scholarly journals Evidence for a cell-specific negative regulatory element in the first intron of the gene for bovine elastin

1994 ◽  
Vol 300 (1) ◽  
pp. 147-152 ◽  
Author(s):  
A Manohar ◽  
R A Anwar
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Regulatory Element ◽  
Muscle Cells ◽  
Mobility Shift ◽  
Negative Regulatory Element ◽  
First Intron ◽  
A Cell ◽  
Translational Start ◽  
Nih 3T3

A cell-specific negative regulatory element has been identified in the first intron of the gene for elastin in a region between 442 and 464 bp from the translational start site. This regulatory element functions both when it is located 5′ of the promoter and 3′ of the chloramphenicol acetyltransferase (CAT) gene. The inhibition is observed both with the homologous elastin promoter and the heterologous SV1 promoter in transient expression experiments using rat aortic smooth-muscle cells. No inhibition was observed with NIH 3T3, Hep G2 and little, if any, with HeLa cells. Cell specificity was further confirmed by DNA mobility shift assays and the position of the negative regulatory element was localized with the use of synthetic duplex oligomers. It is proposed that this negative element plays a significant role in the modulation of the expression of the gene for elastin in the smooth-muscle cells of the aorta during development.

scholarly journals Gene Expression Profiling of Leiomyoma and Myometrial Smooth Muscle Cells in Response to Transforming Growth Factor-β

Endocrinology ◽  
2005 ◽  
Vol 146 (3) ◽  
pp. 1097-1118 ◽  
Author(s):  
Xiaoping Luo ◽  
Li Ding ◽  
Jingxia Xu ◽  
Nasser Chegini
Keyword(s):  
Gene Expression ◽  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Gene Expression Profile ◽  
Expression Profile ◽  
Binding Protein ◽  
Muscle Cells ◽  
Time Dependent ◽  
Early Gene ◽  
A Cell

Altered expression of the TGF-β system is recognized to play a central role in various fibrotic disorders, including leiomyoma. In this study we performed microarray analysis to characterize the gene expression profile of leiomyoma and matched myometrial smooth muscle cells (LSMC and MSMC, respectively) in response to the time-dependent action of TGF-β and, after pretreatment with TGF-β type II receptor (TGF-βRII) antisense oligomer-blocking/reducing TGF-β autocrine/paracrine actions. Unsupervised and supervised assessments of the gene expression values with a false discovery rate selected at P ≤ 0.001 identified 310 genes as differentially expressed and regulated in LSMC and MSMC in a cell- and time-dependent manner by TGF-β. Pretreatment with TGF-βRII antisense resulted in changes in the expression of many of the 310 genes regulated by TGF-β, with 54 genes displaying a response to TGF-β treatment. Comparative analysis of the gene expression profile in TGF-βRII antisense- and GnRH analog-treated cells indicated that these treatments target the expression of 222 genes in a cell-specific manner. Gene ontology assigned these genes functions as cell cycle regulators, transcription factors, signal transducers, tissue turnover, and apoptosis. We validated the expression and TGF-β time-dependent regulation of IL-11, TGF-β-induced factor, TGF-β-inducible early gene response, early growth response 3, CITED2 (cAMP response element binding protein-binding protein/p300-interacting transactivator with ED-rich tail), Nur77, Runx1, Runx2, p27, p57, growth arrest-specific 1, and G protein-coupled receptor kinase 5 in LSMC and MSMC using real-time PCR. Together, the results provide the first comprehensive assessment of the LSMC and MSMC molecular environment targeted by autocrine/paracrine action of TGF-β, highlighting potential involvement of specific genes whose products may influence the outcome of leiomyoma growth and fibrotic characteristics by regulating inflammatory response, cell growth, apoptosis, and tissue remodeling.

Mediating the invasion of smooth muscle cells into a cell-responsive hydrogel under the existence of immune cells

Biomaterials ◽  
2018 ◽  
Vol 180 ◽  
pp. 193-205 ◽  
Author(s):  
Shan Yu ◽  
Yiyuan Duan ◽  
Xingang Zuo ◽  
Xinyi Chen ◽  
Zhengwei Mao ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Immune Cells ◽  
Muscle Cells ◽  
A Cell

Effects of mitogen-activated protein kinases on nuclear protein importThis paper is one of a selection of papers published in this Special Issue, entitled The Nucleus: A Cell Within A Cell.

2006 ◽  
Vol 84 (3-4) ◽  
pp. 469-475 ◽  
Author(s):  
Randolph S. Faustino ◽  
Delphine C. Rousseau ◽  
Melanie N. Landry ◽  
Annette L. Kostenuk ◽  
Grant N. Pierce
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Map Kinase ◽  
Protein Import ◽  
Nuclear Protein ◽  
Muscle Cells ◽  
Inhibitory Effects ◽  
Permeabilized Cell ◽  
A Cell ◽  
Nuclear Protein Import

ERK-2 MAP kinase activation induces inhibitory effects on nuclear protein import in vascular smooth muscle cells. The mechanism and characteristics of this effect of ERK-2 were investigated. An unusual dose-dependent effect of ERK-2 on nuclear protein import was identified. At higher concentrations (1 μg/mL) of ERK-2, nuclear protein import was stimulated, whereas lower concentrations (0.04 μg/mL) inhibited import. Intermediate concentrations exerted intermediate effects. The stimulatory and inhibitory effects at the 2 different ERK-2 concentrations were observed in both conventional, permeabilized cell assays of nuclear protein import and with in situ microinjection of smooth muscle cells. The biphasic effects of ERK-2 on import were also found for the other 2 members of the MAPK family, p38 and JNK. RanGAP was identified by structural analysis as a candidate target protein responsible for mediating the effects of ERK-2. After pretreatment with high concentrations of ERK-2, RanGAP activity was significantly increased by ~50%. In contrast, low concentrations of ERK-2 significantly attenuated RanGAP activity. These results demonstrate that all 3 members of the MAPK family can alter nuclear protein import in opposite directions depending upon the concentration of ERK-2 used. RanGAP represents the MAP kinase target whereby nuclear transport can be stimulated or inhibited.

