scholarly journals Serum response factor mRNA induction in the hypertrophying chicken patagialis muscle

1999 ◽  
Vol 86 (1) ◽  
pp. 377-382 ◽  
Author(s):  
James A. Carson ◽  
Frank W. Booth
Keyword(s):  
Serum Response Factor ◽  
Response Factor ◽  
Mobility Shift ◽  
Mrna Induction ◽  
Mrna Concentration ◽  
Nuclear Extracts ◽  
Actin Promoter ◽  
Gel Mobility Shift ◽  
Fast Twitch ◽  
Serum Response

Gene expression in the stretched chicken patagialis (Pat) muscle has not been extensively examined. This study’s purpose was to determine the Pat muscle’s expression pattern of serum response factor (SRF), skeletal α-actin, and MyoD mRNAs after 3 days (onset of stretch), 6 days (end of first week of rapid growth), and 14 days (slowed rate of stretch-induced growth) of stretch. SRF mRNA demonstrated two species (B1 and B2), with B2 being more prevalent in the predominantly fast-twitch Pat muscle, compared with the slow-tonic muscle. Stretch overload increased B1 and B2 SRF mRNA concentrations, and the increase in B1 SRF mRNA concentration was greater at day 6compared with days 3 or 14. MyoD mRNA concentration was greater in 3-day-stretched Pat muscles, compared with days 6 or 14 . Skeletal α-actin mRNA concentration was not changed during the study. Gel mobility shift assays demonstrated that SRF binding with serum response element 1 of the skeletal α-actin promoter had no altered binding patterns from 6-day-stretched Pat nuclear extracts. It appears that SRF and MyoD mRNAs are induced in the stretch-overloaded Pat muscle but at different time points.

SRF and TEF-1 control of chicken skeletal alpha-actin gene during slow-muscle hypertrophy

1996 ◽  
Vol 270 (6) ◽  
pp. C1624-C1633 ◽  
Author(s):  
J. A. Carson ◽  
R. J. Schwartz ◽  
F. W. Booth
Keyword(s):  
Serum Response Factor ◽  
Direct Injection ◽  
Regulatory Elements ◽  
Transcriptional Enhancer ◽  
Mobility Shift ◽  
Nuclear Extracts ◽  
Anterior Latissimus Dorsi ◽  
Actin Promoter ◽  
Alpha Actin ◽  
Serum Response

The purpose of this study was to delineate the alpha-actin regulatory elements and transcription factors that are responsible for conferring stretch-overload responsiveness during hypertrophy of the anterior latissimus dorsi (ALD) muscle of young chickens by weighting one wing. Minimal promoter constructs were evaluated by direct injection into the ALD, which demonstrated that both serum response element 1 (SRE1) and the transcriptional enhancer factor 1 (TEF-1) elements were sufficient for increased expression during stretch overload. A mutated SRE1 prevented expression in both basal and stretched ALD muscles, whereas a mutated TEF-1 element reduced actin promoter function in both control and stretched muscles. The serum response factor (SRF)-SRE1 binding complex demonstrated faster migration in mobility shift assays from day 3-and day 6-stretched ALD nuclear extracts relative to their control. TEF-1 binding was qualitatively increased in stretched extracts at day 3 but not day 6 of stretch overload. Skeletal alpha-actin mRNA accumulated from day 3 to day 6 of stretch overload. These data demonstrate that SRE1 is necessary and sufficient for stretch-overload responsiveness from the skeletal alpha-actin promoter and that the SRF-SRE1 binding complex migrates faster in stretched nuclear extracts of hypertrophied relative to control extracts from intact ALD muscles of chickens.

Functional antagonism between YY1 and the serum response factor

1992 ◽  
Vol 12 (9) ◽  
pp. 4209-4214
Author(s):  
A Gualberto ◽  
D LePage ◽  
G Pons ◽  
S L Mader ◽  
K Park ◽  
...  
Keyword(s):  
Serum Response Factor ◽  
Regulatory Element ◽  
Target Sequence ◽  
Response Factor ◽  
Basal Expression ◽  
Actin Promoter ◽  
Alpha Actin ◽  
Serum Response

The rapid, transient induction of the c-fos proto-oncogene by serum growth factors is mediated by the serum response element (SRE). The SRE shares homology with the muscle regulatory element (MRE) of the skeletal alpha-actin promoter. It is not known how these elements respond to proliferative and cell-type-specific signals, but the response appears to involve the binding of the serum response factor (SRF) and other proteins. Here, we report that YY1, a multifunctional transcription factor, binds to SRE and MRE sequences in vitro. The methylation interference footprint of YY1 overlaps with that of the SRF, and YY1 competes with the SRF for binding to these DNA elements. Overexpression of YY1 repressed serum-inducible and basal expression from the c-fos promoter and repressed basal expression from the skeletal alpha-actin promoter. YY1 also repressed expression from the individual SRE and MRE sequences upstream from a TATA element. Unlike that of YY1, SRF overexpression alone did not influence the transcriptional activity of the target sequence, but SRF overexpression could reverse YY1-mediated trans repression. These data suggest that YY1 and the SRF have antagonistic functions in vivo.

scholarly journals Recruitment of the tinman homolog Nkx-2.5 by serum response factor activates cardiac alpha-actin gene transcription.

