Global remodelling of cellular microenvironment due to loss of collagen VII
The mammalian cellular microenvironment is shaped by soluble factors and structural components, the extracellular matrix, providing physical support, regulating adhesion and signalling. A global, quantitative mass spectrometry strategy, combined with bioinformatics data processing, was developed to...
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| Published in: | Molecular systems biology Vol. 9; no. 1; pp. 657 - n/a |
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| Main Authors: | , , , , , , , |
| Format: | Journal Article |
| Language: | English |
| Published: |
London
Nature Publishing Group UK
16.04.2013
John Wiley & Sons, Ltd EMBO Press Nature Publishing Group Springer Nature |
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| ISSN: | 1744-4292, 1744-4292 |
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| Abstract | The mammalian cellular microenvironment is shaped by soluble factors and structural components, the extracellular matrix, providing physical support, regulating adhesion and signalling. A global, quantitative mass spectrometry strategy, combined with bioinformatics data processing, was developed to assess proteome differences in the microenvironment of primary human fibroblasts. We studied secreted proteins of fibroblasts from normal and pathologically altered skin and their post‐translational modifications. The influence of collagen VII, an important structural component, which is lost in genetic skin fragility, was used as model. Loss of collagen VII had a global impact on the cellular microenvironment and was associated with proteome alterations highly relevant for disease pathogenesis including decrease in basement membrane components, increase in dermal matrix proteins, TGF‐β and metalloproteases, but not higher protease activity. The definition of the proteome of fibroblast microenvironment and its plasticity in health and disease identified novel disease mechanisms and potential targets of intervention.
Loss of collagen VII causes recessive dystrophic
epidermolysis bullosa
. Quantitative proteomics analysis of the extracellular matrix and secretome of human fibroblasts derived from pathologically altered skin reveals a global remodelling of the cellular microenvironment.
Synopsis
Loss of collagen VII causes recessive dystrophic
epidermolysis bullosa
. Quantitative proteomics analysis of the extracellular matrix and secretome of human fibroblasts derived from pathologically altered skin reveals a global remodelling of the cellular microenvironment.
A global analysis of the microenvironment of human skin fibroblasts was carried out to reveal disease‐related alterations in the extracellular proteome.
The loss of collagen VII causes a deregulation of the basement membrane and dermal matrix proteome.
Post‐translational modifications of secreted proteins were altered in fibroblasts from recessive dystrophic
epidermolysis bullosa
samples.
Metalloproteases displayed reduced activity and turnover in collagen VII‐deficient cells. |
|---|---|
| AbstractList | The mammalian cellular microenvironment is shaped by soluble factors and structural components, the extracellular matrix, providing physical support, regulating adhesion and signalling. A global, quantitative mass spectrometry strategy, combined with bioinformatics data processing, was developed to assess proteome differences in the microenvironment of primary human fibroblasts. We studied secreted proteins of fibroblasts from normal and pathologically altered skin and their post‐translational modifications. The influence of collagen VII, an important structural component, which is lost in genetic skin fragility, was used as model. Loss of collagen VII had a global impact on the cellular microenvironment and was associated with proteome alterations highly relevant for disease pathogenesis including decrease in basement membrane components, increase in dermal matrix proteins, TGF‐β and metalloproteases, but not higher protease activity. The definition of the proteome of fibroblast microenvironment and its plasticity in health and disease identified novel disease mechanisms and potential targets of intervention.
Loss of collagen VII causes recessive dystrophic
epidermolysis bullosa
. Quantitative proteomics analysis of the extracellular matrix and secretome of human fibroblasts derived from pathologically altered skin reveals a global remodelling of the cellular microenvironment.
Loss of collagen VII causes recessive dystrophic
epidermolysis bullosa
. Quantitative proteomics analysis of the extracellular matrix and secretome of human fibroblasts derived from pathologically altered skin reveals a global remodelling of the cellular microenvironment.
image
A global analysis of the microenvironment of human skin fibroblasts was carried out to reveal disease‐related alterations in the extracellular proteome.
The loss of collagen VII causes a deregulation of the basement membrane and dermal matrix proteome.
Post‐translational modifications of secreted proteins were altered in fibroblasts from recessive dystrophic
epidermolysis bullosa
samples.
