Transfection of a DNA locus that mediates the conversion of 10T12 fibroblasts to myoblasts

Lassar, Andrew B.; Paterson, Bruce M.; Weintraub, Harold

doi:10.1016/0092-8674(86)90507-6

Cited by 361 publications

(202 citation statements)

References 22 publications

Supporting

Mentioning

193

Contrasting

Order By: Relevance

“…This was unexpected at first sight, since old seminal studies showed that 5-AZA treatment causes the myogenic conversion of C3H10T1/2 fibroblasts, 42,43 as a consequence of endogenous MyoD de-repression. 44,45 The apparent discrepancy of our result with previous studies could be easily explained if considering that we analyzed MyoD levels at earlier times after 5-AZA treatment, compared to those employed for detecting muscle-converted cell clones. Moreover, our cells overexpress exogenous MyoD, which constant levels probably mask minor variations caused by 5-AZA at the endogenous gene.…”

Section: -Aza Treatment Restores the Functional Interaction Of Myod contrasting

confidence: 53%

A cross-talk between DNA methylation and H3 lysine 9 dimethylation at the KvDMR1 region controls the induction of Cdkn1c in muscle cells

et al. 2016

View full text Add to dashboard Cite

The cdk inhibitor p57 kip2 , encoded by the Cdkn1c gene, plays a critical role in mammalian development and in the differentiation of several tissues. Cdkn1c protein levels are carefully regulated via imprinting and other epigenetic mechanisms affecting both the promoter and distant regulatory elements, which restrict its expression to particular developmental phases or specific cell types. Inappropriate activation of these regulatory mechanisms leads to Cdkn1c silencing, causing growth disorders and cancer. We have previously reported that, in skeletal muscle cells, induction of Cdkn1c expression requires the binding of the bHLH myogenic factor MyoD to a long-distance regulatory element within the imprinting control region KvDMR1. Interestingly, MyoD binding to KvDMR1 is prevented in myogenic cell types refractory to the induction of Cdkn1c. In the present work, we took advantage of this model system to investigate the epigenetic determinants of the differential interaction of MyoD with KvDMR1. We show that treatment with the DNA demethylating agent 5-azacytidine restores the binding of MyoD to KvDMR1 in cells unresponsive to Cdkn1c induction. This, in turn, promotes the release of a repressive chromatin loop between KvDMR1 and Cdkn1c promoter and, thus, the upregulation of the gene. Analysis of the chromatin status of Cdkn1c promoter and KvDMR1 in unresponsive compared to responsive cell types showed that their differential responsiveness to the MyoD-dependent induction of the gene does not involve just their methylation status but, rather, the differential H3 lysine 9 dimethylation at KvDMR1. Finally, we report that the same histone modification also marks the KvDMR1 region of human cancer cells in which Cdkn1c is silenced. On the basis of these results, we suggest that the epigenetic status of KvDMR1 represents a critical determinant of the cell type-restricted expression of Cdkn1c and, possibly, of its aberrant silencing in some pathological conditions.

show abstract

Section: -Aza Treatment Restores the Functional Interaction Of Myod contrasting

confidence: 53%

A cross-talk between DNA methylation and H3 lysine 9 dimethylation at the KvDMR1 region controls the induction of Cdkn1c in muscle cells

et al. 2016

View full text Add to dashboard Cite

show abstract

“…Unlike other mesenchymal lineages (such as adipocytes or osteoblasts), skeletal myoblasts have not been easily differentiated from MSCs. Initial induction protocols to differentiate MSCs into myogenic progenitors have employed 5-azacytidine [11], a strong demethylating agent associated with muscle gene activation, in particular MyoD [12][13][14]. The drawback of this non-physiological method is excessive cell death, which results in virtually none [15] or very few surviving cells that are then endowed with myogenic features (not shown).…”

Section: E X P E R I M E N T a L C E L L R E S E A R Cmentioning

confidence: 99%

Pax3 activation promotes the differentiation of mesenchymal stem cells toward the myogenic lineage

Gang

Bosnakovski

Simsek

et al. 2008

Experimental Cell Research

View full text Add to dashboard Cite

“…Kuo et al {1991) have demonstrated that the two chains are subject to different regulatory influences during F9 differentiation, a result that is consistent with our finding that the two chains are expressed at widely varying levels in different tissues. Although several transcription factors have been described that are selectively expressed in the liver, including C/EBP {Johnson et al 1987;Landschulz et al 1988a), DBP (Mueller et al 1990), LAP (Descombes et al 1990), HNF-3 (Lai et al 1990), andHNF-4 (Sladek et al 1991), none are entirely liver specific and none have the potential, such as MyoD or myogenin (Lassar et al 1986), to convert another cell type into a hepatocyte. Furthermore, most of these factors are expressed at the time of birth, too late in development to play a primary role in organogenesis.…”

Section: Developmental Implications Of Hnf-1 Heterodim Eriza Tionmentioning

confidence: 99%

HNF-1 alpha and HNF-1 beta (vHNF-1) share dimerization and homeo domains, but not activation domains, and form heterodimers in vitro.

Mendel¹,

Hansen²,

Graves³

et al. 1991

Genes Dev.

295

218

View full text Add to dashboard Cite

show abstract

Transfection of a DNA locus that mediates the conversion of 10T12 fibroblasts to myoblasts

Cited by 361 publications

References 22 publications

A cross-talk between DNA methylation and H3 lysine 9 dimethylation at the KvDMR1 region controls the induction of Cdkn1c in muscle cells

A cross-talk between DNA methylation and H3 lysine 9 dimethylation at the KvDMR1 region controls the induction of Cdkn1c in muscle cells

Pax3 activation promotes the differentiation of mesenchymal stem cells toward the myogenic lineage

HNF-1 alpha and HNF-1 beta (vHNF-1) share dimerization and homeo domains, but not activation domains, and form heterodimers in vitro.

Contact Info

Product

Resources

About