1996 ◽  
Vol 16 (11) ◽  
pp. 6372-6384 ◽  
Author(s):  
C Y Chen ◽  
R J Schwartz
Keyword(s):  
Dna Binding ◽  
Serum Response Factor ◽  
Binding Activity ◽  
Dominant Negative ◽  
Actin Gene ◽  
Response Factor ◽  
Dna Binding Activity ◽  
Actin Promoter ◽  
Alpha Actin ◽  
Serum Response

We recently showed that the cardiogenic homeodomain factor Nkx-2.5 served as a positive acting accessory factor for serum response factor (SRF) and that together they provided strong transcriptional activation of the cardiac alpha-actin promoter, depending upon intact serum response elements (SREs) (C. Y. Chen, J. Croissant, M. Majesky, S. Topouz, T. McQuinn, M. J. Frankovsky, and R. J. Schwartz, Dev. Genet. 19:119-130, 1996). As shown here, Nkx-2.5 and SRF collaborated to activate the endogenous murine cardiac alpha-actin gene in 10T1/2 fibroblasts by a mechanism in which SRF recruited Nkx-2.5 to the alpha-actin promoter. Activation of a truncated promoter consisting of the proximal alpha-actin SRE1 occurred even when Nkx-2.5 DNA-binding activity was blocked by a point mutation in the third helix of its homeodomain. Investigation of protein-protein interactions showed that Nkx-2.5 was bound to SRF in the absence of DNA in soluble protein complexes retrieved from cardiac myocyte nuclei but could also be detected in coassociated binding complexes on the proximal SRE1. Recruitment of Nkx-2.5 to an SRE depended upon SRF DNA-binding activity and was blocked by the dominant negative SRFpm1 mutant, which allowed for dimerization of SRF monomers but prevented DNA binding. Interactive regions shared by Nkx-2.5 and SRF were mapped to N-terminal/helix I and helix II/helix III regions of the Nkx-2.5 homeodomain and to the N-terminal extension of the MADS box. Our study suggests that physical association between Nkx-2.5 and SRF is one way that cardiac specified genes are activated in cardiac cell lineages.

scholarly journals The sarcomeric actin CArG-binding factor is indistinguishable from the c-fos serum response factor.

1989 ◽  
Vol 9 (2) ◽  
pp. 515-522 ◽  
Author(s):  
L M Boxer ◽  
R Prywes ◽  
R G Roeder ◽  
L Kedes
Keyword(s):  
Transcriptional Control ◽  
Serum Response Factor ◽  
Specific Binding ◽  
Immune Serum ◽  
Response Factor ◽  
Mobility Shift ◽  
Binding Factor ◽  
Carg Box ◽  
Zinc Addition ◽  
Serum Response

The c-fos serum response element (SRE) and a sarcomeric actin promoter element (CArG box) are similar in sequence and are recognized, respectively, by the serum response factor (SRF) and the CArG-binding factor (CBF). Although the transcriptional controls for the c-fos and sarcomeric actin genes are rather different, SRF and CBF have been found to be indistinguishable by all criteria tested. They exhibited similar chromatographic properties, sedimentation rates, and temperature stabilities. In mobility shift assays, the SRE competed more strongly than the actin CArG box for formation of either the SRF-SRE or the CBF-CArG complex. The symmetric inverted repeat of the left side of the Xenopus cytoskeletal actin SRE also competed, even more strongly, for each complex. The site-specific binding of each protein was inhibited both by orthophenanthroline, whose effects were reversed by zinc addition, and by treatment with potato acid phosphatase. Furthermore, immune serum raised against the c-fos SRF also recognized the actin CBF. We discuss how transcriptional control of these diverse genes might be obtained with a single similar factor.

scholarly journals Functional antagonism between YY1 and the serum response factor.

