast myosin heavy chain first appear ventrolaterally in the myotome, whereas slow myosin heavy chain transcripts first appear in fibers positioned midway between the ventrolateral and dorsomedial lips of the myotome. Therefore, models of epaxial myotome formation must account for the positioning of the oldest fibers in the more ventral-lateral region of the myotome and the youngest fibers in the dorsomedial region.

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Evolutionary significance of myosin heavy chain heterogeneity in birds

Bandman

Rosser

2000

Microsc. Res. Tech.

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Molecular cloning of two fast myosin heavy chain cDNAs from chicken embryo skeletal muscle.

Cited by 46 publications

References 39 publications

Molecular cloning of mRNA sequences for cardiac alpha- and beta-form myosin heavy chains: expression in ventricles of normal, hypothyroid, and thyrotoxic rabbits.

Molecular cloning of mRNA sequences for cardiac alpha- and beta-form myosin heavy chains: expression in ventricles of normal, hypothyroid, and thyrotoxic rabbits.

Regulation of myosin expression during myotome formation

Evolutionary significance of myosin heavy chain heterogeneity in birds

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