Relevant bibliographies by topics / Transforming growth factor β receptor II

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Academic literature on the topic 'Transforming growth factor β receptor II'

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Published: 11 March 2023

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Journal articles on the topic "Transforming growth factor β receptor II"

1

Anders, Robert A., Sandra L. Arline, Jules J. E. Doré, and Edward B. Leof. "Distinct Endocytic Responses of Heteromeric and Homomeric Transforming Growth Factor β Receptors." Molecular Biology of the Cell 8, no. 11 (November 1997): 2133–43. http://dx.doi.org/10.1091/mbc.8.11.2133.

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Transforming growth factor β (TGFβ) family ligands initiate a cascade of events capable of modulating cellular growth and differentiation. The receptors responsible for transducing these cellular signals are referred to as the type I and type II TGFβ receptors. Ligand binding to the type II receptor results in the transphosphorylation and activation of the type I receptor. This heteromeric complex then propagates the signal(s) to downstream effectors. There is presently little data concerning the fate of TGFβ receptors after ligand binding, with conflicting reports indicating no change or decreasing cell surface receptor numbers. To address the fate of ligand-activated receptors, we have used our previously characterized chimeric receptors consisting of the ligand binding domain from the granulocyte/macrophage colony-stimulating factor α or β receptor fused to the transmembrane and cytoplasmic domain of the type I or type II TGFβ receptor. This system not only provides the necessary sensitivity and specificity to address these types of questions but also permits the differentiation of endocytic responses to either homomeric or heteromeric intracellular TGFβ receptor oligomerization. Data are presented that show, within minutes of ligand binding, chimeric TGFβ receptors are internalized. However, although all the chimeric receptor combinations show similar internalization rates, receptor down-regulation occurs only after activation of heteromeric TGFβ receptors. These results indicate that effective receptor down-regulation requires cross-talk between the type I and type II TGFβ receptors and that TGFβ receptor heteromers and homomers show distinct trafficking behavior.
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Zhang, Wei, Yaxin Jiang, Qiang Wang, Xinyong Ma, Zeyu Xiao, Wei Zuo, Xiaohong Fang, and Ye-Guang Chen. "Single-molecule imaging reveals transforming growth factor-β-induced type II receptor dimerization." Proceedings of the National Academy of Sciences 106, no. 37 (August 31, 2009): 15679–83. http://dx.doi.org/10.1073/pnas.0908279106.

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Transforming growth factor-β (TGF-β) elicits its signals through two transmembrane serine/threonine kinase receptors, type II (TβRII) and type I receptors. It is generally believed that the initial receptor dimerization is an essential event for receptor activation. However, previous studies suggested that TGF-β signals by binding to the preexisting TβRII homodimer. Here, using single molecule microscopy to image green fluorescent protein (GFP)-labeled TβRII on the living cell surface, we demonstrated that the receptor could exist as monomers at the low expression level in resting cells and dimerize upon TGF-β stimulation. This work reveals a model in which the activation of serine-threonine kinase receptors is also accomplished via dimerization of monomers, suggesting that receptor dimerization is a general mechanism for ligand-induced receptor activation.
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Wicks, Stephen J., Stephen Lui, Nadia Abdel-Wahab, Roger M. Mason, and Andrew Chantry. "Inactivation of Smad-Transforming Growth Factor β Signaling by Ca2+-Calmodulin-Dependent Protein Kinase II." Molecular and Cellular Biology 20, no. 21 (November 1, 2000): 8103–11. http://dx.doi.org/10.1128/mcb.20.21.8103-8111.2000.

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ABSTRACT Members of the transforming growth factor β (TGF-β) family transduce signals through Smad proteins. Smad signaling can be regulated by the Ras/Erk/mitogen-activated protein pathway in response to receptor tyrosine kinase activation and the gamma interferon pathway and also by the functional interaction of Smad2 with Ca2+-calmodulin. Here we report that Smad–TGF-β-dependent transcriptional responses are prevented by expression of a constitutively activated Ca2+-calmodulin-dependent protein kinase II (Cam kinase II). Smad2 is a target substrate for Cam kinase II in vitro at serine-110, -240, and -260. Cam kinase II induces in vivo phosphorylation of Smad2 and Smad4 and, to a lesser extent, Smad3. A phosphopeptide antiserum raised against Smad2 phosphoserine-240 reacted with Smad2 in vivo when coexpressed with Cam kinase II and by activation of the platelet-derived growth factor receptor, the epidermal growth factor receptor, HER2 (c-erbB2), and the TGF-β receptor. Furthermore, Cam kinase II blocked nuclear accumulation of a Smad2 and induced Smad2-Smad4 hetero-oligomerization independently of TGF-β receptor activation, while preventing TGF-β-dependent Smad2-Smad3 interactions. These findings provide a novel cross-talk mechanism by which Ca2+-dependent kinases activated downstream of multiple growth factor receptors antagonize cell responses to TGF-β.
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Clarke, David C., Meredith L. Brown, Richard A. Erickson, Yigong Shi, and Xuedong Liu. "Transforming Growth Factor β Depletion Is the Primary Determinant of Smad Signaling Kinetics." Molecular and Cellular Biology 29, no. 9 (February 17, 2009): 2443–55. http://dx.doi.org/10.1128/mcb.01443-08.

