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10.1038/cddis.2016.434 http://scihub22266oqcxt.onion/10.1038/cddis.2016.434 C5386453!5386453 !28182006     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28182006 &cmd=llinks): Failed to open stream: HTTP request failed! 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Coordinate activities of BRD4 and CDK9 in the transcriptional elongation complex are required for TGF?-induced Nox4 expression and myofibroblast transdifferentiation |pdf=|usr=}}{{28182006 }} gab.com Text Coordinate activities of BRD4 and CDK9 in the transcriptional elongation complex are required for TGF -induced Nox4 expression and myofibroblast transdifferentiation JO: Cell Death Dis http://www.kidney.de/pget.php?&tw=1&pmid=28182006 #FOAvip Transdifferentiation of quiescent dermal fibroblasts to secretory myofibroblasts has a central role in wound healing and pathological scar formation. This myofibroblast transdifferentiation process involves TGF?-induced de novo synthesis of alpha smooth muscle cell actin (?SMA)+ fibers that enhance contractility as well as increased expression of extracellular matrix (ECM) proteins, including collagen and fibronectin. These processes are mediated upstream by the reactive oxygen species (ROS)-producing enzyme Nox4, whose induction by TGF? is incompletely understood. In this study, we demonstrate that Nox4 is involved in ?SMA+ fiber formation and collagen production in primary human dermal fibroblasts (hDFs) using a small-molecule inhibitor and siRNA-mediated silencing. Furthermore, TGF?-induced signaling via Smad3 is required for myofibroblast transformation and Nox4 upregulation. Immunoprecipitation-selected reaction monitoring (IP-SRM) assays of the activated Smad3 complex suggest that it couples with the epigenetic reader and transcription co-activator bromodomain and extraterminal (BET) domain containing protein 4 (BRD4) to promote Nox4 transcription. In addition, cyclin-dependent kinase 9 (CDK9), a component of positive transcription elongation factor, binds to BRD4 after TGF? stimulation and is also required for RNA polymerase II phosphorylation and Nox4 transcription regulation. Surprisingly, BRD4 depletion decreases myofibroblast differentiation but does not affect collagen or fibronectin expression in primary skin fibroblasts, whereas knockdown of CDK9 decreases all myofibroblast genes. We observe enhanced numbers and persistence of myofibroblast formation and TGF? signaling in hypertrophic scars. BRD4 inhibition reverses hypertrophic skin fibroblast transdifferentiation to myofibroblasts. Our data indicate that BRD4 and CDK9 have independent, coordinated roles in promoting the myofibroblast transition and suggest that inhibition of the Smad3-BRD4 pathway may be a useful strategy to limit hypertrophic scar formation after burn injury. Twit Text FOAVip Coordinate activities of BRD4 and CDK9 in the transcriptional elongation complex are required for TGF -induced Nox4 expression and myofibroblast transdifferentiation ????Cell Death Dis http://www.kidney.de/pget.php?&tw=1&pmid=28182006 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28182006 #FOAvip English Wikipedia <ref>{{Cite pmid|28182006 }}</ref> Coordinate activities of BRD4 and CDK9 in the transcriptional elongation complex are required for TGF?-induced Nox4 expression and myofibroblast transdifferentiation #MMPMID28182006 Ijaz T ; Jamaluddin M ; Zhao Y ; Zhang Y ; Jay J ; Finnerty CC ; Herndon DN ; Tilton RG ; Brasier AR Cell Death Dis 2017[Feb]; 8 (2 ): e2606 PMID28182006 show ga Transdifferentiation of quiescent dermal fibroblasts to secretory myofibroblasts has a central role in wound healing and pathological scar formation. This myofibroblast transdifferentiation process involves TGF?-induced de novo synthesis of alpha smooth muscle cell actin (?SMA)+ fibers that enhance contractility as well as increased expression of extracellular matrix (ECM) proteins, including collagen and fibronectin. These processes are mediated upstream by the reactive oxygen species (ROS)-producing enzyme Nox4, whose induction by TGF? is incompletely understood. In this study, we demonstrate that Nox4 is involved in ?SMA+ fiber formation and collagen production in primary human dermal fibroblasts (hDFs) using a small-molecule inhibitor and siRNA-mediated silencing. Furthermore, TGF?-induced signaling via Smad3 is required for myofibroblast transformation and Nox4 upregulation. Immunoprecipitation-selected reaction monitoring (IP-SRM) assays of the activated Smad3 complex suggest that it couples with the epigenetic reader and transcription co-activator bromodomain and extraterminal (BET) domain containing protein 4 (BRD4) to promote Nox4 transcription. In addition, cyclin-dependent kinase 9 (CDK9), a component of positive transcription elongation factor, binds to BRD4 after TGF? stimulation and is also required for RNA polymerase II phosphorylation and Nox4 transcription regulation. Surprisingly, BRD4 depletion decreases myofibroblast differentiation but does not affect collagen or fibronectin expression in primary skin fibroblasts, whereas knockdown of CDK9 decreases all myofibroblast genes. We observe enhanced numbers and persistence of myofibroblast formation and TGF? signaling in hypertrophic scars. BRD4 inhibition reverses hypertrophic skin fibroblast transdifferentiation to myofibroblasts. Our data indicate that BRD4 and CDK9 have independent, coordinated roles in promoting the myofibroblast transition and suggest that inhibition of the Smad3-BRD4 pathway may be a useful strategy to limit hypertrophic scar formation after burn injury. |Adolescent [MESH] |Cell Cycle Proteins [MESH] |Cell Transdifferentiation/*physiology [MESH] |Cells, Cultured [MESH] |Child [MESH] |Child, Preschool [MESH] |Collagen/metabolism [MESH] |Cyclin-Dependent Kinase 9/*metabolism [MESH] |Female [MESH] |Fibronectins/metabolism [MESH] |Gene Expression Regulation/physiology [MESH] |Humans [MESH] |Infant [MESH] |Infant, Newborn [MESH] |Male [MESH] |Myofibroblasts/*metabolism/physiology [MESH] |NADPH Oxidase 4 [MESH] |NADPH Oxidases/*metabolism [MESH] |Nuclear Proteins/*metabolism [MESH] |Signal Transduction/physiology [MESH] |Smad3 Protein [MESH] |Transcription Factors/*metabolism [MESH] |Transcriptional Elongation Factors/*metabolism [MESH] |Transforming Growth Factor beta/*metabolism [MESH] |Up-Regulation/physiology [MESH]Coordinate activities of BRD4 and CDK9 in the transcriptional elongati(epmc).pdf DeepDyve Pubget Overpricing