Myogenic lineage determination and differentiation: Evidence for a regulatory gene pathway

Pinney, Deborah F.; Pearson‐White, Sonia; Konieczny, Stephen F.; Latham, Keith E.; Emerson, Charles P.

doi:10.1016/0092-8674(88)90095-5

Cited by 241 publications

(106 citation statements)

References 27 publications

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“…Mouse myoD cDNA (Ref. 31; GenBank TM accession number M84918) and mouse growth-associated-binding protein (GABP) ␣ and ␤ cDNAs (GenBank TM accession numbers NM008065 and NM016654) generated by RT-PCR from mouse C2C12 myotubes were subcloned into pcDNA3 for transfection. All cloned sequences were verified before the use.…”

Section: Methodsmentioning

confidence: 99%

Transcriptional Regulation of Acetylcholinesterase-associated Collagen ColQ

Lee

Choi

Ting

et al. 2004

Journal of Biological Chemistry

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The presence of a collagenous protein (ColQ) characterizes the collagen-tailed forms of acetylcholinesterase and butyrylcholinesterase at vertebrate neuromuscular junctions which is tethered in the synaptic basal lamina. ColQ subunits, differing mostly by their signal sequences, are encoded by transcripts ColQ-1 and ColQ-1a, which are differentially expressed in slow and fast twitch muscles in mammals. Two distinct promoters, pColQ-1 and pColQ-1a, were isolated from the upstream sequences of human COLQ gene; they showed musclespecific expression and were activated by myogenic transcriptional elements in cultured myotubes. After in vivo DNA transfection, pColQ-1 showed strong activity in slow twitch muscle (e.g. soleus), whereas pColQ-1a was preferably expressed in fast twitch muscle (e.g. tibialis). Mutation analysis of the ColQ promoters suggested that the muscle fiber type-specific expression pattern of ColQ transcripts were regulated by a slow upsteam regulatory element (SURE) and a fast intronic regulatory element (FIRE). These regulatory elements were responsive to a calcium ionophore and to calcineurin inhibition by cyclosporine A. The slow fiber type-specific expression of ColQ-1 was abolished by the mutation of an NFAT element in pColQ-1. Moreover, both the ColQ promoters contained N-box element that was responsible for the synapse-specific expression of ColQ transcripts. These results explain the specific expression patterns of collagen-tailed acetylcholinesterase in slow and fast muscle fibers.

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Section: Methodsmentioning

confidence: 99%

Transcriptional Regulation of Acetylcholinesterase-associated Collagen ColQ

Lee

Choi

Ting

et al. 2004

Journal of Biological Chemistry

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“…The results of Pinney et al (1988), Wright et al (1989), and Braun et al (1989) and the preliminary identification of the myogenic determination genes Mydl, myogenin, and Myf5 suggest that conversion involves the interplay of multiple genes. Because CMD1, Mydl, Myf5, and MyoD 1 can activate MyoD 1 in 10T1A cells, and MyoD 1 can activate CMD1 in chick cells, interdependent regulatory pathways involving different myogenic factors appear to be operative.…”

Section: Genes and Developmentmentioning

confidence: 99%

“…Following these observations Lassar and associates (Davis et al 1987) isolated a single cDNA clone, MyoD1, representing a gene product expressed uniquely in myogenic cells, that was capable of converting a variety of mesodermal fibroblasts into myoblasts when expressed in these cells. Human genomic DNA cloned into a cosmid vector could also induce myogenic conversion of 10T1A cells, and this gene did not appear to correspond to MyoD 1 by Southern analysis (Pinney et al 1988) yet could activate the endogenous MyoD1 gene. Different myogenic factors, myogenin and myfS, recently have been isolated from rat (Wright et al 1989} andhuman (Braun et al 1989), respectively, that are related functionally to but distinct from MyoD.…”

mentioning

confidence: 99%

An avian muscle factor related to MyoD1 activates muscle-specific promoters in nonmuscle cells of different germ-layer origin and in BrdU-treated myoblasts.

Lin¹,

Dechesne²,

Eldridge³

et al. 1989

Genes Dev.