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ABSTRACT A cell's decision to growth arrest, apoptose, or differentiate in response to transforming growth factor β (TGF-β) superfamily ligands depends on the ligand concentration. How cells sense the concentration of extracellular bioavailable TGF-β remains poorly understood. We therefore undertook a systematic quantitative analysis of how TGF-β ligand concentration is transduced into downstream phospho-Smad2 kinetics, and we found that the rate of TGF-β ligand depletion is the principal determinant of Smad signal duration. TGF-β depletion is caused by two mechanisms: (i) cellular uptake of TGF-β by a TGF-β type II receptor-dependent mechanism and (ii) reversible binding of TGF-β to the cell surface. Our results indicate that cells sense TGF-β dose by depleting TGF-β via constitutive TGF-β type II receptor trafficking processes. Our results also have implications for the role of the TGF-β type II receptor in disease, as tumor cells harboring TGF-β type II receptor mutations exhibit impaired TGF-β depletion, which may contribute to the overproduction of TGF-β and a consequently poor prognosis in cancer.
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Jacko, A. M., L. Nan, S. Li, J. Tan, J. Zhao, D. J. Kass, and Y. Zhao. "De-ubiquitinating enzyme, USP11, promotes transforming growth factor β-1 signaling through stabilization of transforming growth factor β receptor II." Cell Death & Disease 7, no. 11 (November 2016): e2474-e2474. http://dx.doi.org/10.1038/cddis.2016.371.

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HALL, Frederick L., Paul D. BENYA, Silvia R. PADILLA, Denise CARBONARO-HALL, Richard WILLIAMS, Sue BUCKLEY, and David WARBURTON. "Transforming growth factor-β type-II receptor signalling: intrinsic/associated casein kinase activity, receptor interactions and functional effects of blocking antibodies." Biochemical Journal 316, no. 1 (May 15, 1996): 303–10. http://dx.doi.org/10.1042/bj3160303.

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The transforming growth factor β (TGF-β) family of growth factors control proliferation, extracellular matrix synthesis and/ or differentiation in a wide variety of cells. However, the molecular mechanisms governing ligand binding, receptor oligomerization and signal transduction remain incompletely understood. In this study, we utilized a set of antibodies selective for the extracellular and intracellular domains of the TGF-β type-II receptor as probes to investigate the intrinsic kinase activity of this receptor and its physical association in multimeric complexes with type-I and type-III receptors. The type-II receptor immunoprecipitated from human osteosarcoma cells exhibited autophosphorylation and casein kinase activity that was markedly stimulated by polylysine yet was insensitive to heparin. Affinity cross-linking of 125I-TGF-β1 ligand to cellular receptors followed by specific immunoprecipitation demonstrated that type-II receptors form stable complexes with both type-I and type-III receptors expressed on the surfaces of both human osteosarcoma cells and rabbit chondrocytes. Pretreatment of the cultured cells with an antibody directed against a distinct extracellular segment of the type-II receptor (anti-TGF-β-IIR-NT) effectively blocked the 125I-TGF-β labelling of type-I receptors without preventing the affinity labelling of type-II or type-III receptors, indicating a selective disruption of the type-I/type-II hetero-oligomers. The anti-TGF-β-IIR-NT antibodies also blocked the TGF-β-dependent induction of the plasminogen activator inhibitor (PAI-1) promoter observed in mink lung epithelial cells. However, the same anti-TGF-β-IIR-NT antibodies did not prevent the characteristic inhibition of cellular proliferation by TGF-β1, as determined by [3H]thymidine incorporation into DNA. The selective perturbation of PAI-1 promoter induction versus cell-cycle-negative regulation suggests that strategic disruption of TGF-β type-I and -II receptor interactions can effectively alter specific cellular responses to TGF-β signalling.
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Bhowmick, Neil A., Roy Zent, Mayshan Ghiassi, Maureen McDonnell, and Harold L. Moses. "Integrin β1Signaling Is Necessary for Transforming Growth Factor-β Activation of p38MAPK and Epithelial Plasticity." Journal of Biological Chemistry 276, no. 50 (October 5, 2001): 46707–13. http://dx.doi.org/10.1074/jbc.m106176200.

