Relevant bibliographies by topics / Kidney Transcription Factors Transcriptional Activation

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Academic literature on the topic 'Kidney Transcription Factors Transcriptional Activation'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Kidney Transcription Factors Transcriptional Activation"

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Khurana, Simran, Sharmistha Chakraborty, Minh Lam, Yu Liu, Yu-Ting Su, Xuan Zhao, Moin A. Saleem, Peter W. Mathieson, Leslie A. Bruggeman, and Hung-Ying Kao. "Familial Focal Segmental Glomerulosclerosis (FSGS)-linked α-Actinin 4 (ACTN4) Protein Mutants Lose Ability to Activate Transcription by Nuclear Hormone Receptors." Journal of Biological Chemistry 287, no. 15 (February 17, 2012): 12027–35. http://dx.doi.org/10.1074/jbc.m112.345421.

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Mutations in α-actinin 4 (ACTN4) are linked to familial forms of focal segmental glomerulosclerosis (FSGS), a kidney disease characterized by proteinuria due to podocyte injury. The mechanisms underlying ACTN4 mutant-associated FSGS are not completely understood. Although α-actinins are better known to cross-link actin filaments and modulate cytoskeletal organization, we have previously shown that ACTN4 interacts with transcription factors including estrogen receptor and MEF2s and potentiates their transcriptional activity. Nuclear receptors including retinoic acid receptor (RAR) have been proposed to play a protective role in podocytes. We show here that ACTN4 interacts with and enhances transcriptional activation by RARα. In addition, FSGS-linked ACTN4 mutants not only mislocalized to the cytoplasm, but also lost their ability to associate with nuclear receptors. Consequently, FSGS-linked ACTN4 mutants failed to potentiate transcriptional activation by nuclear hormone receptors in podocytes. In addition, overexpression of these mutants suppressed the transcriptional activity mediated by endogenous wild-type ACTN4 possibly by a cytoplasmic sequestration mechanism. Our data provide the first link between FSGS-linked ACTN4 mutants and transcriptional activation by nuclear receptor such as RARα and peroxisome proliferator-activated receptor γ.
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NAGARAJAN, Raman P., Feifei CHEN, Wei LI, Eva VIG, Maureen A. HARRINGTON, Harikrishna NAKSHATRI, and Yan CHEN. "Repression of transforming-growth-factor-β-mediated transcription by nuclear factor κB." Biochemical Journal 348, no. 3 (June 7, 2000): 591–96. http://dx.doi.org/10.1042/bj3480591.

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Activation of transforming growth factor-β (TGF-β) and activin receptors leads to phosphorylation of Sma- and Mad-related protein 2 (Smad2) and Smad3, which function as transcription factors to regulate gene expression. Smad7 is a regulatory protein which is able to inhibit TGF-β and activin signalling in a negative-feedback loop, mediated by a direct regulation by Smad3 and Smad4 via a Smad-binding element (SBE) in the Smad7 promoter. Interestingly, we found that the Smad7 promoter was also regulated by nuclear factor ĸB (NF-ĸB), a transcription factor which plays an important role in inflammation and the immune response. Expression of NF-ĸB p65 subunit was able to inhibit the Smad7 promoter activity, and this inhibition could be reversed by co-expression of IĸB, an inhibitor of NF-ĸB. In addition, the inhibitory activity of p65 was observed in a minimal promoter that contained only the Smad7 SBE and a TATA box, without any consensus NF-ĸB binding site. This inhibitory effect appeared to be common to other TGF-β- and activin-responsive promoters, since p65 also inhibited the forkhead-activin-signal-transducer-2-mediated activation of a Xenopus Mix.2 promoter, as well as the Smad3-mediated activation of 3TP-lux which contains PMA-responsive elements and a plasminogen-activator-inhibitor-1 promoter. Activation of endogenous NF-ĸB by tumour necrosis factor-α (TNF-α) was also able to inhibit the Smad7 promoter in human embryonic kidney 293 cells. In human hepatoma HepG2 cells, TNF-α was able to inhibit TGF-β- and activin-mediated transcriptional activation. Furthermore, overexpression of the transcription co-activator p300 could abrogate the inhibitory effect of NF-ĸB on the Smad7 promoter. Taken together, these data have indicated a novel mode of crosstalk between the Smad and the NF-ĸB signalling cascades at the transcriptional level by competing for a limiting pool of transcription co-activators.
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Zhou, Xiaoming, Joan D. Ferraris, Qi Cai, Anupam Agarwal, and Maurice B. Burg. "Increased reactive oxygen species contribute to high NaCl-induced activation of the osmoregulatory transcription factor TonEBP/OREBP." American Journal of Physiology-Renal Physiology 289, no. 2 (August 2005): F377—F385. http://dx.doi.org/10.1152/ajprenal.00463.2004.