scholarly journals Transcriptional Regulation of S Phase Kinase-associated Protein 2 by NR4A Orphan Nuclear Receptor NOR1 in Vascular Smooth Muscle Cells

2011 ◽  
Vol 286 (41) ◽  
pp. 35485-35493 ◽  
Author(s):  
Florence Gizard ◽  
Yue Zhao ◽  
Hannes M. Findeisen ◽  
Hua Qing ◽  
Dianne Cohn ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
Muscle Cells ◽  
Nuclear Hormone Receptor ◽  
Orphan Nuclear Receptor ◽  
Mobility Shift ◽  
Vsmc Proliferation

Members of the NR4A subgroup of the nuclear hormone receptor superfamily have emerged as key transcriptional regulators of proliferation and inflammation. NOR1 constitutes a ligand-independent transcription factor of this subgroup and induces cell proliferation; however, the transcriptional mechanisms underlying this mitogenic role remain to be defined. Here, we demonstrate that the F-box protein SKP2 (S phase kinase-associated protein 2), the substrate-specific receptor of the ubiquitin ligase responsible for the degradation of p27KIP1 through the proteasome pathway, constitutes a direct transcriptional target for NOR1. Mitogen-induced Skp2 expression is silenced in vascular smooth muscle cells (VSMC) isolated from Nor1-deficient mice or transfected with Nor1 siRNA. Conversely, adenovirus-mediated overexpression of NOR1 induces Skp2 expression in VSMC and decreases protein abundance of its target p27. Transient transfection experiments establish that NOR1 transactivates the Skp2 promoter through a nerve growth factor-induced clone B response element (NBRE). Electrophoretic mobility shift and chromatin immunoprecipitation assays further revealed that NOR1 is recruited to this NBRE site in the Skp2 promoter in response to mitogenic stimulation. In vivo Skp2 expression is increased during the proliferative response underlying neointima formation, and this transcriptional induction depends on the expression of NOR1. Finally, we demonstrate that overexpression of Skp2 rescues the proliferative arrest of Nor1-deficient VSMC. Collectively, these results characterize Skp2 as a novel NOR1-regulated target gene and detail a previously unrecognized transcriptional cascade regulating mitogen-induced VSMC proliferation.

Selective killing of smooth muscle cells in culture by the ricin A-chain conjugated with monoclonal antibodies to a cell surface antigen via a dextran bridge

1985 ◽  
Vol 41 (10) ◽  
pp. 1342-1344 ◽  
Author(s):  
O. Yu. Printseva ◽  
A. I. Faerman ◽  
A. V. Maksimenko ◽  
A. G. Tonevitsky ◽  
O. B. Ilynsky ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Monoclonal Antibodies ◽  
Cell Surface ◽  
Smooth Muscle Cells ◽  
Surface Antigen ◽  
Muscle Cells ◽  
Ricin A Chain ◽  
A Cell ◽  
A Chain ◽  
Ricin A

Ion exchange activity in pulmonary artery smooth muscle cells: the response to hypoxia

2001 ◽  
Vol 280 (2) ◽  
pp. L264-L271 ◽  
Author(s):  
Jane A. Madden ◽  
Daniel E. Ray ◽  
Peter A. Keller ◽  
Jack G. Kleinman
Keyword(s):  
Smooth Muscle ◽  
Pulmonary Artery ◽  
Smooth Muscle Cells ◽  
Pulmonary Arteries ◽  
Muscle Cells ◽  
Cell Types ◽  
Molecular Identity ◽  
A Cell ◽  
Pulmonary Artery Smooth Muscle ◽  
Exchange Activity

The purposes of this study were to determine 1) the presence of the major ion transport activities that regulate cytoplasmic pH (pHc) in cat pulmonary artery smooth muscle cells, i.e., Na+/H+ and the Na+-dependent and -independent Cl−/HCO3 − exchange, 2) whether pHc changes in cells from small (SPAs) and large (LPAs) pulmonary arteries during hypoxia, and 3) whether changes in pHc are due to changes in the balance of exchange activities. Exchange activities as defined by physiological maneuvers rather than molecular identity were ascertained with fluorescence microscopy to document changes in the ratio of the pHc indicator 2′,7′-bis-(2-carboxyethyl)-5-(and-6)-carboxyfluorescein. Steady-state pHc was higher in LPA than in SPA normoxic smooth muscle cells. SPAs and LPAs possessed all three transport activities; in HCO3 −-containing normoxic solutions, Cl−/HCO3 − exchange rather than Na+/H+ exchange set the level of pHc; in HCO3 −-containing hypoxic solutions, pHc increased in SPA and decreased in LPA cells; altering the baseline pHc of a cell type to that of the other did not change the direction of the pHc response during hypoxia. The absence of Na+ prevented hypoxia-induced alkalinization in SPA cells; in both cell types, inhibiting the Cl−/HCO3 − exchange activities reversed the normal direction of pHc changes during hypoxia.

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