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Transforming growth factor-β (TGF-β) can induce epithelial to mesenchymal transdifferentiation (EMT) in mammary epithelial cells. TGF-β-meditated EMT involves the stimulation of a number of signaling pathways by the sequential binding of the type II and type I serine/threonine kinase receptors, respectively. Integrins comprise a family of heterodimeric extracellular matrix receptors that mediate cell adhesion and intracellular signaling, hence making them crucial for EMT progression. In light of substantial evidence indicating TGF-β regulation of various β1integrins and their extracellular matrix ligands, we examined the cross-talk between the TGF-β and integrin signal transduction pathways. Using an inducible system for the expression of a cytoplasmically truncated dominant negative TGF-β type II receptor, we blocked TGF-β-mediated growth inhibition, transcriptional activation, and EMT progression. Dominant negative TGF-β type II receptor expression inhibited TGF-β signaling to the SMAD and AKT pathways, but did not block TGF-β-mediated p38MAPK activation. Interestingly, blocking integrin β1function inhibited TGF-β-mediated p38MAPK activation and EMT progression. Limiting p38MAPK activity through the expression of a dominant negative-p38MAPK also blocked TGF-β-mediated EMT. In summary, TGF-β-mediated p38MAPK activation is dependent on functional integrin β1, and p38MAPK activity is required but is not sufficient to induce EMT.
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Tsuchida, K., K. A. Lewis, L. S. Mathews, and W. W. Vale. "Molecular Characterization of Rat Transforming Growth Factor-β Type II Receptor." Biochemical and Biophysical Research Communications 191, no. 3 (March 1993): 790–95. http://dx.doi.org/10.1006/bbrc.1993.1286.

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Datta, Pran K., and Harold L. Moses. "STRAP and Smad7 Synergize in the Inhibition of Transforming Growth Factor β Signaling." Molecular and Cellular Biology 20, no. 9 (May 1, 2000): 3157–67. http://dx.doi.org/10.1128/mcb.20.9.3157-3167.2000.

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ABSTRACT Smad proteins play a key role in the intracellular signaling of the transforming growth factor β (TGF-β) superfamily of extracellular polypeptides that initiate signaling from the cell surface through serine/threonine kinase receptors. A subclass of Smad proteins, including Smad6 and Smad7, has been shown to function as intracellular antagonists of TGF-β family signaling. We have previously reported the identification of a WD40 repeat protein, STRAP, that associates with both type I and type II TGF-β receptors and that is involved in TGF-β signaling. Here we demonstrate that STRAP synergizes specifically with Smad7, but not with Smad6, in the inhibition of TGF-β-induced transcriptional responses. STRAP does not show cooperation with a C-terminal deletion mutant of Smad7 that does not bind with the receptor and consequently has no inhibitory activity. STRAP associates stably with Smad7, but not with the Smad7 mutant. STRAP recruits Smad7 to the activated type I receptor and forms a complex. Moreover, STRAP stabilizes the association between Smad7 and the activated receptor, thus assisting Smad7 in preventing Smad2 and Smad3 access to the receptor. STRAP interacts with Smad2 and Smad3 but does not cooperate functionally with these Smads to transactivate TGF-β-dependent transcription. The C terminus of STRAP is required for its phosphorylation in vivo, which is dependent on the TGF-β receptor kinases. Thus, we describe a mechanism to explain how STRAP and Smad7 function synergistically to block TGF-β-induced transcriptional activation.
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Fernandez, Tania, Stephanie Amoroso, Shellyann Sharpe, Gary M. Jones, Valery Bliskovski, Alexander Kovalchuk, Lalage M. Wakefield, Seong-Jin Kim, Michael Potter, and John J. Letterio. "Disruption of Transforming Growth Factor β Signaling by a Novel Ligand-dependent Mechanism." Journal of Experimental Medicine 195, no. 10 (May 13, 2002): 1247–55. http://dx.doi.org/10.1084/jem.20011521.

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Transforming growth factor (TGF)-β is the prototype in a family of secreted proteins that act in autocrine and paracrine pathways to regulate cell development and function. Normal cells typically coexpress TGF-β receptors and one or more isoforms of TGF-β, thus the synthesis and secretion of TGF-β as an inactive latent complex is considered an essential step in regula-ting the activity of this pathway. To determine whether intracellular activation of TGF-β results in TGF-β ligand–receptor interactions within the cell, we studied pristane-induced plasma cell tumors (PCTs). We now demonstrate that active TGF-β1 in the PCT binds to intracellular TGF-β type II receptor (TβRII). Disruption of the expression of TGF-β1 by antisense TGF-β1 mRNA restores localization of TβRII at the PCT cell surface, indicating a ligand-induced impediment in receptor trafficking. We also show that retroviral expression of a truncated, dominant-negative TβRII (dnTβRII) effectively competes for intracellular binding of active ligand in the PCT and restores cell surface expression of the endogenous TβRII. Analysis of TGF-β receptor–activated Smad2 suggests the intracellular ligand–receptor complex is not capable of signaling. These data are the first to demonstrate the formation of an intracellular TGF-β–receptor complex, and define a novel mechanism for modulating the TGF-β signaling pathway.
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Dissertations / Theses on the topic "Transforming growth factor β receptor II"

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Abe, Hideharu. "A Vitamin D Analog Regulates Mesangial Cell Smooth Muscle Phenotypes in a Transforming Growth Factor-β Type II Receptor-mediated Manner." Kyoto University, 2001. http://hdl.handle.net/2433/150576.

