Relevant bibliographies by topics / Β-CATENIN CASCADE

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Academic literature on the topic 'Β-CATENIN CASCADE'

Author: Grafiati
Published: 11 September 2023

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Journal articles on the topic "Β-CATENIN CASCADE"

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Palchevska, O. L., V. V. Balatskyi, L. L. Macewicz, and O. O. Piven. "Cardiospecific deletion of β-catenin gene associated with an activity violation of signaling cascades involved in the development of myocardial hypertrophy." Visnik ukrains'kogo tovaristva genetikiv i selekcioneriv 15, no. 2 (February 28, 2018): 181–86. http://dx.doi.org/10.7124/visnyk.utgis.15.2.877.

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The aim of our study was to investigate the molecular mechanisms of hypertrophy response under cardiospecific β-catenin haploinsufficiency condition. Materials and methods. Studies were done with β-catenin condtional knockout mice (β-catflox/flox) and α-MHC-Cre-transgenic mice. To induce hypertrophy we used swimming test during 6 weeks. Using western-blot, we have analyzed the level of studied proteins. Results. It has been shown that the β-catenin haploinsufficiency is associated with increased signaling activity of MAPK, PI3-kinase-mTOR-dependent signaling cascades in both: with prolonged physical activity and without it. However, even with an increased activity of this signalling, β-catenin haploinsufficient mice expressed weaker hypertrophic response. Conclusions. The transcriptional activity of β-catenin is necessary for the proper interaction of signaling cascades during heart maturation and adaptation to stress. Keywords: β-catenin, hypertrophy, Wnt-signalling, MAPK signalling, PI3-kinase-mTOR-dependent cascade, PKA-signalling, myocardium.
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Zeller, Eva, Katharina Mock, Moritz Horn, Sabine Colnot, Michael Schwarz, and Albert Braeuning. "Dual-specificity phosphatases are targets of the Wnt/β-catenin pathway and candidate mediators of β-catenin/Ras signaling interactions." Biological Chemistry 393, no. 10 (October 1, 2012): 1183–91. http://dx.doi.org/10.1515/hsz-2012-0130.

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Abstract The Wnt/β-catenin and the Ras/mitogen-activated protein kinase (MAPK) pathways play important roles in cancer development. Both pathways have been studied discretely, but the mechanisms of possible crosstalk are still not fully understood. We have previously shown that β-catenin and MAPK signaling interfere with each other in murine liver in vivo and in vitro. Here, we show that dual specificity phosphatases (Dusps) 6 and 14, known to play an essential role in regulating MAPK pathway activity via feedback mechanisms, are up-regulated by activation of β-catenin in murine liver cells, whereas the epidermal growth factor receptor, an upstream effector in the Ras/MAPK cascade, is down-regulated by β-catenin. In addition, we identified a β-catenin-binding site within the Dusp6 promoter, which is responsible for the activation of the promoter by β-catenin signaling, and demonstrated reduced inducibility of MAPK signaling in cultured mouse hepatoma cells following β-catenin activation. Thus, β-catenin is able to inhibit activation of the Egfr/Ras/MAPK signaling cascade, both at the receptor level and by interfering with MAPK activity via Dusps.
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Cesari, Francesca. "A Rac1–JNK2–β-catenin domino cascade." Nature Reviews Molecular Cell Biology 9, no. 6 (May 9, 2008): 425. http://dx.doi.org/10.1038/nrm2412.

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Yang, Shengsen, Fei Zhou, Yi Dong, and Fei Ren. "α-Mangostin Induces Apoptosis in Human Osteosarcoma Cells Through ROS-Mediated Endoplasmic Reticulum Stress via the WNT Pathway." Cell Transplantation 30 (January 1, 2021): 096368972110350. http://dx.doi.org/10.1177/09636897211035080.

