We are analyzing https://link.springer.com/article/10.1186/bcr1524.

Title:
β3Integrin and Src facilitate transforming growth factor-β mediated induction of epithelial-mesenchymal transition in mammary epithelial cells | Breast Cancer Research
Description:
Introduction Transforming growth factor (TGF)-β suppresses breast cancer formation by preventing cell cycle progression in mammary epithelial cells (MECs). During the course of mammary tumorigenesis, genetic and epigenetic changes negate the cytostatic actions of TGF-β, thus enabling TGF-β to promote the acquisition and development of metastatic phenotypes. The molecular mechanisms underlying this conversion of TGF-β function remain poorly understood but may involve signaling inputs from integrins. Methods β3 Integrin expression or function in MECs was manipulated by retroviral transduction of active or inactive β3 integrins, or by transient transfection of small interfering RNA (siRNA) against β3 integrin. Altered proliferation, invasion, and epithelial-mesenchymal transition (EMT) stimulated by TGF-β in control and β3 integrin manipulated MECs was determined. Src involvement in β3 integrin mediated alterations in TGF-β signaling was assessed by performing Src protein kinase assays, and by interdicting Src function pharmacologically and genetically. Results TGF-β stimulation induced αvβ3 integrin expression in a manner that coincided with EMT in MECs. Introduction of siRNA against β3 integrin blocked its induction by TGF-β and prevented TGF-β stimulation of EMT in MECs. β3 integrin interacted physically with the TGF-β receptor (TβR) type II, thereby enhancing TGF-β stimulation of mitogen-activated protein kinases (MAPKs), and of Smad2/3-mediated gene transcription in MECs. Formation of β3 integrin:TβR-II complexes blocked TGF-β mediated growth arrest and increased TGF-β mediated invasion and EMT. Dual β3 integrin:TβR-II activation induced tyrosine phosphorylation of TβR-II, a phosphotransferase reaction mediated by Src in vitro. Inhibiting Src activity in MECs prevented the ability of β3 integrin to induce TβR-II tyrosine phosphorylation, MAPK activation, and EMT stimulated by TGF-β. Lastly, wild-type and D119A β3 integrin expression enhanced and abolished, respectively, TGF-β stimulation of invasion in human breast cancer cells. Conclusion We show that β3 integrin alters TGF-β signaling in MECs via Src-mediated TβR-II tyrosine phosphorylation, which significantly enhanced the ability of TGF-β to induce EMT and invasion. Our findings suggest that β3 integrin interdiction strategies may represent an innovative approach to re-establishing TGF-β mediated tumor suppression in progressing human breast cancers.
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Keywords {🔍}

tgfβ, integrin, cells, cell, nmumg, expression, emt, pubmed, figure, src, article, google, scholar, tβrii, cas, growth, antibodies, stimulated, invasion, protein, kinase, integrins, ability, expressing, mecs, activation, cancer, signaling, tyrosine, transforming, phosphorylation, stimulation, breast, factor, receptor, mediated, control, response, monitored, ngml, mapk, extracts, epithelial, mec, usa, gfp, biol, subsequently, significantly, smad,

Topics {✒️}

tgf-β family signalling c-jun amino-terminal kinase anti-β-actin antibodies served transforming growth factor-β transforming growth factor-β1 carboxyl-terminally tag c-src fluorescence-activated cell sorting mitogen-activated protein kinase smad2/3-mediated gene transcription src-mediated tyrosine phosphorylation 4α-phorbol 12-myristate 13-acetate integrin-mediated cell adhesion arginine-glycine-aspartic acid fluorescence-activated cell sorter extracellular signal-regulated kinase article download pdf tgf-β mediated cytostasis β3integrin expression increases anti-tβr-ii antibodies showed anti-human β3 integrin mitogen-activated protein kinases bi-cistronic retroviral transduction dual-specificity protein kinase β3 integrin-mediated recruitment inhibit epithelial-mesenchymal transition epithelial-mesenchymal cell transition tgf-β induces emt mutant c-src cdnas fak integrates growth-factor transforming growth factor transforming growth factor anti-β3 integrin antibodies integrin β1-mediated invasion enhanced tgf-β stimulation induce growth arrest pcmv-β-gal cdnas integrin signalling prevented tgf-β stimulation gfp-expressing nmumg cells tgfβ-mediated fibroblastic transdifferentiation tgf-β targeted promoters tβr-ii tyrosine phosphorylation anti-β1 integrin antibodies anti-β-actin antibodies tgf-β signaling system tgf-β receptor complexes tgf-β mediated emt stimulate epithelial-mesenchymal transitions tgf-β receptor tβr anti-αvβ3 lm609 antibody

Questions {❓}

Lee JO, Bankston LA, Arnaout MA, Liddington RC: Two conformations of the integrin A-domain (I-domain): a pathway for activation?

