Regulation of muscle gene expression

Caravatti, M; Minty, Adrian; Robert, Benoît; Montarras, Didier; Weydert, A.; Cohen, Arlette; Daubas, Philippe; Buckingham, Margaret

doi:10.1016/0022-2836(82)90131-0

Cited by 108 publications

(16 citation statements)

References 39 publications

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“…An increase in ,8 enolase transcript level accompanied terminal differentiation and paralleled the expression of other markers of myogenesis in culture (19,33) such as a actin examined here. The increase in the ratio of 3 to a enolase mRNA levels indicates that the developmental transition to the adult pattern of enolase isozymes coincides with myotube formation.…”

Section: Discussionmentioning

confidence: 89%

Murine muscle-specific enolase: cDNA cloning, sequence, and developmental expression.

Lamandé

Mazo²,

Lucas³

et al. 1989

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

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In vertebrates, the glycolytic enzyme enolase (EC 4.2.1.11) is present as homodimers and heterodimers formed from three distinct subunits of identical molecular weight, a, 13, and y. We report the cloning and sequencing of a cDNA encoding the ,B subunit of murine muscle-specific enolase. The corresponding amino acid sequence shows >80% homology with the ,B subunit from chicken obtained by protein sequencing and with a and y subunits from rat and mouse deduced from cloned cDNAs. In contrast, there is no homology between the 3' untranslated regions of mouse a, /3, and y enolase mRNAs, which also differ greatly in length.

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Section: Discussionmentioning

confidence: 89%

Murine muscle-specific enolase: cDNA cloning, sequence, and developmental expression.

Lamandé

Mazo²,

Lucas³

et al. 1989

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

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“…RNA samples were prepared, denatured with glyoxal, separated on an agarose gel and blotted onto a diazotised Biodyne A membrane (Pall, US) as described in Caravatti et al (1982). Hybridisations were as above but final washings were in 0.1 x SSC and 0.1 % SDS at 60°C.…”

Section: Restriction Mappingmentioning

confidence: 99%

A 5′ duplication of the alpha-cardiac actin gene in BALB/c mice is associated with abnormal levels of alpha-cardiac and alpha-skeletal actin mRNAs in adult cardiac tissue.

Garner¹,

Minty²,

Alonso³

et al. 1986

The EMBO Journal

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We describe the structure and transcriptional activity of the 5′ portion of the alpha‐cardiac actin gene of BALB/c mice. Southern blotting and DNA sequencing reveal that the promoter and first three exons of the gene are present as perfect repeats in a direct duplication of 9.5 kbp situated immediately upstream of the gene. Both promoters are active in adult cardiac tissue. Transcripts from the partial gene duplication give rise to novel RNAs that are spliced correctly in the actin region and polyadenylated. The level of mature alpha‐cardiac actin mRNA is only 16.5% that found in mice that do not possess the duplication. This is due, at least in part, to interference at the transcriptional level. Transcripts from the alpha‐skeletal actin gene accumulate to abnormally high levels in the hearts of such mutant mice. This result suggests tight regulatory coupling for this actin gene pair.

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“…DNA (5 ,4g) from each mouse was digested with the appropriate restriction enzyme and analyzed by Southern blotting (20). RNA was extracted, electrophoresed, and transferred to filters as described (12,21). After hybridization with 32P-labeled probes, filters were Abbreviations: MHC, myosin heavy chain; MLC, myosin light chain; RFLP, restriction fragment length polymorphism; bp, base pair(s); kb, kilobase(s).…”

mentioning

confidence: 99%

“…DNA (5 ,4g) from each mouse was digested with the appropriate restriction enzyme and analyzed by Southern blotting (20). RNA was extracted, electrophoresed, and transferred to filters as described (12,21). After hybridization with 32P-labeled probes, filters were and lanes f and h (1.5 ,ug)], from adult heart ventricle [lanes e and g (1.5 ,ug)], and from 18-day fetal skeletal muscle [lanes k and n (2 ,ug)], electrophoresed in agarose gels, and transferred to nitrocellulose as described (12,21).…”

mentioning

confidence: 99%

“…RNA was extracted, electrophoresed, and transferred to filters as described (12,21). After hybridization with 32P-labeled probes, filters were and lanes f and h (1.5 ,ug)], from adult heart ventricle [lanes e and g (1.5 ,ug)], and from 18-day fetal skeletal muscle [lanes k and n (2 ,ug)], electrophoresed in agarose gels, and transferred to nitrocellulose as described (12,21). The RNA blots were hybridized with the following nick-translated probes: the 320-bp Pst I-Pst I fragment of pMHC2.2 (embryonic skeletal MHC-specific; lanes a and b), the total insert of pMHC32 (adult skeletal; lanes c, d, g, h, i, j, and k), the 250-and 400-bp Pst I-Pst I fragments ofpMHC101 [a(V1) cardiac; lanes e and fl, and the 250-bp Pst I-Pst I fragment of pMHC16.2A (perinatal; lanes 1, m, and n).…”