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The signaling pathways leading to high NaCl-induced activation of the transcription factor tonicity-responsive enhancer binding protein/osmotic response element binding protein (TonEBP/OREBP) remain incompletely understood. High NaCl has been reported to produce oxidative stress. Reactive oxygen species (ROS), which are a component of oxidative stress, contribute to regulation of transcription factors. The present study was undertaken to test whether the high NaCl-induced increase in ROS contributes to tonicity-dependent activation of TonEBP/OREBP. Human embryonic kidney 293 cells were used as a model. We find that raising NaCl increases ROS, including superoxide. N-acetylcysteine (NAC), an antioxidant, and MnTBAP, an inhibitor of superoxide, reduce high NaCl-induced superoxide activity and suppress both high NaCl-induced increase in TonEBP/OREBP transcriptional activity and high NaCl-induced increase in expression of BGT1mRNA, a transcriptional target of TonEBP/OREBP. Catalase, which decomposes hydrogen peroxide, does not have these effects, whether applied exogenously or overexpressed within the cells. Furthermore, NAC and MnTBAP, but not catalase, blunt high NaCl-induced increase in TonEBP/OREBP transactivation. NG-monomethyl-l-arginine, a general inhibitor of nitric oxide synthase, has no significant effect on either high NaCl-induced increase in superoxide or TonEBP/OREBP transcriptional activity, suggesting that the effects of ROS do not involve nitric oxide. Ouabain, an inhibitor of Na-K-ATPase, attenuates high NaCl-induced superoxide activity and inhibits TonEBP/OREBP transcriptional activity. We conclude that the high NaCl-induced increase in ROS, including superoxide, contributes to activation of TonEBP/OREBP by increasing its transactivation.
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MacDougald, O. A., and D. B. Jump. "Identification of functional cis-acting elements within the rat liver S14 promoter." Biochemical Journal 280, no. 3 (December 15, 1991): 761–67. http://dx.doi.org/10.1042/bj2800761.

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The structure of DNAase I hypersensitive site 1 (Hss-1), located adjacent to the 5′ end of the rat liver S14 gene, is regulated by tissue-specific factors, and its formation correlates with the transcriptional activation of the S14 gene. We propose that tissue-specific trans-acting factors interacting with key cis-linked elements within this site function in the initiation of S14 gene transcription. To examine this hypothesis we used DNAase I footprint, gel shift and in vitro transcriptional analyses to identify cis-linked elements that function in the control of S14 gene transcription. Binding of rat liver nuclear proteins to the S14 promoter (from -8 to -464 bp) produced four DNAase I footprints (designated A-D). Gel shift studies showed that DNA-protein binding was tissue- and sequence-specific, differentially heat-sensitive, and abolished by proteinase K. The function of the four cis-acting elements was assessed by using an in vitro transcription initiation assay in which the S14 promoter was fused to a reporter gene (G-free cassette). Deletion studies showed that nuclear factors binding to regions A (-48 to -63 bp), B (-88 to -113 bp) and D (-286 to -310 bp) enhanced the rate of initiation of transcription, while proteins binding to region C (-227 to -244 bp) suppressed the rate of initiation of transcription. Based on oligonucleotide competition studies, we suggest that hepatic NF-1 (or a related protein) binding to the A region enhances the rate of initiation of S14 gene transcription. Since trans-acting factors interacting with regions B and D are found in liver but not in spleen or kidney, we suggest that the proteins interacting with these regions may be involved in the tissue-specific augmentation of S14 gene transcription.
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Matsuda, Miyuki, Kouichi Tamura, Hiromichi Wakui, Toru Dejima, Akinobu Maeda, Masato Ohsawa, Tomohiko Kanaoka, et al. "Involvement of Runx3 in the basal transcriptional activation of the mouse angiotensin II type 1 receptor-associated protein gene." Physiological Genomics 43, no. 14 (July 2011): 884–94. http://dx.doi.org/10.1152/physiolgenomics.00005.2011.

