A Composite CMV-IE Enhancer/β-Actin Promoter Is Ubiquitously Expressed in Mouse Cutaneous Epithelium

1998 ◽  
Vol 244 (1) ◽  
pp. 367-369 ◽  
Author(s):  
Janet A. Sawicki ◽  
Rebecca J. Morris ◽  
Bob Monks ◽  
Katsunaga Sakai ◽  
Jun-ichi Miyazaki
Keyword(s):  
Actin Promoter ◽  
Cutaneous Epithelium

scholarly journals The β actin promoter

1989 ◽  
Vol 264 (16) ◽  
pp. 9539-9546 ◽  
Author(s):  
W W Quitschke ◽  
Z Y Lin ◽  
L DePonti-Zilli ◽  
B M Paterson
Keyword(s):  
Actin Promoter

Cloning of actin Promoter and Transformation of the Marine-Sourced Filamentous Fungus Phoma herbarum YS4108

2008 ◽  
Vol 6 (4) ◽  
pp. 307-311
Author(s):  
Tian ZHOU ◽  
Ming-Qian FENG ◽  
Wen-Jie WEI ◽  
Ren-Xiang TAN ◽  
Yong-Chun SONG
Keyword(s):  
Filamentous Fungus ◽  
Phoma Herbarum ◽  
Actin Promoter

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.

Regulated expression of a transfected human cardiac actin gene during differentiation of multipotential murine embryonal carcinoma cells

1988 ◽  
Vol 8 (1) ◽  
pp. 406-417
Author(s):  
M A Rudnicki ◽  
M Ruben ◽  
M W McBurney
Keyword(s):  
Cardiac Muscle ◽  
Thymidine Kinase ◽  
Embryonal Carcinoma ◽  
Actin Gene ◽  
P19 Cells ◽  
Cardiac Muscle Cells ◽  
Cardiac Actin ◽  
Ec Cells ◽  
Actin Promoter ◽  
Actin Mrna

P19 embryonal carcinoma (EC) cells are multipotential stem cells which can be induced to differentiate in vitro into a variety of cell types, including cardiac muscle cells. A cloned human cardiac actin (CH-actin) gene was transfected into P19 cells, and stable transformants were isolated. Low levels of CH-actin mRNA were present in transformed EC cells, but a marked increase in the level of CH-actin mRNA was found as these cells differentiated into cardiac muscle. The accumulation of CH-actin mRNA paralleled that of the endogenous mouse cardiac actin mRNA. A chimeric gene, which consisted of the CH-actin promoter linked to the herpes simplex virus thymidine kinase coding region, was constructed and transfected into P19 cells. In these transformants, the thymidine kinase protein was located almost exclusively in cardiac muscle cells and was generally not detectable in EC or other nonmuscle cells. These results suggest that the transfected CH-actin promoter functions in the appropriate developmental and tissue-specific manner during the differentiation of multipotential EC cells in culture.

Memoirs: The Nerve Terminations in the Cutaneous Epithelium of the Tadpole

1885 ◽  
Vol s2-26 (101) ◽  
pp. 53-70
Author(s):  
A. B. MACALLUM
Keyword(s):  
Epithelial Cell ◽  
Nerve Network ◽  
Cutaneous Epithelium

The results of this work may be summarised in the following statements: 1. Certain fibres of the nerve network, situated below the corium, and known as the fundamental plexus, give origin to fibrils which enter the epithelium and terminate in comparatively large beadlike bodies between the cells. 2. From a network of fine anastomising nerve-fibrils situated immediately below the epithelium, and forming meshes, each narrower than the surface covered by an epithelial cell, arise other excessively fine fibrils, which end either within or between the cells, or, after branching, in both fashions. 3. One, commonly two, often three or more, nerve-fibrils terminate in the interior of each epithelial cell near its nucleus. 4. The figures of Eberth are sheaths for intracellular nerve terminations.

scholarly journals β1-Integrin and PI 3-kinase regulate RhoA-dependent activation of skeletal α-actin promoter in myoblasts

2000 ◽  
Vol 278 (6) ◽  
pp. H1736-H1743 ◽  
Author(s):  
Lei Wei ◽  
Wei Zhou ◽  
Lu Wang ◽  
Robert J. Schwartz
Keyword(s):  
Gene Expression ◽  
Promoter Activity ◽  
Serum Response Factor ◽  
Critical Role ◽  
Dominant Negative ◽  
Dominant Negative Mutant ◽  
Muscle Gene Expression ◽  
Actin Promoter ◽  
Muscle Gene ◽  
Negative Mutant

RhoA GTPase, a regulator of actin cytoskeleton, is also involved in regulating c- fos gene expression through its effect on serum response factor (SRF) transcriptional activity. We have also shown that RhoA plays a critical role in myogenesis and regulates expression of SRF-dependent muscle genes, including skeletal α-actin. In the present study, we examined whether the RhoA signaling pathway cross talks with other myogenic signaling pathways to modulate skeletal α-actin promoter activity in myoblasts. We found that extracellular matrix proteins and the β1-integrin stimulated RhoA-dependent activation of the α-actin promoter. The muscle-specific isoform β1Dselectively activated the α-actin promoter in concert with RhoA but inhibited the c- fos promoter. In addition, focal adhesion kinase (FAK) and phosphatidylinositol (PI) 3-kinase were required for full activation of the α-actin promoter by RhoA. Expression of a dominant negative mutant of FAK, application of wortmannin to cultured myoblasts, or expression of a dominant negative mutant of PI 3-kinase inhibited α-actin promoter activity induced by RhoA. These results suggest that RhoA, β1-integrin, FAK, and PI 3-kinase serve together as an important signaling network in regulating muscle gene expression.

scholarly journals DNA-binding site for two skeletal actin promoter factors is important for expression in muscle cells.

1988 ◽  
Vol 8 (4) ◽  
pp. 1800-1802 ◽  
Author(s):  
K Walsh ◽  
P Schimmel
Keyword(s):  
Skeletal Muscle ◽  
Binding Site ◽  
Muscle Cells ◽  
Factor Binding Site ◽  
Nuclear Factors ◽  
Dna Binding Site ◽  
Nonmuscle Cells ◽  
Actin Promoter ◽  
Promoter Mutations ◽  
Low Expression

Two nuclear factors bind to the same site in the chicken skeletal actin promoter. Mutations in the footprint sequence which eliminate detectable binding decrease expression in transfected skeletal muscle cells by a factor of 25 to 50 and do not elevate the low expression in nonmuscle cells. These results show that the factor-binding site contributes to the activation of expression in muscle cells and that it alone does not contribute significantly to repress expression in nonmuscle cells.

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