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Titolo:
MULTIPLE REGULATORY ELEMENTS CONTRIBUTE DIFFERENTIALLY TO MUSCLE CREATINE-KINASE ENHANCER ACTIVITY IN SKELETAL AND CARDIAC-MUSCLE
Autore:
AMACHER SL; BUSKIN JN; HAUSCHKA SD;
Indirizzi:
UNIV WASHINGTON,DEPT BIOCHEM SJ70 SEATTLE WA 98195 UNIV WASHINGTON,DEPT BIOCHEM SJ70 SEATTLE WA 98195
Titolo Testata:
Molecular and cellular biology
fascicolo: 5, volume: 13, anno: 1993,
pagine: 2753 - 2764
SICI:
0270-7306(1993)13:5<2753:MRECDT>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALPHA-ACTIN GENE; TRANSCRIPTION FACTOR AP-2; SERUM RESPONSE ELEMENT; RAT MYOCARDIAL-CELLS; PROTEIN-BINDING SITE; LOOP-HELIX PROTEINS; MYOSIN HEAVY-CHAIN; C-FOS GENE; DNA-BINDING; UPSTREAM ELEMENTS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
99
Recensione:
Indirizzi per estratti:
Citazione:
S.L. Amacher et al., "MULTIPLE REGULATORY ELEMENTS CONTRIBUTE DIFFERENTIALLY TO MUSCLE CREATINE-KINASE ENHANCER ACTIVITY IN SKELETAL AND CARDIAC-MUSCLE", Molecular and cellular biology, 13(5), 1993, pp. 2753-2764

Abstract

We have used transient transfections in MM14 skeletal muscle cells, newborn rat primary ventricular myocardiocytes, and nonmuscle cells to characterize regulatory elements of the mouse muscle creatine kinase (MCK) gene. Deletion analysis of MCK 5'-flanking sequence reveals a striated muscle-specific, positive regulatory region between -1256 and -1020. A 206-bp fragment from this region acts as a skeletal muscle enhancer and confers orientation-dependent activity in myocardiocytes. A 110-bp enhancer subfragment confers high-level expression in skeletal myocytes but is inactive in myocardiocytes, indicating that skeletal and cardiac muscle MCK regulatory sites are distinguishable. To further delineate muscle regulatory sequences, we tested six sites within the MCK enhancer for their functional importance. Mutations at five sites decrease expression in skeletal muscle, cardiac muscle, and nonmuscle cells. Mutations at two of these sites, Left E box and MEF2, cause similar decreases in all three cell types. Mutations at three sites have larger effects in muscle than nonmuscle cells; an A/T-rich site mutation has a pronounced effect in both striated muscle types, mutations atthe MEF1 (Right E-box) site are relatively specific to expression in skeletal muscle, and mutations at the CArG site are relatively specific to expression in cardiac muscle. Changes at the AP2 site tend to increase expression in muscle cells but decrease it in nonmuscle cells. In contrast to reports involving cotransfection of 10T1/2 cells with plasmids expressing the myogenic determination factor MyoD, we show thatthe skeletal myocyte activity of multimerized MEF1 sites is 30-fold lower than that of the 206-bp enhancer. Thus, MyoD binding sites alone are not sufficient for high-level expression in skeletal myocytes containing endogenous levels of MyoD and other myogenic determination factors.

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Documento generato il 25/09/20 alle ore 00:04:08