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We previously cloned a molecule that interacts with angiotensin II type 1 (AT1) receptor to exert an inhibitory function on AT1 receptor signaling that we named ATRAP/ Agtrap (for AT1 receptor-associated protein). In the present study we examined the regulation of basal ATRAP gene expression using renal distal convoluted tubule cells. We found that serum starvation upregulated basal expression of ATRAP gene, a response that required de novo mRNA and protein synthesis. Luciferase assay revealed that the proximal promoter region directs transcription and that a putative binding site of runt-related transcription factors (RBE) is important for transcriptional activation. The results of RBE-decoy transfection and endogenous knockdown by small interference RNA showed that the runt-related transcription factor Runx3 is involved in ATRAP gene expression. Chromatin immunoprecipitation assay also supported the binding of Runx3 to the ATRAP promoter in renal distal convoluted tubule cells. Immunohistochemistry demonstrated the expression of Runx3 and ATRAP proteins in the distal convoluted and connecting tubules of the kidney in consecutive sections. Furthermore, the Runx3 immunostaining was decreased together with a concomitant suppression of ATRAP expression in the affected kidney after 7 days of unilateral ureteral obstruction. These findings indicate that Runx3 plays a role in ATRAP gene expression in renal distal tubular cells both in vitro and in vivo.
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Pecorino, L. T., A. L. Darrow, and S. Strickland. "In vitro analysis of the tissue plasminogen activator promoter reveals a GC box-binding activity present in murine brain but undetectable in kidney and liver." Molecular and Cellular Biology 11, no. 6 (June 1991): 3139–47. http://dx.doi.org/10.1128/mcb.11.6.3139.

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Tissue plasminogen activator (t-PA) mRNA levels are high in murine brain, lower in kidney, and undetectable in liver. Differences in t-PA mRNA levels are regulated in part at the transcriptional level. Brain, kidney, and liver nuclear extracts direct regulated transcription from the murine t-PA promoter in a manner that reflects the relative levels of t-PA gene expression in these tissues in vivo. Analysis of mutants has defined two GC box motifs as important elements for regulated transcription in vitro. Upon investigation of protein-DNA binding, we detected an activity in brain extracts which was not detected in kidney or liver extracts. An Sp1-like factor also binds to this region in all three tissue types. DNA interference experiments show that the brain-enriched binding activity and the Sp1-like factor contact the same GC-rich sequences. These studies provide additional evidence that brain-enriched DNA-binding activities can interact with sequences also recognized by ubiquitous transcription factors.
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Pecorino, L. T., A. L. Darrow, and S. Strickland. "In vitro analysis of the tissue plasminogen activator promoter reveals a GC box-binding activity present in murine brain but undetectable in kidney and liver." Molecular and Cellular Biology 11, no. 6 (June 1991): 3139–47. http://dx.doi.org/10.1128/mcb.11.6.3139-3147.1991.

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Tissue plasminogen activator (t-PA) mRNA levels are high in murine brain, lower in kidney, and undetectable in liver. Differences in t-PA mRNA levels are regulated in part at the transcriptional level. Brain, kidney, and liver nuclear extracts direct regulated transcription from the murine t-PA promoter in a manner that reflects the relative levels of t-PA gene expression in these tissues in vivo. Analysis of mutants has defined two GC box motifs as important elements for regulated transcription in vitro. Upon investigation of protein-DNA binding, we detected an activity in brain extracts which was not detected in kidney or liver extracts. An Sp1-like factor also binds to this region in all three tissue types. DNA interference experiments show that the brain-enriched binding activity and the Sp1-like factor contact the same GC-rich sequences. These studies provide additional evidence that brain-enriched DNA-binding activities can interact with sequences also recognized by ubiquitous transcription factors.
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Chan, Siu Chiu, Ying Zhang, Annie Shao, Svetlana Avdulov, Jeremy Herrera, Karam Aboudehen, Marco Pontoglio, and Peter Igarashi. "Mechanism of Fibrosis in HNF1B-Related Autosomal Dominant Tubulointerstitial Kidney Disease." Journal of the American Society of Nephrology 29, no. 10 (August 10, 2018): 2493–509. http://dx.doi.org/10.1681/asn.2018040437.