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許諾条件により本文は公開していません : 本文は「THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol.274, No.30, pp.20874-20878」に掲載
本文データは平成22年度国立国会図書館の学位論文(博士)のデジタル化実施により作成された画像ファイルを基にpdf変換したものである
Kyoto University (京都大学)
0048
新制・課程博士
博士(医学)
甲第8877号
医博第2380号
新制||医||771(附属図書館)
UT51-2001-F207
京都大学大学院医学研究科内科系専攻
(主査)教授 中尾 一和, 教授 小川 修, 教授 北 徹
学位規則第4条第1項該当
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Sharmin, Nahid. "Therapeutic Targeting of BMP and TGF-β Signalling Pathways for the Resolution of Pulmonary Arterial Hypertension." Thesis, University of Bradford, 2018. http://hdl.handle.net/10454/17177.

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Vascular remodelling due to excessive proliferation and apoptosis resistance of pulmonary arterial smooth muscle (PASMCs) and endothelial cells (ECs) has been attributed to the pathogenesis of pulmonary arterial hypertension (PAH). It is an incurable cardiovascular disorder, which leads to right heart failure and death, if left untreated. Heterozygous germline mutations in the bone morphogenetic protein receptor type II (BMPR2) have been linked with the majority (~75%) of the familial form of the disease (HPAH). Mutations in the BMPR2 gene impinge upon the BMP signalling which perturbs the balance between BMP and TGF-β pathways leading to the clinical course of the disease. Current therapies were discovered prior to the knowledge that PAH has substantial genetic components. Hence, this study aims to identify novel therapeutic intervention and provide novel insights into how the dysfunctional BMPRII signalling contributes to the pathogenesis of PAH. This work demonstrates that cryptolepines and FDA approved drugs (doxorubicin, taxol, digitoxin and podophyllotoxin) inhibit the excessive proliferation and induce apoptosis in BMPR2 mutant PASMCs by modulating the BMP and TGF-β pathways. Moreover, established drug PTC124 has also been tested but has failed to promote translational readthrough. I have also shown that dysregulated apoptosis of PASMCs and HPAECs is mediated through the BMPRII-ALK1-BclxL axis. Finally, the siRNA screen targeting approximately 1000 genes has identified novel proteins including PPP1CA, IGF-1R, MPP1, MCM5 and SRC each capable of modulating the BMPRII signalling. Taken together, this study for the very first time has identified novel compounds with pro-BMP and anti-TGFβ activities which may provide therapeutic intervention prior to or after the onset of PAH.
Commonwealth Scholarship Commission in the UK
The full text will be available at the end of the embargo period, 31st July 2024.
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Alyahya, Linda. "Expression of ADAM metalloproteases during transforming growth factor β-induced senescence in breast cancer cells." Thesis, Kansas State University, 2017. http://hdl.handle.net/2097/35375.

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Master of Science
Biochemistry and Molecular Biophysics Interdepartmental Program
Anna Zolkiewska
Cellular senescence is a state of irreversible cell cycle arrest in response to non-lethal stress. In cancer cells, senescence can be induced by chemotherapy, radiation, or signals from the tumor microenvironment, such as transforming growth factor β (TGFβ). Senescent cells are metabolically active and have altered gene expression compared to their non-senescent counterparts. Senescent cells release a wide variety of factors, including extracellular domains of transmembrane proteins that require proteolytic cleavage by specific proteases. ADAMs (A Disintegrin and Metalloprotease domain-containing proteins) are enzymes that cleave many transmembrane proteins, such as growth factor precursors or adhesion molecules, and thus may act as sheddases in senescent cells. Here, we investigate ADAM expression levels during TGFβ- induced cellular senescence. SUM149PT and SUM102PT breast cancer cells were incubated with TGFβ, followed by treatment with high doses of paclitaxel to remove actively proliferating, non-senescent cells. Induction of cellular senescence was examined by evaluating changes in cell size and granularity, and by β-galactosidase staining. ADAM mRNA levels were measured by quantitative reverse transcription polymerase chain reaction (qRT-PCR). Among several ADAMs tested, ADAM12 mRNA was significantly upregulated in senescent cells. In addition, we demonstrated that ADAM12 knock-down leads to decreased activation of epidermal growth factor receptor (EGFR), an important modulator of cancer cell growth, survival, and metastasis. This effect of ADAM12 knock-down was likely due to a diminished release of soluble EGF or EGF-like ligands from cells. Since senescent cells often release increased amounts of these ligands, ADAM12 may modulate the senescence secretome in senescent breast cancer cells.
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Holásková, Ida. "I. Distribution of transforming growth factor beta 1, TGF receptor II and decorin in the sheep uterus shortly after breeding." Morgantown, W. Va. : [West Virginia University Libraries], 2007. https://eidr.wvu.edu/etd/documentdata.eTD?documentid=5373.

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Thesis (Ph. D.)--West Virginia University, 2007.
Title from document title page. Document formatted into pages; contains ix, 144 p. : ill. (some col.). Includes abstract. Includes bibliographical references (p. 126-144).
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Mohan, D. Saravana. "Xenopus Laevis TGF-ß: Cloning And Characterization Of The Signaling Receptors." Thesis, Indian Institute of Science, 2000. http://hdl.handle.net/2005/228.