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WebPage:
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         headline:β3Integrin and Src facilitate transforming growth factor-β mediated induction of epithelial-mesenchymal transition in mammary epithelial cells
         description:Transforming growth factor (TGF)-β suppresses breast cancer formation by preventing cell cycle progression in mammary epithelial cells (MECs). During the course of mammary tumorigenesis, genetic and epigenetic changes negate the cytostatic actions of TGF-β, thus enabling TGF-β to promote the acquisition and development of metastatic phenotypes. The molecular mechanisms underlying this conversion of TGF-β function remain poorly understood but may involve signaling inputs from integrins. β3 Integrin expression or function in MECs was manipulated by retroviral transduction of active or inactive β3 integrins, or by transient transfection of small interfering RNA (siRNA) against β3 integrin. Altered proliferation, invasion, and epithelial-mesenchymal transition (EMT) stimulated by TGF-β in control and β3 integrin manipulated MECs was determined. Src involvement in β3 integrin mediated alterations in TGF-β signaling was assessed by performing Src protein kinase assays, and by interdicting Src function pharmacologically and genetically. TGF-β stimulation induced αvβ3 integrin expression in a manner that coincided with EMT in MECs. Introduction of siRNA against β3 integrin blocked its induction by TGF-β and prevented TGF-β stimulation of EMT in MECs. β3 integrin interacted physically with the TGF-β receptor (TβR) type II, thereby enhancing TGF-β stimulation of mitogen-activated protein kinases (MAPKs), and of Smad2/3-mediated gene transcription in MECs. Formation of β3 integrin:TβR-II complexes blocked TGF-β mediated growth arrest and increased TGF-β mediated invasion and EMT. Dual β3 integrin:TβR-II activation induced tyrosine phosphorylation of TβR-II, a phosphotransferase reaction mediated by Src in vitro. Inhibiting Src activity in MECs prevented the ability of β3 integrin to induce TβR-II tyrosine phosphorylation, MAPK activation, and EMT stimulated by TGF-β. Lastly, wild-type and D119A β3 integrin expression enhanced and abolished, respectively, TGF-β stimulation of invasion in human breast cancer cells. We show that β3 integrin alters TGF-β signaling in MECs via Src-mediated TβR-II tyrosine phosphorylation, which significantly enhanced the ability of TGF-β to induce EMT and invasion. Our findings suggest that β3 integrin interdiction strategies may represent an innovative approach to re-establishing TGF-β mediated tumor suppression in progressing human breast cancers.
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            Focal Adhesion Kinase
            Mammary Epithelial Cell
            Integrin Expression
            NMuMG Cell
            Cancer Research
            Oncology
            Surgical Oncology
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      headline:β3Integrin and Src facilitate transforming growth factor-β mediated induction of epithelial-mesenchymal transition in mammary epithelial cells
      description:Transforming growth factor (TGF)-β suppresses breast cancer formation by preventing cell cycle progression in mammary epithelial cells (MECs). During the course of mammary tumorigenesis, genetic and epigenetic changes negate the cytostatic actions of TGF-β, thus enabling TGF-β to promote the acquisition and development of metastatic phenotypes. The molecular mechanisms underlying this conversion of TGF-β function remain poorly understood but may involve signaling inputs from integrins. β3 Integrin expression or function in MECs was manipulated by retroviral transduction of active or inactive β3 integrins, or by transient transfection of small interfering RNA (siRNA) against β3 integrin. Altered proliferation, invasion, and epithelial-mesenchymal transition (EMT) stimulated by TGF-β in control and β3 integrin manipulated MECs was determined. Src involvement in β3 integrin mediated alterations in TGF-β signaling was assessed by performing Src protein kinase assays, and by interdicting Src function pharmacologically and genetically. TGF-β stimulation induced αvβ3 integrin expression in a manner that coincided with EMT in MECs. Introduction of siRNA against β3 integrin blocked its induction by TGF-β and prevented TGF-β stimulation of EMT in MECs. β3 integrin interacted physically with the TGF-β receptor (TβR) type II, thereby enhancing TGF-β stimulation of mitogen-activated protein kinases (MAPKs), and of Smad2/3-mediated gene transcription in MECs. Formation of β3 integrin:TβR-II complexes blocked TGF-β mediated growth arrest and increased TGF-β mediated invasion and EMT. Dual β3 integrin:TβR-II activation induced tyrosine phosphorylation of TβR-II, a phosphotransferase reaction mediated by Src in vitro. Inhibiting Src activity in MECs prevented the ability of β3 integrin to induce TβR-II tyrosine phosphorylation, MAPK activation, and EMT stimulated by TGF-β. Lastly, wild-type and D119A β3 integrin expression enhanced and abolished, respectively, TGF-β stimulation of invasion in human breast cancer cells. We show that β3 integrin alters TGF-β signaling in MECs via Src-mediated TβR-II tyrosine phosphorylation, which significantly enhanced the ability of TGF-β to induce EMT and invasion. Our findings suggest that β3 integrin interdiction strategies may represent an innovative approach to re-establishing TGF-β mediated tumor suppression in progressing human breast cancers.
      datePublished:2006-07-19T00:00:00Z
      dateModified:2006-07-19T00:00:00Z
      pageStart:1
      pageEnd:16
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      keywords:
         Integrin
         Focal Adhesion Kinase
         Mammary Epithelial Cell
         Integrin Expression
         NMuMG Cell
         Cancer Research
         Oncology
         Surgical Oncology
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