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BackgroundMutation of HNF1B, the gene encoding transcription factor HNF-1β, is one cause of autosomal dominant tubulointerstitial kidney disease, a syndrome characterized by tubular cysts, renal fibrosis, and progressive decline in renal function. HNF-1β has also been implicated in epithelial–mesenchymal transition (EMT) pathways, and sustained EMT is associated with tissue fibrosis. The mechanism whereby mutated HNF1B leads to tubulointerstitial fibrosis is not known.MethodsTo explore the mechanism of fibrosis, we created HNF-1β–deficient mIMCD3 renal epithelial cells, used RNA-sequencing analysis to reveal differentially expressed genes in wild-type and HNF-1β–deficient mIMCD3 cells, and performed cell lineage analysis in HNF-1β mutant mice.ResultsThe HNF-1β–deficient cells exhibited properties characteristic of mesenchymal cells such as fibroblasts, including spindle-shaped morphology, loss of contact inhibition, and increased cell migration. These cells also showed upregulation of fibrosis and EMT pathways, including upregulation of Twist2, Snail1, Snail2, and Zeb2, which are key EMT transcription factors. Mechanistically, HNF-1β directly represses Twist2, and ablation of Twist2 partially rescued the fibroblastic phenotype of HNF-1β mutant cells. Kidneys from HNF-1β mutant mice showed increased expression of Twist2 and its downstream target Snai2. Cell lineage analysis indicated that HNF-1β mutant epithelial cells do not transdifferentiate into kidney myofibroblasts. Rather, HNF-1β mutant epithelial cells secrete high levels of TGF-β ligands that activate downstream Smad transcription factors in renal interstitial cells.ConclusionsAblation of HNF-1β in renal epithelial cells leads to the activation of a Twist2-dependent transcriptional network that induces EMT and aberrant TGF-β signaling, resulting in renal fibrosis through a cell-nonautonomous mechanism.
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Bollinger, Lance M., Carol A. Witczak, Joseph A. Houmard, and Jeffrey J. Brault. "SMAD3 augments FoxO3-induced MuRF-1 promoter activity in a DNA-binding-dependent manner." American Journal of Physiology-Cell Physiology 307, no. 3 (August 1, 2014): C278—C287. http://dx.doi.org/10.1152/ajpcell.00391.2013.

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Muscle-specific RING finger-1 (MuRF-1), a ubiquitin ligase and key regulator of proteasome-dependent protein degradation, is highly expressed during skeletal muscle atrophy. The transcription factor forkhead box O3 (FoxO3) induces MuRF-1 expression, but the direct role of other major atrophy-related transcription factors, such as SMAD3, is largely unknown. The goal of this study was to determine whether SMAD3 individually regulates, or with FoxO3 coordinately regulates, MuRF-1 expression. In cultured myotubes or human embryonic kidney cells, MuRF-1 mRNA content and promoter activity were increased by FoxO3 but not by SMAD3 overexpression. However, FoxO3 and SMAD3 coexpression synergistically increased MuRF-1 mRNA and promoter activity. Mutation of the SMAD-binding element (SBE) in the proximal MuRF-1 promoter or overexpression of a SMAD3 DNA-binding mutant attenuated FoxO3-dependent MuRF-1 promoter activation, showing that SMAD binding to DNA is required for optimal activation of FoxO3-induced transcription of MuRF-1. Using chromatin immunoprecipitation, SMAD3 DNA binding increased FoxO3 abundance and SBE mutation reduced FoxO3 abundance on the MuRF-1 promoter. Furthermore, SMAD3 overexpression dose-dependently increased FoxO3 protein content, and coexpression of FoxO3 and SMAD3 synergistically increased FoxO-dependent gene transcription [assessed with a FoxO response element (FRE)-driven reporter]. Collectively, these results show that SMAD3 regulates transcription of MuRF-1 by increasing FoxO3 binding at a conserved FRE-SBE motif within the proximal promoter region, and by increasing FoxO3 protein content and transcriptional activity. These data are the first to indicate that two major transcription factors regulating protein degradation, FoxO3 and SMAD3, converge to coordinately and directly regulate transcription of MuRF-1.
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Nishiya, Yuri, Kohei Kawaguchi, Kosuke Kudo, Takuya Kawaguchi, Juma Obayashi, Kunihide Tanaka, Kei Ohyama, et al. "The Expression of Transcription Factors in Fetal Lamb Kidney." Journal of Developmental Biology 9, no. 2 (June 19, 2021): 22. http://dx.doi.org/10.3390/jdb9020022.