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The amphibian species Xenopus laevis, along with mouse and chicken is a very important model system, used widely to dissect the molecular intricacies of various aspects of vertebrate development. Study with Xenopus has clear advantages in terms of various technical considerations including the ease of handling early stage of embryos and due to the remarkable documentation of several early molecular events during development. The concept of inductive interactions between various cell types during early development was first revealed by the studies performed in Xenopus, and among the various factors proposed for mesoderm induction, the members of transforming growth factor-β (TGF- β) superfamily have been considered to be the most probable candidates. About forty different members of the TGF-β superfamily have been cloned and characterized from various organisms. The superfamily members like activins and BMPs have been studied extensively with respect to their functional role during development. While BMPs were assigned as candidates for inducing ventral mesoderm, activins oppose the role of BMPs by inducing dorsal mesoderm. Studies that helped in delineating their roles were performed using three approaches that utilized the ligands, receptors or down stream signaling components (Smads). All the three components were studied with respect to their endogenous expression pattern and effects of ectopic expressions of the wild type or dominant negative mutants. These approaches led to the accumulation of evidences supporting the importance of these signaling molecules. All the above mentioned studies were only possible due to the cloning and characterization of cDNAs of the various proteins involved in the signaling pathway including the ligands. TGF-β2 and 5 are the two isoforms of TGF-β cloned from the amphibian system. We have earlier cloned and characterized the promoter for TGF-β5 gene, which suggested possible regulation of this factor by tissue specific transcription factors. Messenger RNA in situ hybridization analysis to study the TGF-β5-expression pattern during Xenopus development, showed spatial and temporal expression pattern. The expression was confined to specific regions that include notochord, somites, and tail bud among others, in the various stages analyzed. This suggested a possible role for TGF-β5 in organogenesis during the amphibian development. To better understand the role of TGF-β in Xenopus development, studies to examine the specific receptor expression pattern for this growth factor is very essential. With the lack of any reports on cloning of TGF-β receptors from this system, the aim of the present study was to isolate and characterize the receptors for TGF-β from Xenopus laevis. PCR cloning using degenerate primers based on the conserved kinase domains of this class of receptors, coupled to library screenings enabled the identification of two novel receptor cDNAs of the TGF-β receptor superfamily. Characterization of the isolated cDNAs suggested that one of them codes for a type II receptor for TGF-β. Further the cDNAs were found to be ubiquitously expressed during development, as judged by RT-PCR analysis. The cloned cDNAs can now be employed as tools, to study the expression pattern by means of mRNA in situ hybridization, on the various developmental stage embryos and to perform studies using antisense and dominant negative mRNA injection experiments in vivo. Such studies will greatly assist in delineating the role of TGF-β ligands and receptors during amphibian development.
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Davies, R. J. "Dysfunctional response to transforming growth factor-beta contribute to the development of familial pulmonary arterial hypertension due to mutations in bone morphogenetic protein type II receptor." Thesis, University of Cambridge, 2010. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.598337.

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TGF-β1 significantly inhibited the growth of human and mouse control cells. Cells harbouring dysfunctional BMPR-11 signalling were resistant to this growth inhibition. Mutant BMPR-11 cells had reduced BMP4 induced Smad 1/5 phosphorylation, reduced transcription of the BRE-luciferase reporter as well as reduced induction of inhibitors of DNA binding gene (Id1, 2 and 4) transcription. However, there was no difference in the level of activation of the TGF-β pathway, either at second messenger or transcriptional level, between control and mutant PASMCs to account for the loss of the growth inhibitory effects of TGF-β in the mutant cells. Microarray data generated from our PASMCs indicated a potential increase in the NFκB signalling pathway in BMPR-11 mutant PASMCs. Immunoblotting revealed increased basal expression of the NFκB signalling subunit, phospho-p65, in mutant cells indicating increased baseline activity of this signalling pathway. ELISA showed increased baseline IL-8 release in the mutant PASMCs compared with controls. Furthermore, incubation of BMPR-11 mutant PASMCs with an IL-8 neutralising antibody re-sensitised the mutant cells to the inhibitory growth effects of TGF-β returning them to the phenotype of control PASMCs. BMPR-11 signalling was also found to be crucial I the control of growth of HPAECs. BMP9 was shown to phosphorylate both Smad 1/5 and Smad 2 via ALK1 in conjunction with ActR-11 and BMPR-11. A reduction in BMPR-11 expression reduced the growth inhibitory effects of BMP9. Inhibition of NFκB signalling, thus normalising TGF-β responses in the setting of FPAH, may be a promising therapeutic target.
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SACCOMANI, Gianmaria. "Expression, purification and crystallization attempts of a functional domain of human transforming growth factor beta receptor II - structural characterization of bile acid-binding proteins (Doctoral Thesis)." Doctoral thesis, 2009. http://hdl.handle.net/11562/337422.