Metalloproteases displayed reduced activity and turnover in collagen VII‐deficient cells. Loss of collagen VII causes recessive dystrophic epidermolysis bullosa. Quantitative proteomics analysis of the extracellular matrix and secretome of human fibroblasts derived from pathologically altered skin reveals a global remodelling of the cellular microenvironment. A global analysis of the microenvironment of human skin fibroblasts was carried out to reveal disease-related alterations in the extracellular proteome. The loss of collagen VII causes a deregulation of the basement membrane and dermal matrix proteome. Post-translational modifications of secreted proteins were altered in fibroblasts from recessive dystrophic epidermolysis bullosa samples. Metalloproteases displayed reduced activity and turnover in collagen VII-deficient cells. The mammalian cellular microenvironment is shaped by soluble factors and structural components, the extracellular matrix, providing physical support, regulating adhesion and signalling. A global, quantitative mass spectrometry strategy, combined with bioinformatics data processing, was developed to assess proteome differences in the microenvironment of primary human fibroblasts. We studied secreted proteins of fibroblasts from normal and pathologically altered skin and their post-translational modifications. The influence of collagen VII, an important structural component, which is lost in genetic skin fragility, was used as model. Loss of collagen VII had a global impact on the cellular microenvironment and was associated with proteome alterations highly relevant for disease pathogenesis including decrease in basement membrane components, increase in dermal matrix proteins, TGF-β and metalloproteases, but not higher protease activity. The definition of the proteome of fibroblast microenvironment and its plasticity in health and disease identified novel disease mechanisms and potential targets of intervention. The mammalian cellular microenvironment is shaped by soluble factors and structural components, the extracellular matrix, providing physical support, regulating adhesion and signalling. A global, quantitative mass spectrometry strategy, combined with bioinformatics data processing, was developed to assess proteome differences in the microenvironment of primary human fibroblasts. We studied secreted proteins of fibroblasts from normal and pathologically altered skin and their post‐translational modifications. The influence of collagen VII, an important structural component, which is lost in genetic skin fragility, was used as model. Loss of collagen VII had a global impact on the cellular microenvironment and was associated with proteome alterations highly relevant for disease pathogenesis including decrease in basement membrane components, increase in dermal matrix proteins, TGF‐β and metalloproteases, but not higher protease activity. The definition of the proteome of fibroblast microenvironment and its plasticity in health and disease identified novel disease mechanisms and potential targets of intervention. Loss of collagen VII causes recessive dystrophic epidermolysis bullosa . Quantitative proteomics analysis of the extracellular matrix and secretome of human fibroblasts derived from pathologically altered skin reveals a global remodelling of the cellular microenvironment. Synopsis Loss of collagen VII causes recessive dystrophic epidermolysis bullosa . Quantitative proteomics analysis of the extracellular matrix and secretome of human fibroblasts derived from pathologically altered skin reveals a global remodelling of the cellular microenvironment. A global analysis of the microenvironment of human skin fibroblasts was carried out to reveal disease‐related alterations in the extracellular proteome. The loss of collagen VII causes a deregulation of the basement membrane and dermal matrix proteome. Post‐translational modifications of secreted proteins were altered in fibroblasts from recessive dystrophic epidermolysis bullosa samples. Metalloproteases displayed reduced activity and turnover in collagen VII‐deficient cells. The mammalian cellular microenvironment is shaped by soluble factors and structural components, the extracellular matrix, providing physical support, regulating adhesion and signalling. A global, quantitative mass spectrometry strategy, combined with bioinformatics data processing, was developed to assess proteome differences in the microenvironment of primary human fibroblasts. We studied secreted proteins of fibroblasts from normal and pathologically altered skin and their post‐translational modifications. The influence of collagen VII, an important structural component, which is lost in genetic skin fragility, was used as model. Loss of collagen VII had a global impact on the cellular microenvironment and was associated with proteome alterations highly relevant for disease pathogenesis including decrease in basement membrane components, increase in dermal matrix proteins, TGF‐β and metalloproteases, but not higher