1992 ◽  
Vol 12 (9) ◽  
pp. 4209-4214 ◽  
Author(s):  
A Gualberto ◽  
D LePage ◽  
G Pons ◽  
S L Mader ◽  
K Park ◽  
...  
Keyword(s):  
Serum Response Factor ◽  
Regulatory Element ◽  
Target Sequence ◽  
Response Factor ◽  
Basal Expression ◽  
Actin Promoter ◽  
Alpha Actin ◽  
Serum Response

The rapid, transient induction of the c-fos proto-oncogene by serum growth factors is mediated by the serum response element (SRE). The SRE shares homology with the muscle regulatory element (MRE) of the skeletal alpha-actin promoter. It is not known how these elements respond to proliferative and cell-type-specific signals, but the response appears to involve the binding of the serum response factor (SRF) and other proteins. Here, we report that YY1, a multifunctional transcription factor, binds to SRE and MRE sequences in vitro. The methylation interference footprint of YY1 overlaps with that of the SRF, and YY1 competes with the SRF for binding to these DNA elements. Overexpression of YY1 repressed serum-inducible and basal expression from the c-fos promoter and repressed basal expression from the skeletal alpha-actin promoter. YY1 also repressed expression from the individual SRE and MRE sequences upstream from a TATA element. Unlike that of YY1, SRF overexpression alone did not influence the transcriptional activity of the target sequence, but SRF overexpression could reverse YY1-mediated trans repression. These data suggest that YY1 and the SRF have antagonistic functions in vivo.

The sarcomeric actin CArG-binding factor is indistinguishable from the c-fos serum response factor

1989 ◽  
Vol 9 (2) ◽  
pp. 515-522
Author(s):  
L M Boxer ◽  
R Prywes ◽  
R G Roeder ◽  
L Kedes
Keyword(s):  
Transcriptional Control ◽  
Serum Response Factor ◽  
Specific Binding ◽  
Immune Serum ◽  
Response Factor ◽  
Mobility Shift ◽  
Binding Factor ◽  
Carg Box ◽  
Zinc Addition ◽  
Serum Response

The c-fos serum response element (SRE) and a sarcomeric actin promoter element (CArG box) are similar in sequence and are recognized, respectively, by the serum response factor (SRF) and the CArG-binding factor (CBF). Although the transcriptional controls for the c-fos and sarcomeric actin genes are rather different, SRF and CBF have been found to be indistinguishable by all criteria tested. They exhibited similar chromatographic properties, sedimentation rates, and temperature stabilities. In mobility shift assays, the SRE competed more strongly than the actin CArG box for formation of either the SRF-SRE or the CBF-CArG complex. The symmetric inverted repeat of the left side of the Xenopus cytoskeletal actin SRE also competed, even more strongly, for each complex. The site-specific binding of each protein was inhibited both by orthophenanthroline, whose effects were reversed by zinc addition, and by treatment with potato acid phosphatase. Furthermore, immune serum raised against the c-fos SRF also recognized the actin CBF. We discuss how transcriptional control of these diverse genes might be obtained with a single similar factor.

Smooth muscle γ-actin promoter regulation by RhoA and serum response factor signaling

2003 ◽  
Vol 1628 (2) ◽  
pp. 133-139 ◽  
Author(s):  
James A Carson ◽  
Donald E Culberson ◽  
Raymond W Thompson ◽  
Rebecca A Fillmore ◽  
Warren Zimmer
Keyword(s):  
Smooth Muscle ◽  
Serum Response Factor ◽  
Response Factor ◽  
Promoter Regulation ◽  
Actin Promoter ◽  
Serum Response

The proximal serum response element in the Egr-1 promoter mediates response to thrombin in primary human endothelial cells

Blood ◽  
2002 ◽  
Vol 100 (13) ◽  
pp. 4454-4461 ◽  
Author(s):  
Sheng-Qian Wu ◽  
Takashi Minami ◽  
Diana J. Donovan ◽  
William C. Aird
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase ◽  
Serum Response Factor ◽  
Core Promoter ◽  
Mitogen Activated Protein Kinase ◽  
Human Endothelial Cells ◽  
Mobility Shift ◽  
Nuclear Extracts ◽  
Mitogen Activated Protein ◽  
Serum Response

Thrombin signaling in endothelial cells provides an important link between coagulation and inflammation. We report here that thrombin induces endogenous Egr-1 mRNA and Egr-1 promoter activity in primary human endothelial cells by approximately 6-fold and 3-fold, respectively. In transient transfection assays, deletion of the 3′ cluster of serum response elements (SREs), but not the 5′ cluster of SREs, resulted in a loss of thrombin response. When coupled to a heterologous core promoter, a region spanning the 3′ SRE cluster contained information for thrombin response, whereas a region spanning the 5′ SRE cluster had no such effect. A point mutation of the most proximal SRE (SRE-1), but not of the proximal Ets motif or upstream SREs, abrogated the response to thrombin. In electrophoretic mobility shift assays, nuclear extracts from thrombin-treated cells displayed increased binding of total and phosphorylated serum response factor (SRF) to SRE-1. Thrombin-mediated induction of Egr-1 was blocked by inhibitors of MEK1/2, but not by inhibitors of protein kinase C, phosphatidylinositol 3-kinase, or p38 mitogen-activated protein kinase (MAPK). Taken together, these data suggest that thrombin induces Egr-1 expression in endothelial cells by a MAPK-dependent mechanism that involves an interaction between SRF and SRE-1.

Sign in / Sign up

Export Citation Format

Share Document