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(1) Background: Renal development involves frequent expression and loss of transcription factors, resulting in the activation of genes. Wilms’ tumor 1 (WT1), hepatocyte nuclear factor-1-beta (HNF1β), and paired box genes 2 and 8 (Pax2 and Pax8) play an important role in renal development. With this in vivo study, we examined the period and location of expression of these factors in renal development. (2) Methods: Fetal lamb kidneys (50 days from gestation to term) and adult ewe kidneys were evaluated by hematoxylin and eosin staining. Serial sections were subjected to immunohistochemistry for WT1, HNF1β, Pax2, and Pax8. (3) Results: Pax2, Pax8, and HNF1β expression was observed in the ureteric bud and collecting duct epithelial cells. We observed expression of WT1 alone in metanephric mesenchymal cells, glomerular epithelial cells, and interstitial cells in the medullary rays and Pax8 and HNF1β expression in tubular epithelial cells. WT1 was highly expressed in cells more proximal to the medulla in renal vesicles and in C- and S-shaped bodies. Pax2 was expressed in the middle and peripheral regions, and HNF1β in cells in the region in the middle of these. (4) Conclusions: WT1 is involved in nephron development. Pax2, Pax8, and HNF1β are involved in nephron maturation and the formation of peripheral collecting ducts from the Wolffian duct.
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Dissertations / Theses on the topic "Kidney Transcription Factors Transcriptional Activation"

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Al-Rasheed, Nawal Mohammed. "Proinsulin C-peptide : activation of intracellular signalling pathways and modulation of transcription factors in opossum kidney proximal tubular cells." Thesis, University of Leicester, 2006. http://hdl.handle.net/2381/29949.