protease activity. The definition of the proteome of fibroblast microenvironment and its plasticity in health and disease identified novel disease mechanisms and potential targets of intervention. Loss of collagen VII causes recessive dystrophic epidermolysis bullosa. Quantitative proteomics analysis of the extracellular matrix and secretome of human fibroblasts derived from pathologically altered skin reveals a global remodelling of the cellular microenvironment. Synopsis Loss of collagen VII causes recessive dystrophic epidermolysis bullosa. Quantitative proteomics analysis of the extracellular matrix and secretome of human fibroblasts derived from pathologically altered skin reveals a global remodelling of the cellular microenvironment. A global analysis of the microenvironment of human skin fibroblasts was carried out to reveal disease‐related alterations in the extracellular proteome. The loss of collagen VII causes a deregulation of the basement membrane and dermal matrix proteome. Post‐translational modifications of secreted proteins were altered in fibroblasts from recessive dystrophic epidermolysis bullosa samples. Metalloproteases displayed reduced activity and turnover in collagen VII‐deficient cells. The mammalian cellular microenvironment is shaped by soluble factors and structural components, the extracellular matrix, providing physical support, regulating adhesion and signalling. A global, quantitative mass spectrometry strategy, combined with bioinformatics data processing, was developed to assess proteome differences in the microenvironment of primary human fibroblasts. We studied secreted proteins of fibroblasts from normal and pathologically altered skin and their post-translational modifications. The influence of collagen VII, an important structural component, which is lost in genetic skin fragility, was used as model. Loss of collagen VII had a global impact on the cellular microenvironment and was associated with proteome alterations highly relevant for disease pathogenesis including decrease in basement membrane components, increase in dermal matrix proteins, TGF-β and metalloproteases, but not higher protease activity. The definition of the proteome of fibroblast microenvironment and its plasticity in health and disease identified novel disease mechanisms and potential targets of intervention. The mammalian cellular microenvironment is shaped by soluble factors and structural components, the extracellular matrix, providing physical support, regulating adhesion and signalling. A global, quantitative mass spectrometry strategy, combined with bioinformatics data processing, was developed to assess proteome differences in the microenvironment of primary human fibroblasts. We studied secreted proteins of fibroblasts from normal and pathologically altered skin and their post-translational modifications. The influence of collagen VII, an important structural component, which is lost in genetic skin fragility, was used as model. Loss of collagen VII had a global impact on the cellular microenvironment and was associated with proteome alterations highly relevant for disease pathogenesis including decrease in basement membrane components, increase in dermal matrix proteins, TGF-β and metalloproteases, but not higher protease activity. The definition of the proteome of fibroblast microenvironment and its plasticity in health and disease identified novel disease mechanisms and potential targets of intervention.The mammalian cellular microenvironment is shaped by soluble factors and structural components, the extracellular matrix, providing physical support, regulating adhesion and signalling. A global, quantitative mass spectrometry strategy, combined with bioinformatics data processing, was developed to assess proteome differences in the microenvironment of primary human fibroblasts. We studied secreted proteins of fibroblasts from normal and pathologically altered skin and their post-translational modifications. The influence of collagen VII, an important structural component, which is lost in genetic skin fragility, was used as model. Loss of collagen VII had a global impact on the cellular microenvironment and was associated with proteome alterations highly relevant for disease pathogenesis including decrease in basement membrane components, increase in dermal matrix proteins, TGF-β and metalloproteases, but not higher protease activity. The definition of the proteome of fibroblast microenvironment and its plasticity in health and disease identified novel disease mechanisms and potential targets of intervention. Abstract The mammalian cellular microenvironment is shaped by soluble factors and structural components, the extracellular matrix, providing physical support, regulating adhesion and signalling. A global, quantitative mass spectrometry strategy, combined with bioinformatics data processing, was developed to assess proteome differences in the microenvironment of primary human fibroblasts. We studied secreted proteins of fibroblasts from normal and pathologically altered skin and their post‐translational modifications. The influence of collagen VII, an important structural component, which is lost in genetic skin fragility, was used as model. Loss of collagen VII had a global impact on the cellular microenvironment and was associated with proteome alterations highly relevant for disease pathogenesis including decrease in basement membrane components, increase in dermal matrix proteins, TGF‐β and metalloproteases, but not higher protease activity. The definition of the proteome of fibroblast microenvironment and its plasticity in health and disease identified novel disease mechanisms and potential targets of intervention. |