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α-mangostin has been confirmed to promote the apoptosis of MG-63 cells, but its specific pro-apoptosis mechanism in osteosarcoma (OS) remains further investigation. Here, we demonstrated that α-mangostin restrained the viability of OS cells (143B and Saos-2), but had little effect on the growth of normal human osteoblast. α-mangostin increased OS cell apoptosis by activating the caspase-3/8 cascade. Besides, α-mangostin induced endoplasmic reticulum (ER) stress and restrained the Wnt/β-catenin pathway activity. 4PBA (an ER stress inhibitor) or LiCl (an effective Wnt activator) treatment effectively hindered α-mangostin-induced apoptosis and the caspase-3/8 cascade. Furthermore, we also found that α-mangostin induced ER stress by promoting ROS production. And ER stress-mediated apoptosis caused by ROS accumulation depended on the inactivation of Wnt/β-catenin pathway. In addition, α-mangostin significantly hindered the growth of xenograft tumors, induced the expression of ER stress marker proteins and activation of the caspase-3/8 cascade, and restrained the Wnt/β-catenin signaling in vivo. In short, ROS-mediated ER stress was involved in α-mangostin triggered apoptosis, which might depended on Wnt/β-catenin signaling inactivation.
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Hendriksen, Jolita, Francois Fagotto, Hella van der Velde, Martijn van Schie, Jasprien Noordermeer, and Maarten Fornerod. "RanBP3 enhances nuclear export of active β-catenin independently of CRM1." Journal of Cell Biology 171, no. 5 (November 28, 2005): 785–97. http://dx.doi.org/10.1083/jcb.200502141.

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β-Catenin is the nuclear effector of the Wnt signaling cascade. The mechanism by which nuclear activity of β-catenin is regulated is not well defined. Therefore, we used the nuclear marker RanGTP to screen for novel nuclear β-catenin binding proteins. We identified a cofactor of chromosome region maintenance 1 (CRM1)–mediated nuclear export, Ran binding protein 3 (RanBP3), as a novel β-catenin–interacting protein that binds directly to β-catenin in a RanGTP-stimulated manner. RanBP3 inhibits β-catenin–mediated transcriptional activation in both Wnt1- and β-catenin–stimulated human cells. In Xenopus laevis embryos, RanBP3 interferes with β-catenin–induced dorsoventral axis formation. Furthermore, RanBP3 depletion stimulates the Wnt pathway in both human cells and Drosophila melanogaster embryos. In human cells, this is accompanied by an increase of dephosphorylated β-catenin in the nucleus. Conversely, overexpression of RanBP3 leads to a shift of active β-catenin toward the cytoplasm. Modulation of β-catenin activity and localization by RanBP3 is independent of adenomatous polyposis coli protein and CRM1. We conclude that RanBP3 is a direct export enhancer for β-catenin, independent of its role as a CRM1-associated nuclear export cofactor.
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Skokowa, Julia, Gunnar Cario, Lan Dan, Cornelia Zeidler, Vesna Bucan, and Karl Welte. "Proto-Oncogenes β- and γ-Catenin in Leukemogenesis in Severe Congenital Neutropenia (CN)." Blood 106, no. 11 (November 16, 2005): 94. http://dx.doi.org/10.1182/blood.v106.11.94.94.