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confidence: 99%

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Genes for skeletal muscle myosin heavy chains are clustered and are not located on the same mouse chromosome as a cardiac myosin heavy chain gene.

Weydert¹,

P²,

Lazaridis³

et al. 1985

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

112

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Myosin heavy chain (MHC) genes are expressed as several distinct isoforms in a tissue-and stagespecific manner; three skeletal muscle MHC isoforms appear sequentially during development. We have isolated cDNA clones, identified by RNA blot hybridization and by nucleotide sequence determination as coding for portions of the embryonic (pMHC2.2), perinatal (pMHC16.2A), and a(V1) cardiac (pMHC141 and pMHC101) MHC isoforms. These four probes and the adult skeletal MHC probe (pMHC32) have been used on Southern blots of genomic DNA to detect restriction fragment length polymorphisms defining the alleles for these genes in mouse species Mus musculus and Mus spretus. In this way, we followed the segregation of skeletal and cardiac MHC genes in 42 offspring resulting from an interspecies backcross. We found that (i) the embryonic, perinatal, and adult skeletal MHC genes are clustered on chromosome 11 near the locus nude, (it) the skeletal and cardiac MHC genes do not cosegregate, and (iii) the a(V1) cardiac MHC gene is located on chromosome 14 close to Np-i. This result is in contrast to that for other contractile protein genes such as the alkali myosin light chain and the actin multigene families, which are dispersed in the genome.The myosin heavy chain (MHC) family in mammals consists of at least 11 isoforms: 1 superfast skeletal, 2 adult fast skeletal, 1 perinatal skeletal, 1 embryonic/fetal skeletal, 2 cardiac [a(V1) and f(V3)], 1 adult slow skeletal, 1 smooth muscle, and 2 nonmuscle (1). Analysis of mRNA and genomic DNA sequences has provided evidence for the presence of different MHC genes (2, 3-7). During skeletal muscle development there is a sequential transition of different skeletal MHC isoforms from embryonic/fetal MHC to perinatal MHC and finally to adult MHC, as demonstrated in the rat (8). This phenomenon has also been shown at the mRNA level in the rat (9) and in the mouse, where a fetal MHC mRNA is replaced by an adult MHC mRNA at birth (2). A similar situation prevails for the two cardiac myosin isoforms, V1 (aa homodimer) and V3 (P3P homodimer): V3 is predominant over V1 in fetal heart ventricles and is replaced by V1 after birth in the mouse (10). In contrast to the sequential expression of MHC genes during striated muscle development, myosin alkali light chain (alkali MLC) genes and actin genes exhibit coexpression of the adult protein with the corresponding fetal isoform (refs. 11 and 12 and unpublished data). In these cases, the fetal isoform is also expressed in adult cardiac tissue. Based on a chromosomal analysis of hybrid cell lines, it has been reported that the genes coding for skeletal a-actin, cardiac a-actin, cytoplasmic f-actin, and the skeletal isoform of MLC2 are located on different mouse chromosomes (13, 14), whereas all the MHC genes are on chromosome 11 (13,15). Using backcrosses of an interspecies Mus 1 (DBA/2) x Mus 3 (M. spretus) cross and following the Mendelian segregation of muscle-specific genes by restriction fragment length polymorphism (RFLP), Robert et al. (16) d...

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Regulation of muscle gene expression

Cited by 108 publications

References 39 publications

Murine muscle-specific enolase: cDNA cloning, sequence, and developmental expression.

Murine muscle-specific enolase: cDNA cloning, sequence, and developmental expression.

A 5′ duplication of the alpha-cardiac actin gene in BALB/c mice is associated with abnormal levels of alpha-cardiac and alpha-skeletal actin mRNAs in adult cardiac tissue.

Genes for skeletal muscle myosin heavy chains are clustered and are not located on the same mouse chromosome as a cardiac myosin heavy chain gene.

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