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In recent years an increasingly substantial body of data, supports a role for C-peptide in several biological activities. However, the precise molecular mechanisms of C-peptide action are not fully understood. The aim of this thesis was to study the intracellular signalling pathways and the transcription factors that C-peptide activates in proximal tubular cells using opossum kidney cells (OK) as a model. Using specific inhibitors and phospho-specific antibodies, intracellular signalling pathways activated by C-peptide were examined by kinase assay and Western blotting. The results show that C-peptide is able to activate extracellular signal regulated kinase (ERK), phosphatidylinositol 3-kinase (PI 3-kinase) and PKC-a. ERK activation was attenuated by PKC inhibitor pre-treatment and activation of ERK and PKC-a were abolished in the absence of extracellular Ca2+. Elevations of [Ca2+]i were examined using confocal microscopy. C-peptide induced transient increase in [Ca2+]i but the response of cells was variable. Thymidine incorporation assay was used to assess proliferation. C-peptide was found to be a functional mitogen in this cell type stimulating significantly increased cell proliferation. Proliferator-activated receptor (PPAR) transcriptional activity was measured using a luciferase reporter assay in OK cells. C-peptide induced concentration-dependent stimulation of PPARy activity. C-peptide also substantially augmented ciglitazone-stimulated PPARy activity. GW9662, an irreversible PPARy antagonist, blocked PPARy activation by ciglitazone, but had no effect on C-peptide-stimulated PPARy activity. C-peptide stimulation of PPARy was attenuated by wortmannin pre-treatment, and by expression of a dominant negative PI 3-kinase p85 regulatory subunit (Ap85). C-peptide had no effect on protein expression levels of PPARy. PPARy phosphorylation was examined by [32P]-orthophosphate labelling of OK cells and immunoprecipitation of phospho-PPARy. C-peptide-induced PI 3-kinase dependent phosphorylation of PPARy. C-peptide is able to protect against tumor necrosis factor-alpha- (TNF-a) induced proximal tubular cells toxicity. Stimulation with 300ng/ml TNF-a for 24 hours resulted in significant reduction of cell viability which was reversed by pretreatment with C-peptide. TNF-a induced apoptosis was detected by measuring histone associated DNA fragments and DNA nick end-labelling of OK cells. Incubation of cells with 300ng/ml TNF-a for 24 hours induced apoptosis, but C-peptide pr-etreatment protected against TNF-a induced apoptosis. The protective effects of C-peptide were associated with activation of nuclear factor kB (NFkB) and increased expression of TNF receptor-associated factor 2, the product of an NFkB-dependent survival gene. This was dependent upon activation of PI 3-kinase, but not ERK. All C-peptide effects were abolished by pretreatment with PTX implicating a G-protein coupled receptor (GPCR), to either Goii or GOo, in the transduction of these events. C-peptide increased [35S]-GTPyS binding to Ga* in OK cell membranes. This study has now for the first time demonstrated specifically that Ga* proteins are activated by C-peptide binding to a GPCR. Despite being ignored for many years it is now clear that C-peptide possesses important biological properties and may potentially protect against diabetic complications.
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Siu, Yeung-tung, and 蕭揚東. "Activation of TORC1 transcriptional coactivator through MEKK1-introduced phosphorylation and ubiquitination." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2009. http://hub.hku.hk/bib/B42841653.

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Siu, Yeung-tung. "Activation of TORC1 transcriptional coactivator through MEKK1-introduced phosphorylation and ubiquitination." Click to view the E-thesis via HKUTO, 2009. http://sunzi.lib.hku.hk/hkuto/record/B42841653.

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Malin, Stephen. "Deciphering mechanisms of transcriptional activation and repression in B lymphocytes /." Stockholm : Karolinska institutet, 2004. http://diss.kib.ki.se/2004/91-7349-958-7/.

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Miyata, Kenji Sean. "The molecular mechanism of transcriptional activation by the peroxisome proliferator activated-receptor (alpha) /." *McMaster only, 1999.

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Perissi, Valentina. "A specific corepressor/coactivator exchange complex required in development and homeostasis for transcriptional activation by nuclear receptors, and other transcription factors /." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2004. http://wwwlib.umi.com/cr/ucsd/fullcit?p3120447.

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Wang, Zhibin. "Molecular mechanism of Arabidopsis CBF mediated plant cold-regulated gene transcriptional activation." Columbus, Ohio : Ohio State University, 2006. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1158600906.

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Almengor, Audry C. "Transcriptional regulation of the MGA virulence regulon in Streptococcus pyogenes." Access to abstract only; dissertation is embargoed until after 12/19/2006, 2005. http://www4.utsouthwestern.edu/library/ETD/etdDetails.cfm?etdID=115.

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Bothe, Anna Melissa [Verfasser]. "Investigating the Genomic Effects of Glucocorticoid Receptor Activation : An Analysis of Transcriptional Memory and Mechanisms That Direct Divergent Genomic Occupancy of Related Transcription Factors / Anna Melissa Bothe." Berlin : Freie Universität Berlin, 2021. http://nbn-resolving.de/urn:nbn:de:kobv:188-refubium-31999-3.

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Zhao, Xueyan. "Regulation of human MMP-9 gene expression by transcriptional coactivators and interferon beta." Thesis, Birmingham, Ala. : University of Alabama at Birmingham, 2008. https://www.mhsl.uab.edu/dt/2009r/zhao.pdf.

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Books on the topic "Kidney Transcription Factors Transcriptional Activation"

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Transcriptional regulation: Methods and protocols. New York: Humana Press, 2012.

