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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Vydáno v:	Molecular systems biology Ročník 9; číslo 1; s. 657 - n/a
Hlavní autoři:	Küttner, Victoria, Mack, Claudia, Rigbolt, Kristoffer TG, Kern, Johannes S, Schilling, Oliver, Busch, Hauke, Bruckner‐Tuderman, Leena, Dengjel, Jörn
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	London Nature Publishing Group UK 16.04.2013 John Wiley & Sons, Ltd EMBO Press Nature Publishing Group Springer Nature
Témata:	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 Germany mass spectrometry primary human fibroblasts extracellular matrix (ECM) MMP14 disease proteomics
ISSN:	1744-4292, 1744-4292
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Shrnutí:	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.
Bibliografie:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23
ISSN:	1744-4292 1744-4292
DOI:	10.1038/msb.2013.17