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L’obiettivo di questo lavoro di tesi era quello di determinare la struttura tridimensionale del dominio citoplasmatico del transforming growth factor β receptor II e delle ileal bile acid-binding protein umana e di zebrafish (HiBABP e ZiBABP) attraverso la tecnica di diffrazione di raggi X. L’espressione del TGFBR2 è stata provata utilizzando diversi sistemi di espressione (E. coli, Pichia pastoris, cellule d’insetto transfettate con baculovirus ricombinate e Nicotiana benthamiana) ma è stata ottenuta una piccola quantità di proteina ricombinante solubile. Inoltre è stato utilizzato un metodo di refolding per ottenere la proteina di interesse da corpi di inclusione e in questo caso sono stati trovati due microcristalli nelle prove di cristallizzazione preliminari, ma questi non erano utilizzabili per gli esperimenti di diffrazione di raggi X. Le ileal BABP umana e di zebrafish sono state espresse in E. coli e purificate tramite cromatografia di affinità, sfruttando il tag di sei istidine all’estremità C-terminale delle proteine. La struttura tridimensionale della ZiBABP è stata determinata sia nella sua forma apo sia legata all’acido colico per sostituzione molecolare. La risoluzione era 1.6 Ǻ per la forma apo e 2.2 Ǻ per le due diverse forme cristalline del complesso con l’acido colico. Questa è la prima struttura cristallografica di una Ileal bile acid-binding protein. Nel caso della HiBABP si sono ottenuti dei cristalli in due diverse condizioni di cristallizzazione, ma la loro qualità non ha permesso di procedere con la determinazione della struttura. Comunque sono stati allestiti degli esperimenti di ottimizzazione dei parametri di cristallizzazione per migliorare la qualità dei cristalli. Uno studio recente ha dimostrato la presenza di una variante della HiBABP denominata human ileal bile acid-binding protein long (HiBABP-L), così un altro obiettivo del lavoro di tesi è la determinazione della struttura tridimensionale di questa proteina. La HiBABP-L è stata espressa in E. coli ed al momento sono in corso alcuni tentativi per purificare la proteina di interesse.
The aim of this thesis work was to determine the three-dimensional structure of the cytoplasmatic domain of the transforming growth factor β receptor II, and of zebrafish and human ileal bile acid-binding proteins using the X-ray diffraction technique. The expression of TGFBR2 was attempted using different expression systems (E. coli, Pichia pastoris, insect cells transfected with recombinant baculovirus and Nicotiana benthamiana) but only a low amount of soluble recombinant protein was obtained. A refolding method was used to obtain the soluble protein from inclusion bodies and using the refolded protein two microcrystals were found in the preliminary crystallization trials, but they were not suitable for X-ray diffraction experiments. The optimization trials did not produce better samples than microcrystals. Human ileal bile acid-binding protein (HiBABP) and zebrafish ileal bile acid-binding protein (ZiBABP) were expressed in E. coli and purified by immobilized metal ion affinity chromatography, using the hexa-histidine tag added to the C-terminus of the proteins. The three dimensional structure of ZiBABP was determinated both in its apo-form and bound to cholic acid by the molecular replacement method. The resolution was 1.6 Ǻ for the apo-form and 2.2 Ǻ for the two different crystal forms of the complex with cholate. This is the first crystallographic structure of an Ileal bile acid-binding protein. In the case of HiBABP, crystals were obtained in two different crystallization conditions, but their size and quality did not allow to proceed with the structure determination. Optimization experiments of the crystallization conditions are currently being carried out to improve the quality of those crystals. A recent study has shown the presence of a new variant of HiBABP called Human Ileal bile acid-binding protein long (HiBABP-L) and therefore another goal of this thesis work was to determine the three-dimensional structure of this protein. HiBABP-L was expressed in E. coli and attempts to purify the protein of interest are still in progress.
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Lin, Ching-Yi, and 林靜宜. "Helicobacter pylori Heat Shock Protein 60 Trigger SMAD Signal Pathway by Interacting with Transforming Growth Factor-β receptor II." Thesis, 2008. http://ndltd.ncl.edu.tw/handle/18092904893492487352.

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博士
國立交通大學
生物科技系所
97
Helicobacter pylori have explored multiple mechanisms to evade host immune surveillance for chronic infection. But either of them is restricted by certain bacterial strains containing potential virulent factors, or those immune-restrained functions only limit to some specific immunocytes. However, the long-term persistence of H. pylori suggests a more comprehensive and powerful factor(s) hinds behind to regulate host immune system. Helicobacter pylori heat shock protein 60 (HpHsp60) was previous identified as an adhesion molecule or a potent immunogen. This study aims to study the structure of HpHsp60s and evaluates their functions on host immune responses. Analyzing the structure of HpHsp60 via amino acid blast, circular dichroism and electrophoresis indicated most recombinant HpHsp60s form dimers or tetramers that are quite different than E. coli Hsp60 protein structure. Moreover, a novel property of HpHsp60 was found, which is, by mimicking TGF-β1, HpHsp60 could exert immune regulatory effects. With structural homology to the receptor binding site of TGF-β1, HpHsp60 could interact with TGF-β receptor II, trigger SMAD pathway, and inhibiting the immune functions of THP-1 monocytic cells and peripheral mononuclear cells (PBMCs). Our study provides a new hint that H. pylori may employ Hsp60 to surrender host immunity.
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Kohli, Gurneet. "Investigations of transforming growth factor -ß1 action during zebrafish oocyte maturation and cloning of its type II receptor /." 2005.