161

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We isolated the cDNA encoding a myogenic [actor expressed in embryonic chick breast muscle by virtue of its weak hybridization to the mouse MyoD1 clone. Nucleotide sequence analysis and amino acid comparison define this clone, CMD1, as encoding a protein similar to mouse MyoD1. CMD1 encodes a polypeptide smaller than MyoD1, 298 versus 318 amino acids, respectively, and is 80% concordant by amino acid sequence overall. The basic and myc domains required for myogenic conversion of mouse 10TI/2 'fibroblasts' to myoblasts with MyoD1 are completely conserved in CMD1. CMD1 is just as efficient as the mouse homolog in myogenic conversion of 10TV2 cells and coactivates the endogenous mouse MyoD1 gene in the process. The efficiency of myoblast conversion depends on the levels of CMD 1 expression and suggests that the cellular concentration of CMD1 plays a role in the onset of myogenesis. Transient expression of CMD1 in a variety of nonmuscle cells from different germ-layer origins activates both cotransfected muscle-specific promoters and, in some cases, endogenous muscle-specific genes. 5-Bromodeoxyuridine (BrdU) treatment of chicken and mouse myoblasts reduces the expression of CMD1 and MyoD1, respectively, and may explain how this thymidine analog inhibits myogenesis and the activity of transfected muscle-specific promoters in BrdU-treated myoblasts. Transient expression of CMD 1 in BrdU-treated myoblasts reactivates cotransfected muscle-specific promoters. CMD1 activates muscle-specific promoters in cotransfections regardless of cell type, whereas 'housekeeping' or constitutive promoters can be activated moderately, unaffected, or repressed, depending on the promoter and cell background. The rate and degree of myogenic conversion may be more restricted by cell phenotype than by germ-layer origin.

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“…Related myogenic factors have also been identified in a variety of vertebrate and invertebrate species (22,30,35,39,44,47,57,65,72). An additional gene, myd, that appears to be structurally unrelated to the MyoD family, has been identified as a genomic clone that can induce myogenesis in 1OT1/2 cells, but it has not yet been characterized at the molecular level (59).…”

mentioning

confidence: 99%

Analysis of the myogenin promoter reveals an indirect pathway for positive autoregulation mediated by the muscle-specific enhancer factor MEF-2.

Edmondson¹,

Cheng²,

Cserjesi³

et al. 1992

Mol. Cell. Biol.

291

253

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Transcriptional cascades that specify cell fate have been well described in invertebrates. In mammalian development, however, gene hierarchies involved in determination of cell lineage are not understood. With the recent cloning of the MyoD family of myogenic regulatory factors, a model system has become available with which to study the dynamics of muscle determination in mammalian development. Myogenin, along with other members of the MyoD gene family, possesses the apparent ability to redirect nonmuscle cells into the myogenic lineage. This ability appears to be due to the direct activation of an array of subordinate or downstream genes which are responsible for formation and function of the muscle contractile apparatus. Myogenin-directed transcription has been shown to occur through interaction with a DNA consensus sequence known as an E box (CANNTG) present in the control regions of numerous downstream genes. In addition to activating the transcription of subordinate genes, members of the MyoD family positively regulate their own expression and cross-activate one another's expression. These autoregulatory interactions have been suggested as a mechanism for induction and maintenance of the myogenic phenotype, but the molecular details of the autoregulatory circuits are undefined. Here we show that the myogenin promoter contains a binding site for the myocytespecific enhancer-binding factor, MEF-2, which can function as an intermediary of myogenin autoactivation. Since MEF-2 can be induced by myogenin, these results suggest that myogenin and MEF-2 participate in a transcriptional cascade in which MEF-2, once induced by myogenin, acts to amplify and maintain the myogenic phenotype by acting as a positive regulator of myogenin expression.The formation of skeletal muscle during vertebrate development involves the induction of mesoderm from primary ectoderm and the subsequent generation of proliferating myoblasts that ultimately terminally differentiate in response to environmental cues. The recent discovery of a family of related muscle-specific factors that can convert fibroblasts to myoblasts has contributed to rapid progress toward understanding the molecular events that underlie the establishment of the skeletal muscle phenotype (for reviews, see references 55 and 69). Members of this muscle regulatory gene family include MyoD (21), myogenin (25, 77), myf5 (9), and MRF4/herculin/myf6 (8,48,61), each of which can activate myogenesis when introduced into a wide range of nonmuscle cell types.

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Myogenic lineage determination and differentiation: Evidence for a regulatory gene pathway

Cited by 241 publications

References 27 publications

Transcriptional Regulation of Acetylcholinesterase-associated Collagen ColQ

Transcriptional Regulation of Acetylcholinesterase-associated Collagen ColQ

An avian muscle factor related to MyoD1 activates muscle-specific promoters in nonmuscle cells of different germ-layer origin and in BrdU-treated myoblasts.

Analysis of the myogenin promoter reveals an indirect pathway for positive autoregulation mediated by the muscle-specific enhancer factor MEF-2.

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