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Abstract Severe congenital neutropenia (CN) is characterized by a “maturation arrest” of myeloid progenitors at the promyelocytic stage with few or no mature neutrophils in the bone marrow and blood. Administration of granulocyte colony-stimulating factor (G-CSF) increases neutrophil numbers in most CN patients. Approximately 10–15 % of CN patients develop AML or MDS by mechanisms that are as yet unknown. Since AML/MDS are not observed in cyclic (CyN) or idiopathic neutropenia patients treated with G-CSF, an underlying defect of hematopoiesis rather than G-CSF therapy per se predisposes to malignant transformation in CN patients. Recently, activation of Wnt/β-catenin-/γ-catenin-signaling cascade has been considered as important mechanism in the pathogenesis of AML and CML by enhancement of self-renewal activity and by increase of leukemic potential of myeloid progenitors. Moreover, stabilization of β-catenin led to an increased formation of nuclear β-catenin-T-cell factor complexes and altered expression of Wnt-inducible target genes in a variety of human malignancies. In the present study we investigated the role of β-catenin/γ-catenin in leukemogenesis in CN patients. CD33+ progenitors from CN patients expressed 2.5 times higher levels of b-catenin and 4 times higher levels of γ-catenin mRNA and protein, as assessed by quantitative real-time PCR and Western Blot analysis. Most important, in CN patients this increase was paralleled by dramatically elevated levels of activated nuclear β-catenin and intracellular γ-catenin proteins in CD33+ cells, as compared to G-CSF-treated healthy controls and CyN patients. Moreover, mRNA and protein levels of β- and γ-catenins were further increased in CD33+ cells and leukemic blasts from 4 CN patients, who developed AML. In line with high β-/γ-catenins levels, expression of target genes c-jun, fra-1 and PPARD was also up-regulated. There was no correlation between activated Wnt/β-/γ-catenin signaling system and mutations in G-CSF receptor, or ELA2 gene. To investigate the mechanisms of stabilization and increased nuclear translocation of b-catenin, we analyzed the components of b-catenin-degradation multiprotein complex, which contains of Axin, GSK3β, and APC. No differences in expression of Axin, GSK3β and APC as well as in phosphorylation status of GSK3β in CD33+ cells from CN patients and controls were observed. Sequence analysis revealed no mutations in β-catenin gene. Furthermore we analysed the expression of E-cadherin, which forms the transmembrane core of adherent junctions by bridging to β-catenin and therefore modulates its subcellular localization and nuclear translocation. E-cadherin mRNA and protein expression was dramatically downregulated in CD33+ myeloid progenitors from CN patients, in comparison to G-CSF treated healthy controls. Moreover, confocal microscopy revealed very low levels of co-localized E-cadherin and β-catenin in CD33+ cells from CN patients. Therefore, we hypothesize that loss of E-cadherin expression results in nuclear accumulation of β-catenin and activation of its downstream signaling in CN. Taken together, high expression of the proto-oncogenes β- and γ-catenins and nuclear accumulation of β-catenin could contribute to the malignant transformation of myelopoiesis in CN.
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Kumar, Amit, Ravindra B. Chalamalasetty, Mark W. Kennedy, Sara Thomas, Shreya N. Inala, Robert J. Garriock, and Terry P. Yamaguchi. "Zfp703 Is a Wnt/β-Catenin Feedback Suppressor Targeting the β-Catenin/Tcf1 Complex." Molecular and Cellular Biology 36, no. 12 (April 18, 2016): 1793–802. http://dx.doi.org/10.1128/mcb.01010-15.

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The Wnt/β-catenin signaling pathway controls embryonic development and adult stem cell maintenance through the regulation of transcription. Failure to downregulate Wnt signaling can result in embryonic malformations and cancer, highlighting the important role of negative regulators of the pathway. The Wnt pathway activates several negative feedback targets, including axin2 and Dkk1, that function at different levels of the signaling cascade; however, none have been identified that directly target active β-catenin/Tcf1 transcriptional complexes. We show thatZfp703is a Wnt target gene that inhibits Wnt/β-catenin activity in Wnt reporter assays and in Wnt-dependent mesoderm differentiation in embryonic stem cells. Zfp703 binds directly to Tcf1 to inhibit β-catenin/Tcf1 complex formation and does so independently of the Groucho/Tle transcriptional corepressor. We propose that Zfp703 is a novel feedback suppressor of Wnt/β-catenin signaling that functions by inhibiting the association of β-catenin with Tcf1 on Wnt response elements in target gene enhancers.
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Wang, Xiaohong, Neeta Adhikari, Qinglu Li, and Jennifer L. Hall. "LDL receptor-related protein LRP6 regulates proliferation and survival through the Wnt cascade in vascular smooth muscle cells." American Journal of Physiology-Heart and Circulatory Physiology 287, no. 6 (December 2004): H2376—H2383. http://dx.doi.org/10.1152/ajpheart.01173.2003.