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Thesis (M.Sc.)--York University, 2005. Graduate Programme in Biology.
Typescript. Includes bibliographical references (leaves 56-62). Also available on the Internet. MODE OF ACCESS via web browser by entering the following URL: http://gateway.proquest.com/openurl?url%5Fver=Z39.88-2004&res%5Fdat=xri:pqdiss &rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&rft_dat=xri:pqdiss:MR11827
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Lin, Yi-Fan, and 林逸凡. "Extract of Reishi Polysaccharides Regulates Epithelial-Mesenchymal Transitions via the Lipid Rafts-dependent Ubiquitination of Transforming Growth Factor-β Receptor in MDA-MB-231 Breast Cancer Cells." Thesis, 2012. http://ndltd.ncl.edu.tw/handle/59452972963242012772.

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Abstract:
碩士
國立陽明大學
生醫光電研究所
100
Ten leading cause of death in Taiwan, cancer is always at the first of placing, and breast cancer mortality has been rising. One reason of that because the cancer cell will metastasis, then cancer metastasis-related mechanisms be paid great attention more and more in recent years. Epithelial-mesenchymal transition (EMT) is a process that cancer cells become aggressive, and it has been marker of tumor metastasis in recent years. Besides, Transforming growth factor beta 1 (TGF-β1) is one of the important factors that cause EMT. Ganoderma Lucidum (Reishi) is treatment of many diseases in Chinese herbal medicine. Ganoderma lucidum polysaccharides is one of many constituents that have bioactivity which are known in Ganoderma Lucidum . MDA-MB-231 is an invasion human breast cancer cell line. In our study, we conjecture that EMT was affected by EORP because the EMT markers (E-cadherin, γ-catenin, N-cadherin and vimentin) change after we used EORP to treatment MDA-MB-231. We also found the production of TGFβ-RI and TGFβ-RII were down after a treatment of EORP. And the TGFβ-RI and TGFβ-RII was ubiquitination in MDA-MB-231 after a treatment of EORP. In addition, EORP also induced lipid rafts expression that with TGFβ-RI or TGFβ-RII expression. These results showed that EORP regulates EMT via the lipid rafts-dependent ubiquitination of TGFβ-R in MDA-MB-231 Breast Cancer Cells.
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Books on the topic "Transforming growth factor β receptor II"

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Jakowlew, Sonia B., ed. Transforming Growth Factor-β in Cancer Therapy, Volume II. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-293-9.

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Book chapters on the topic "Transforming growth factor β receptor II"

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Naumann, Ulrike, and Michael Weller. "Modulating TGF-β Receptor Signaling: A Novel Approach of Cancer Therapy." In Transforming Growth Factor-β in Cancer Therapy, Volume II, 653–69. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-293-9_39.

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De Crescenzo, Gregory, Heman Chao, John Zwaagstra, Yves Durocher, and Maureen D. O’Connor-McCourt. "Engineering TGF-β Traps: Artificially Dimerized Receptor Ectodomains as High-affinity Blockers of TGF-β Action." In Transforming Growth Factor-β in Cancer Therapy, Volume II, 671–84. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-293-9_40.

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Bandyopadhyay, Abhik, and LuZhe Sun. "Soluble TGF-β Type III Receptor Suppresses Malignant Progression of Human Cancer Cells." In Transforming Growth Factor-β in Cancer Therapy, Volume II, 723–35. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-293-9_44.

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Wang, Guiying Y., Xiaochua H. Hu, Rongmei M. Zhang, Lindsey J. Leach, and Zewei W. Luo. "TGF-β Ligands, TGF-β Receptors, and Lung Cancer." In Transforming Growth Factor-β in Cancer Therapy, Volume II, 79–93. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-293-9_6.

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Suzuki, Eiji, and Steven M. Albelda. "Soluble Type II Transforming Growth Factor-β Receptor Inhibits Tumorigenesis by Augmenting Host Antitumor Immunity." In Transforming Growth Factor-β in Cancer Therapy, Volume II, 697–706. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-293-9_42.

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Ruscetti, Francis, Salem Akel, Maria Birchenall-Roberts, Zhouhong Cao, and Anita B. Roberts. "Smad Signaling in Leukemic Growth and Differentiation: Crosstalk Between Smad and Multiple Pathways Through Activation of the TGF-β Type I Receptor." In Transforming Growth Factor-β in Cancer Therapy, Volume II, 247–61. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-293-9_17.