| Author | Mack, Claudia Dengjel, Jörn Kern, Johannes S Rigbolt, Kristoffer TG Küttner, Victoria Schilling, Oliver Bruckner‐Tuderman, Leena Busch, Hauke |
| Author_xml | – sequence: 1 givenname: Victoria surname: Küttner fullname: Küttner, Victoria organization: School of Life Science‐LifeNet, Freiburg Institute for Advanced Studies (FRIAS), University of Freiburg, ZBSA Center for Biological Systems Analysis, University of Freiburg, Department of Dermatology, University Freiburg Medical Center, Faculty of Biology, University of Freiburg – sequence: 2 givenname: Claudia surname: Mack fullname: Mack, Claudia organization: Department of Dermatology, University Freiburg Medical Center – sequence: 3 givenname: Kristoffer TG surname: Rigbolt fullname: Rigbolt, Kristoffer TG organization: School of Life Science‐LifeNet, Freiburg Institute for Advanced Studies (FRIAS), University of Freiburg, ZBSA Center for Biological Systems Analysis, University of Freiburg – sequence: 4 givenname: Johannes S surname: Kern fullname: Kern, Johannes S organization: Department of Dermatology, University Freiburg Medical Center – sequence: 5 givenname: Oliver surname: Schilling fullname: Schilling, Oliver organization: Institute for Molecular Medicine and Cell Research, University of Freiburg, BIOSS Centre for Biological Signalling Studies, University of Freiburg – sequence: 6 givenname: Hauke surname: Busch fullname: Busch, Hauke organization: School of Life Science‐LifeNet, Freiburg Institute for Advanced Studies (FRIAS), University of Freiburg, ZBSA Center for Biological Systems Analysis, University of Freiburg, Institute for Molecular Medicine and Cell Research, University of Freiburg – sequence: 7 givenname: Leena surname: Bruckner‐Tuderman fullname: Bruckner‐Tuderman, Leena email: bruckner-tuderman@uniklinik-freiburg.de organization: School of Life Science‐LifeNet, Freiburg Institute for Advanced Studies (FRIAS), University of Freiburg, ZBSA Center for Biological Systems Analysis, University of Freiburg, Department of Dermatology, University Freiburg Medical Center, BIOSS Centre for Biological Signalling Studies, University of Freiburg, School of Life Science‐LifeNet, Freiburg Institute for Advanced Studies (FRIAS), University of Freiburg – sequence: 8 givenname: Jörn surname: Dengjel fullname: Dengjel, Jörn email: joern.dengjel@frias.uni-freiburg.de organization: School of Life Science‐LifeNet, Freiburg Institute for Advanced Studies (FRIAS), University of Freiburg, ZBSA Center for Biological Systems Analysis, University of Freiburg, BIOSS Centre for Biological Signalling Studies, University of Freiburg, School of Life Science‐LifeNet, Freiburg Institute for Advanced Studies (FRIAS), University of Freiburg |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/23591773$$D View this record in MEDLINE/PubMed |
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| Keywords | mass spectrometry primary human fibroblasts extracellular matrix (ECM) MMP14 disease proteomics |
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| SubjectTerms | Basement Membrane - metabolism Basement Membrane - pathology Bioinformatics Case-Control Studies Cell adhesion & migration Cell Communication Cellular Microenvironment - genetics Cellular structure Collagen Collagen Type VII - deficiency Collagen Type VII - genetics Data processing Dermis - metabolism Dermis - pathology disease proteomics EMBO24 EMBO31 Epidermolysis Bullosa Dystrophica - genetics Epidermolysis Bullosa Dystrophica - metabolism Epidermolysis Bullosa Dystrophica - pathology Extracellular matrix extracellular matrix (ECM) Extracellular Matrix - genetics Extracellular Matrix - pathology Female Fibroblasts Fibroblasts - metabolism Fibroblasts - pathology Fragility Gene Expression Grants Growth factors Humans Infant Infant, Newborn Male Mass spectrometry Mass spectroscopy Metalloproteases - genetics Metalloproteases - metabolism MMP14 Mutation Pathogenesis Primary Cell Culture primary human fibroblasts Protein Processing, Post-Translational Proteins Proteomes Proteomics Signal transduction Skin Transforming Growth Factor beta - genetics Transforming Growth Factor beta - metabolism |
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| Title | Global remodelling of cellular microenvironment due to loss of collagen VII |
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