Abstract
The β-cardiac myosin heavy chain is the major contractile protein expressed in two sarcomeric muscles of distinct embryologic origins, the ventricular myocardium and slow twitch skeletal muscle. Characterization of the cis-acting regulatory sequences of the human and the rat β-MHC genes established that their expression in these two muscle types is controlled, at least in part, by common mechanisms involving a muscle-specific enhancer. This enhancer consists of distinct but cooperative subelements that interact with muscle-specific nuclear proteins. In contrast to other muscle-specific enhancers, the β-MHC gene enhancer is unresponsive, directly or indirectly, to the muscle lineage-determining and muscle gene-transactivating helix-loop-helix factors MyoD and myogenin. A MyoD-binding site in the rat β-MHC promoter is not required for transcriptional activity in skeletal and cardiac cells, but is necessary for activation in 10T1/2 and CV1 cells transfected with MyoD. In addition, this element is absent from the human β-MHC promoter. Thus, MyoD and MyoD-related processes are neither required nor sufficient for the expression of the β-MHC gene either in cardiac or skeletal muscle cells. These observations provide evidence for the existence of myogenic regulatory programs that precede and/or differ from those governed by known myogenic helix-loophelix transactivators.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 22678-22688 |
| Number of pages | 11 |
| Journal | Journal of Biological Chemistry |
| Volume | 266 |
| Issue number | 33 |
| State | Published - 1991 |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- Biochemistry
Cite this
A myod1-independent muscle-specific enhancer controls the expression of the β-myosin heavy chain gene in skeletal and cardiac muscle cells. / Thompson, Reid; Nadal-Ginard, Bernardo; Mahdavi, Vijak.
In: Journal of Biological Chemistry, Vol. 266, No. 33, 1991, p. 22678-22688.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A myod1-independent muscle-specific enhancer controls the expression of the β-myosin heavy chain gene in skeletal and cardiac muscle cells
AU - Thompson, Reid
AU - Nadal-Ginard, Bernardo
AU - Mahdavi, Vijak
PY - 1991
Y1 - 1991
N2 - The β-cardiac myosin heavy chain is the major contractile protein expressed in two sarcomeric muscles of distinct embryologic origins, the ventricular myocardium and slow twitch skeletal muscle. Characterization of the cis-acting regulatory sequences of the human and the rat β-MHC genes established that their expression in these two muscle types is controlled, at least in part, by common mechanisms involving a muscle-specific enhancer. This enhancer consists of distinct but cooperative subelements that interact with muscle-specific nuclear proteins. In contrast to other muscle-specific enhancers, the β-MHC gene enhancer is unresponsive, directly or indirectly, to the muscle lineage-determining and muscle gene-transactivating helix-loop-helix factors MyoD and myogenin. A MyoD-binding site in the rat β-MHC promoter is not required for transcriptional activity in skeletal and cardiac cells, but is necessary for activation in 10T1/2 and CV1 cells transfected with MyoD. In addition, this element is absent from the human β-MHC promoter. Thus, MyoD and MyoD-related processes are neither required nor sufficient for the expression of the β-MHC gene either in cardiac or skeletal muscle cells. These observations provide evidence for the existence of myogenic regulatory programs that precede and/or differ from those governed by known myogenic helix-loophelix transactivators.
AB - The β-cardiac myosin heavy chain is the major contractile protein expressed in two sarcomeric muscles of distinct embryologic origins, the ventricular myocardium and slow twitch skeletal muscle. Characterization of the cis-acting regulatory sequences of the human and the rat β-MHC genes established that their expression in these two muscle types is controlled, at least in part, by common mechanisms involving a muscle-specific enhancer. This enhancer consists of distinct but cooperative subelements that interact with muscle-specific nuclear proteins. In contrast to other muscle-specific enhancers, the β-MHC gene enhancer is unresponsive, directly or indirectly, to the muscle lineage-determining and muscle gene-transactivating helix-loop-helix factors MyoD and myogenin. A MyoD-binding site in the rat β-MHC promoter is not required for transcriptional activity in skeletal and cardiac cells, but is necessary for activation in 10T1/2 and CV1 cells transfected with MyoD. In addition, this element is absent from the human β-MHC promoter. Thus, MyoD and MyoD-related processes are neither required nor sufficient for the expression of the β-MHC gene either in cardiac or skeletal muscle cells. These observations provide evidence for the existence of myogenic regulatory programs that precede and/or differ from those governed by known myogenic helix-loophelix transactivators.
UR - http://www.scopus.com/inward/record.url?scp=0025889701&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0025889701&partnerID=8YFLogxK
M3 - Article
C2 - 1939278
AN - SCOPUS:0025889701
VL - 266
SP - 22678
EP - 22688
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 33
ER -