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Liu, Wei, Chekhau Chua, Zhen Gao, Xiaoli Wu, and Yilin Cao. "Overexpressed Truncated TGF-β Type II Receptor Inhibits Fibrotic Behavior of Keloid Fibroblasts In Vitro and Experimental Scar Formation In Vivo." In Transforming Growth Factor-β in Cancer Therapy, Volume I, 703–21. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-292-2_45.

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Lacher, Markus D., W. Michael Korn, and Rosemary J. Akhurst. "Reversal of EMT by Small-Molecule Inhibitors of TGF-β Type I and II Receptors: Implications for Carcinoma Treatment." In Transforming Growth Factor-β in Cancer Therapy, Volume II, 707–22. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-293-9_43.

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Salajegheh, Ali. "Transforming Growth Factor Beta-Receptor Type II (TGFβR2)." In Angiogenesis in Health, Disease and Malignancy, 339–43. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-28140-7_54.

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Rowley, David R. "Reactive Stroma and Evolution of Tumors: Integration of Transforming Growth Factor-β, Connective Tissue Growth Factor, and Fibroblast Growth Factor-2 Activities." In Transforming Growth Factor-β in Cancer Therapy, Volume II, 475–505. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-293-9_30.

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Conference papers on the topic "Transforming growth factor β receptor II"

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Murari, Catherine, Gillian M. Howell, and Michael G. Brattain. "Abstract B60: Identification of the specific histone deacetylases involved in the silencing of transforming growth factor β receptor II in colon cancer." In Abstracts: AACR Special Conference on Chromatin and Epigenetics in Cancer - June 19-22, 2013; Atlanta, GA. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.cec13-b60.

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Santhekadur, Prasanna K., Rachel Gredler, Maaged Akiel, Paul Dent, Paul B. Fisher, and Devanand Sarkar. "Abstract 2628: The multifunctional protein staphylococcal nuclease domain containing-1 (SND1) promotes migration and invasion of hepatocellular carcinoma (HCC) cells by modulating angiotensin II type 1 receptor (AT1R) and transforming growth factor-β (TGF-β) s." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-2628.

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Ng, Evelyn, and John Di Guglielmo. "Abstract 4593: Analysis of transforming growth factor β receptor trafficking on different signaling transduction pathways." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-4593.

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Rosman, Diana S., Yana Bromberg, Aliyah Weinstein, and Michael Reiss. "Abstract 2118: Phenotypic diversity of disease-associated transforming growth factor-β (TGF-β) type I receptor gene (TGFBR1) mutants." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-2118.

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Pozarska, Agnieszka, Gero Niess, Werner Seeger, and Rory Morty. "A role for the accessory type III transforming growth factor β receptor (Tgfbr3) in lung alveolarisation." In ERS International Congress 2016 abstracts. European Respiratory Society, 2016. http://dx.doi.org/10.1183/13993003.congress-2016.pa4026.

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Park, Jin-hong, Seung-Hee Ryu, Jeong-Yoon Oh, Youn-Joo Yang, and Sang-wook Lee. "Abstract 2494: The protective effect of a novel transforming growth factor-β receptor inhibitor against radiation-induced fibrosis." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-2494.

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Malkoski, Stephen, Timothy Cleaver, Sarah Haeger, Karen Rodriguez, Jessyka Lighthall, Shi-Long Lu, Daniel Merrick, and Xiao-Jing Wang. "Transforming Growth Factor Beta Receptor Type II Deletion Increases The Multiplicity And Growth Of K-RAS Induced Lung Cancers." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a4044.

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Moshkovich, Nellie, Misako Sato, Binwu Tang, Yu-an Yang, Kathleen C. Flanders, Mitsutaka Kadota, Howard Yang, Maxwell P. Lee, and Lalage M. Wakefield. "Abstract 2244: Functional interactions between estrogen-related-receptor β (ESRRB) and transforming growth factor-beta (TGF-β) in the regulation of breast cancer stem cell dynamics." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-2244.

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Babiker, Nusaiba A., Ahmed T. Negmeldin, and Eman M. El-labbad. "In Silico Fragment-Based Drug Design and Molecular Docking of Tranilast Analogues as Potential Inhibitors of Transforming Growth Factor- β Receptor Type 1." In ECMC 2022. Basel Switzerland: MDPI, 2022. http://dx.doi.org/10.3390/ecmc2022-13472.

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Li, Min, Manda Sai Krishnaveni, Changgong Li, Zea Borok, and Parviz Minoo. "Epithelial-Specific Deletion Of Transforming Growth Factor-² (TGF-²) Receptor Type II (T²RII) In The Lung Confers Relative Resistance To Bleomycin Injury." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a3525.

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Reports on the topic "Transforming growth factor β receptor II"

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Forbes, Digna S., and Roby A. Jensen. Mechanisms of Transforming Growth Factor Beta-Receptor II Loss in Breast Neoplasia. Fort Belvoir, VA: Defense Technical Information Center, December 2002. http://dx.doi.org/10.21236/ada420478.

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