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Initial studies have established expression of low-density lipoprotein (LDL) receptor-related protein 6 (LRP6) in vascular smooth muscle cells (VSMCs). We hypothesized that LRP6 is a critical mediator governing the regulation of the canonical Wnt/β-catenin/T cell factor 4 (Tcf-4) cascade in the vasculature. This hypothesis was based on our previous work demonstrating a role for the β-catenin/Tcf-4 pathway in vascular remodeling as well as work in other cell systems establishing a role for LRP family members in the Wnt cascade. In line with our hypothesis, LRP6 upregulation significantly increased Wnt-1-induced Tcf activation. Moreover, a dominant interfering LRP6 mutant lacking the carboxyl intracellular domain (LRP6ΔC) abolished Tcf activity. LRP6-induced stimulation of Tcf was blocked in VSMCs harboring constitutive expression of a dominant negative Tcf-4 transgene lacking the β-catenin binding domain, suggesting that LRP6-induced activation of Tcf was mediated through a β-catenin-dependent signal. Expression of the dominant interfering LRP6ΔC transgene was sufficient to abolish the Wnt-induced survival as well as cyclin D1 activity and cell cycle progression. In conclusion, these findings provide the first evidence of a role for an LDL receptor-related protein in the regulation of VSMC proliferation and survival through the evolutionary conserved Wnt signaling cascade.
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HAGEN, Thilo, Jaswinder K. SETHI, Neale FOXWELL, and Antonio VIDAL-PUIG. "Signalling activity of beta-catenin targeted to different subcellular compartments." Biochemical Journal 379, no. 2 (April 15, 2004): 471–77. http://dx.doi.org/10.1042/bj20031749.

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β-Catenin plays a dual role as an adhesion molecule in adherens junctions at the plasma membrane and as a key intermediate in the canonical Wnt signalling pathway. The cytosolic soluble pool of β-catenin, involved in the transmission of the Wnt signal, is normally subjected to rapid protein degradation. On activation of the Wnt cascade, β-catenin becomes stabilized and then translocates into the nucleus where it co-activates transcription factors of the TCF (T-cell factor)/LEF (lymphoid enhancer factor) family. The expression of plasma membrane-targeted forms of β-catenin has been shown to also activate TCF/LEF-dependent transcription and different mechanisms have been put forward. In the present study, we have undertaken a systematic analysis of the signalling capability of non-degradable forms of β-catenin targeted to different cellular compartments. β-Catenin targeted to the plasma membrane activated transcription to a greater extent compared with non-targeted β-catenin, and led to a marked stabilization of cytosolic soluble β-catenin. These effects were independent of the competition with endogenous β-catenin for binding to E-cadherin at the plasma membrane, since targeting non-degradable β-catenin to other cellular compartments, i.e. the outer mitochondrial membrane and the endoplasmic reticulum membrane, also resulted in the accumulation of cytosolic wild-type β-catenin and activation of β-catenin-dependent signalling. In contrast, nuclear-targeted β-catenin was without significant effect on cytosolic wild-type β-catenin and did not activate transcription. Our results suggest that cytosolic accumulation of β-catenin is a prerequisite for the activation of TCF/LEF-dependent transcription in the nucleus.
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Ishitani, Tohru, Satoshi Kishida, Junko Hyodo-Miura, Naoto Ueno, Jun Yasuda, Marian Waterman, Hiroshi Shibuya, Randall T. Moon, Jun Ninomiya-Tsuji, and Kunihiro Matsumoto. "The TAK1-NLK Mitogen-Activated Protein Kinase Cascade Functions in the Wnt-5a/Ca2+ Pathway To Antagonize Wnt/β-Catenin Signaling." Molecular and Cellular Biology 23, no. 1 (January 1, 2003): 131–39. http://dx.doi.org/10.1128/mcb.23.1.131-139.2003.

