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Biologically-active laminin-111 fragment that modulates the epithelial-to-mesenchymal transition in embryonic stem cells.

The dynamic interplay between the extracellular matrix and embryonic stem cells (ESCs) constitutes one of the key steps in understanding stem cell differentiation in vitro. Here we report a biologically-active laminin-111 fragment generated by matrix metalloproteinase 2 (MMP2) processing, which is h... Full description

Journal Title: Proceedings of the National Academy of Sciences of the United States of America April 22, 2014, Vol.111(16), pp.5908-5913
Main Author: Horejs, Christine-Maria
Other Authors: Serio, Andrea , Purvis, Alan , Gormley, Adam J , Bertazzo, Sergio , Poliniewicz, Anna , Wang, Alex J , Dimaggio, Peter , Hohenester, Erhard , Stevens, Molly M
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1403139111
Link: http://search.proquest.com/docview/1518813223/?pq-origsite=primo
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title: Biologically-active laminin-111 fragment that modulates the epithelial-to-mesenchymal transition in embryonic stem cells.
format: Article
creator:
  • Horejs, Christine-Maria
  • Serio, Andrea
  • Purvis, Alan
  • Gormley, Adam J
  • Bertazzo, Sergio
  • Poliniewicz, Anna
  • Wang, Alex J
  • Dimaggio, Peter
  • Hohenester, Erhard
  • Stevens, Molly M
subjects:
  • Animals–Metabolism
  • Basigin–Metabolism
  • Binding Sites–Cytology
  • Cadherins–Metabolism
  • Cell Adhesion–Genetics
  • Embryonic Stem Cells–Metabolism
  • Epithelial-Mesenchymal Transition–Metabolism
  • Gene Expression Regulation–Metabolism
  • Humans–Metabolism
  • Integrin Alpha3beta1–Metabolism
  • Laminin–Metabolism
  • Matrix Metalloproteinase 2–Metabolism
  • Matrix Metalloproteinase 9–Metabolism
  • Mice–Metabolism
  • Peptide Fragments–Metabolism
  • Protein Binding–Metabolism
  • Signal Transduction–Metabolism
  • Tissue Inhibitor of Metalloproteinase-1–Metabolism
  • Tissue Inhibitor of Metalloproteinase-2–Metabolism
  • Bsg Protein, Mouse
ispartof: Proceedings of the National Academy of Sciences of the United States of America, April 22, 2014, Vol.111(16), pp.5908-5913
description: The dynamic interplay between the extracellular matrix and embryonic stem cells (ESCs) constitutes one of the key steps in understanding stem cell differentiation in vitro. Here we report a biologically-active laminin-111 fragment generated by matrix metalloproteinase 2 (MMP2) processing, which is highly up-regulated during differentiation. We show that the β1-chain-derived fragment interacts via α3β1-integrins, thereby triggering the down-regulation of MMP2 in mouse and human ESCs. Additionally, the expression of MMP9 and E-cadherin is up-regulated in mouse ESCs--key players in the epithelial-to-mesenchymal transition. We also demonstrate that the fragment acts through the α3β1-integrin/extracellular matrix metalloproteinase inducer complex. This study reveals a previously unidentified role of laminin-111 in early stem cell differentiation that goes far beyond basement membrane assembly and a mechanism by which an MMP2-cleaved laminin fragment regulates the expression of E-cadherin, MMP2, and MMP9.
language: eng
source:
identifier: E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1403139111
fulltext: fulltext
issn:
  • 10916490
  • 1091-6490
url: Link


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titleBiologically-active laminin-111 fragment that modulates the epithelial-to-mesenchymal transition in embryonic stem cells.
creatorHorejs, Christine-Maria ; Serio, Andrea ; Purvis, Alan ; Gormley, Adam J ; Bertazzo, Sergio ; Poliniewicz, Anna ; Wang, Alex J ; Dimaggio, Peter ; Hohenester, Erhard ; Stevens, Molly M
contributorHorejs, Christine-Maria (correspondence author) ; Horejs, Christine-Maria (record owner)
ispartofProceedings of the National Academy of Sciences of the United States of America, April 22, 2014, Vol.111(16), pp.5908-5913
identifierE-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1403139111
subjectAnimals–Metabolism ; Basigin–Metabolism ; Binding Sites–Cytology ; Cadherins–Metabolism ; Cell Adhesion–Genetics ; Embryonic Stem Cells–Metabolism ; Epithelial-Mesenchymal Transition–Metabolism ; Gene Expression Regulation–Metabolism ; Humans–Metabolism ; Integrin Alpha3beta1–Metabolism ; Laminin–Metabolism ; Matrix Metalloproteinase 2–Metabolism ; Matrix Metalloproteinase 9–Metabolism ; Mice–Metabolism ; Peptide Fragments–Metabolism ; Protein Binding–Metabolism ; Signal Transduction–Metabolism ; Tissue Inhibitor of Metalloproteinase-1–Metabolism ; Tissue Inhibitor of Metalloproteinase-2–Metabolism ; Bsg Protein, Mouse
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descriptionThe dynamic interplay between the extracellular matrix and embryonic stem cells (ESCs) constitutes one of the key steps in understanding stem cell differentiation in vitro. Here we report a biologically-active laminin-111 fragment generated by matrix metalloproteinase 2 (MMP2) processing, which is highly up-regulated during differentiation. We show that the β1-chain-derived fragment interacts via α3β1-integrins, thereby triggering the down-regulation of MMP2 in mouse and human ESCs. Additionally, the expression of MMP9 and E-cadherin is up-regulated in mouse ESCs--key players in the epithelial-to-mesenchymal transition. We also demonstrate that the fragment acts through the α3β1-integrin/extracellular matrix metalloproteinase inducer complex. This study reveals a previously unidentified role of laminin-111 in early stem cell differentiation that goes far beyond basement membrane assembly and a mechanism by which an MMP2-cleaved laminin fragment regulates the expression of E-cadherin, MMP2, and MMP9.
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titleBiologically-active laminin-111 fragment that modulates the epithelial-to-mesenchymal transition in embryonic stem cells.
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titleBiologically-active laminin-111 fragment that modulates the epithelial-to-mesenchymal transition in embryonic stem cells.
authorHorejs, Christine-Maria ; Serio, Andrea ; Purvis, Alan ; Gormley, Adam J ; Bertazzo, Sergio ; Poliniewicz, Anna ; Wang, Alex J ; Dimaggio, Peter ; Hohenester, Erhard ; Stevens, Molly M
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