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Hughes, Jeremy. Proteinuria as a direct cause of progression. Edited by David J. Goldsmith. Oxford University Press, 2015. http://dx.doi.org/10.1093/med/9780199592548.003.0137.

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Proximal tubular cells reabsorb any filtered proteins during health via cell surface receptors such as megalin and cubulin so that very low levels of protein are present in the excreted urine. Significant proteinuria is a common finding in patients with many renal diseases. Proteinuria is a marker of glomerular damage and podocyte loss and injury in particular. The degree of proteinuria at presentation or during the course of the disease correlates with long-term outcome in many renal diseases. Proteinuria per se may be nephrotoxic and thus directly relevant to the progression of renal disease rather than simply acting as a marker of the severity of glomerular injury and podocytes loss. Seminal studies used the atypical renal anatomy of the axolotl to instill proteins directly into the tubular lumen without requiring passage through the glomerulus. This indicated that tubular protein could be cytotoxic and induce interstitial inflammation and fibrosis in the peritubular region. Cell culture studies demonstrate that exposure to proteins results in proximal tubular cell activation and the production of pro-inflammatory and pro-fibrotic mediators. Proximal tubular cell death occurred in some studies reinforcing the potential of protein to exert cytotoxic effects via oxidative stress or endoplasmic reticulum stress. Analysis of renal biopsy material from both experimental studies using models of proteinuric disease or patients with various proteinuric diseases provided evidence of activation of transcription factors and production of chemokines and pro-inflammatory mediators by proximal tubular cells. These data strongly suggest that although proteinuria is the result of glomerular disease it also represents an important cause of progression in patients with chronic kidney disease associated with proteinuria.
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Yang, Jin, Pei Han, Wei Li, and Ching-Pin Chang. Epigenetics and post-transcriptional regulation of cardiovascular development. Edited by José Maria Pérez-Pomares, Robert G. Kelly, Maurice van den Hoff, José Luis de la Pompa, David Sedmera, Cristina Basso, and Deborah Henderson. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780198757269.003.0032.

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Cardiac organogenesis requires the control of gene expression at distinct developmental windows in order to organize morphogenetic steps in the correct sequence for heart development. This is facilitated by concerted regulation at three levels: chromatin, transcription, and post-transcriptional modifications. Epigenetic regulation at the chromatin level changes the chromatin scaffold of DNA to regulate accessibility of the DNA sequence to transcription factors for genetic activation or repression. At the genome, long non-coding RNAs work with epigenetic factors to alter the chromatin scaffold or form DNA-RNA complexes at specific genomic loci to control the transcription of genetic information. After RNA transcription, the expression of genetic information can be further modified by microRNAs. Each layer of gene regulation requires the participation of many factors, with their combinatorial interactions providing variations of genetic expression at distinct pathophysiological phases of the heart. The major functions of chromatin remodellers and non-coding RNAs are discussed.
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Book chapters on the topic "Kidney Transcription Factors Transcriptional Activation"

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Herrera, F. J., D. D. Shooltz, and S. J. Triezenberg. "Mechanisms of Transcriptional Activation in Eukaryotes." In Transcription Factors, 3–31. Berlin, Heidelberg: Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/978-3-642-18932-6_1.

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Li, Bin. "Using Systems Biology Approaches to Predict New Players in the Innate Immune System." In Handbook of Research on Computational and Systems Biology, 428–77. IGI Global, 2011. http://dx.doi.org/10.4018/978-1-60960-491-2.ch020.

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Toll-like receptors (TLRs) are critical players in the innate immune response to pathogens. However, transcriptional regulatory mechanisms in the TLR activation pathways are still relatively poorly characterized. To address this question, the author of this chapter applied a systematic approach to predict transcription factors that temporally regulate differentially expressed genes under diverse TLR stimuli. Time-course microarray data were selected from mouse bone marrow-derived macrophages stimulated by six TLR agonists. Differentially regulated genes were clustered on the basis of their dynamic behavior. The author then developed a computational method to identify positional overlapping transcription factor (TF) binding sites in each cluster, so as to predict possible TFs that may regulate these genes. A second microarray dataset, on wild-type, Myd88-/- and Trif-/- macrophages stimulated by lipopolysaccharide (LPS), was used to provide supporting evidence on this combined approach. Overall, the author was able to identify known TLR TFs, as well as to predict new TFs that may be involved in TLR signaling.
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Distler, Oliver, and Caroline Ospelt. "Rheumatoid arthritis: basic mechanisms in joints." In ESC CardioMed, 1109–12. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780198784906.003.0271.