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ABSTRACT Wnt signaling controls a variety of developmental processes. The canonical Wnt/β-catenin pathway functions to stabilize β-catenin, and the noncanonical Wnt/Ca2+ pathway activates Ca2+/calmodulin-dependent protein kinase II (CaMKII). In addition, the Wnt/Ca2+ pathway activated by Wnt-5a antagonizes the Wnt/β-catenin pathway via an unknown mechanism. The mitogen-activated protein kinase (MAPK) pathway composed of TAK1 MAPK kinase kinase and NLK MAPK also negatively regulates the canonical Wnt/β-catenin signaling pathway. Here we show that activation of CaMKII induces stimulation of the TAK1-NLK pathway. Overexpression of Wnt-5a in HEK293 cells activates NLK through TAK1. Furthermore, by using a chimeric receptor (β2AR-Rfz-2) containing the ligand-binding and transmembrane segments from the β2-adrenergic receptor (β2AR) and the cytoplasmic domains from rat Frizzled-2 (Rfz-2), stimulation with the β-adrenergic agonist isoproterenol activates activities of endogenous CaMKII, TAK1, and NLK and inhibits β-catenin-induced transcriptional activation. These results suggest that the TAK1-NLK MAPK cascade is activated by the noncanonical Wnt-5a/Ca2+ pathway and antagonizes canonical Wnt/β-catenin signaling.
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Book chapters on the topic "Β-CATENIN CASCADE"

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Lai, Keane K. Y., and Michael Kahn. "Pharmacologically Targeting the WNT/β-Catenin Signaling Cascade: Avoiding the Sword of Damocles." In Pharmacology of the WNT Signaling System, 383–422. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/164_2021_523.

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Conference papers on the topic "Β-CATENIN CASCADE"

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Evert, K., Y. Qiao, J. Wang, E. Karagoz, X. Song, M. Xu, L. Che, et al. "Loss of Axin1 induced hepatocarcinogenesis requires intact β-Catenin but not Notch cascade in mice." In 35. Jahrestagung der Deutschen Arbeitsgemeinschaft zum Studium der Leber. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0038-1677207.

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Šeklić, Dragana, Milena Jovanović, Nevena Milivojević, and Marko Živanović. "PLATINUM(IV) COMPLEX AND ITS CORRESPONDING LIGAND SUPPRESS CELL MOTILITY AND PROMOTE EXPRESSION OF FRIZZLED-7 RECEPTOR IN COLORECTAL CANCER CELLS." In 1st INTERNATIONAL Conference on Chemo and BioInformatics. Institute for Information Technologies, University of Kragujevac, 2021. http://dx.doi.org/10.46793/iccbi21.288s.

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Suppression of cell movement is an imperative in the effectiveness of future generations of chemotherapeutics. Frizzled 7 receptor (FZD7), as the first protein of Wnt/β-catenin signaling cascade, plays a significant role in regulation of cell differentiation, proliferation, and cell migration. This study aimed to investigate the potential effects of platinum (IV) complex: [PtCl4 (dbu-S, S-eddp)] – C1, and its corresponding ligand – L1 on cell movement, as well as the FZD7 expression and localization after treatments on two human colorectal carcinoma cell lines (HCT-116, SW-480). A Wound healing assay was used to examine cell migration, while FZD7 protein expression was examined by immunofluorescence. Chemical compounds, especially L1, reduced cell motility of both tested cell lines. They showed a particularly good effect on HCT-116 cells, increasing protein expression of the antimigratory marker FZD7 whose localization was observed on the cell membrane of HCT-116 cells. Suppression of cell movement was significantly lower in SW-480 cells after treatments, when compared to HCT-116, with an obvious decrease of FZD7 receptor expression and its localization in the cytoplasm of these cells. Our results indicate that among the examined treatments, the ligand showed more significant results in the suppression of HCT-116 cell movement, most likely through the stimulation of differentiation, which is indicated by the promotion of FZD7 expression.
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Ghadimi, D., A. Nielsen, M. Farghaly Yoness Hassan, R. Fölster-Holst, M. de Vrese, and KJ Heller. "Modulation of GSK – 3β/β – catenin cascade by commensal bifidobateria plays an important role for the inhibition of metaflammation-related biomarkers in response to LPS or non-physiological concentrations of fructose: An in vitro study." In 47. Jahrestagung der Gesellschaft für Gastroenterologie in Bayern e.V. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-1688867.

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Nava, Miguel, Nwamaka A. Amobi, Yanyuan Wu, Robin Farias-Eisner, and Jay Vadgama. "Abstract 1333: Cross talk between mitogen-activated protein kinase signaling cascades and Wnt/β-catenin in HER2+ overexpressing breast cancer cells." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-1333.

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