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Rheumatoid arthritis (RA) is a destructive polyarthritis which mostly starts in the small joints of the hands and feet. In the course of the disease, more proximal joints also become involved. The progressive destruction of joint structures is mediated by the chronically inflamed, hyperplasic synovial tissue, which attaches to and degrades the adjacent joint cartilage. Typical changes of the RA synovium are increased cellularity in the synovial lining and sublining layer, including vascularization, giant cell formation, and immigration of immune cells. The inflammatory cell infiltrate comprises macrophages, monocytes, dendritic cells, T cells, B cells, plasma cells, innate lymphoid cells, and mast cells. These cells together with resident stromal cells (synovial fibroblasts) form a complex network and maintain inflammatory and destructive processes via the secretion of various cytokines and chemokines. Intracellularly, cytokine-activated receptor signalling is mediated via protein kinase-dependent signalling pathways, such as mitogen-activated protein kinases and Janus kinase, which leads to the activation of transcription factors and thus changes in the transcriptional programme. Gene transcription is additionally modified by epigenetic mechanisms and post-transcriptionally by microRNA.
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Lucchesi, John C. "Stem cells." In Epigenetics, Nuclear Organization & Gene Function, 191–204. Oxford University Press, 2019. http://dx.doi.org/10.1093/oso/9780198831204.003.0017.

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Abstract:
The zygote and the very early cells are totipotent because they can produce a whole organism. Later, cells become pluripotent because they can differentiate into different subgroups of tissues. These cells can be extracted as embryonic stem cells (ESCs). Their pluripotent nature is due to the action of the pioneer transcription factors Oct4, Sox2 and Nanog. Multipotent or progenitor stem cells are present in adult organisms where they can differentiate into the various cells present in specific tissues. Differentiation depends on their microenvironment or niche. Differentiation of stem cells requires the silencing of the pluripotency genes and the activation of genes that are characteristic of different cell types. The genome of stem cells exhibits the same features of topological organization that are found in somatic cells. At the onset and throughout differentiation, the topological organization of the ESC genome changes, reflecting the changes in transcriptional activity that underlie the progression of pluripotent cells to multipotent progenitor cells and then to differentiated cells.
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5

Song, Jie, and Maréne Landström. "Lys63-Linked Polyubiquitination of Transforming Growth Factor β Type I Receptor (TβRI) Specifies Oncogenic Signaling." In Ubiquitin - Proteasome Pathway. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.93065.

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Abstract:
Transforming growth factor β (TGFβ) is a multifunctional cytokine with potent regulatory effects on cell fate during embryogenesis, in the normal adult organism, and in cancer cells. In normal cells, the signal from the TGFβ ligand is transduced from the extracellular space to the cell nucleus by transmembrane serine–threonine kinase receptors in a highly specific manner. The dimeric ligand binding to the TGFβ Type II receptor (TβRII) initiates the signal and then recruits the TGFβ Type I receptor (TβRI) into the complex, which activates TβRI. This causes phosphorylation of receptor-activated Smad proteins Smad2 and Smad3 and promotes their nuclear translocation and transcriptional activity in complex with context-dependent transcription factors. In several of our most common forms of cancer, this pathway is instead regulated by polyubiquitination of TβRI by the E3 ubiquitin ligase TRAF6, which is associated with TβRI. The activation of TRAF6 promotes the proteolytic cleavage of TβRI, liberating its intracellular domain (TβRI-ICD). TβRI-ICD enters the cancer cell nucleus in a manner dependent on the endosomal adaptor proteins APPL1/APPL2. Nuclear TβRI-ICD promotes invasion by cancer cells and is recognized as acting distinctly and differently from the canonical TGFβ-Smad signaling pathway occurring in normal cells.
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