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  Time- and compartment-resolved proteome profiling of the extracellular niche in lung injury and repair

Schiller, H. B., Fernandez, I. E., Burgstaller, G., Schaab, C., Scheltema, R. A., Schwarzmayr, T., et al. (2015). Time- and compartment-resolved proteome profiling of the extracellular niche in lung injury and repair. MOLECULAR SYSTEMS BIOLOGY, 11(7): 819. doi:10. 15252 /msb. 20156123.

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 Creators:
Schiller, Herbert B.1, Author              
Fernandez, Isis E.2, Author
Burgstaller, Gerald2, Author
Schaab, Christoph3, Author              
Scheltema, Richard A.1, Author              
Schwarzmayr, Thomas2, Author
Strom, Tim M.2, Author
Eickelberg, Oliver2, Author
Mann, Matthias1, Author              
Affiliations:
1Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              
2external, ou_persistent22              
3Cox, Jürgen / Computational Systems Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_2063284              

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Free keywords: IDIOPATHIC PULMONARY-FIBROSIS; AIRWAY STEM-CELLS; BRANCHING-MORPHOGENESIS; ENDOTHELIAL-CELLS; BASEMENT-MEMBRANE; MATRIX; REGENERATION; QUANTIFICATION; MECHANISMS; EPITHELIUMextracellular matrix; fibrosis; proteomics; regeneration; secretome;
 Abstract: The extracellular matrix (ECM) is a key regulator of tissue morphogenesis and repair. However, its composition and architecture are not well characterized. Here, we monitor remodeling of the extracellular niche in tissue repair in the bleomycin-induced lung injury mouse model. Mass spectrometry quantified 8,366 proteins from total tissue and bronchoalveolar lavage fluid (BALF) over the course of 8 weeks, surveying tissue composition from the onset of inflammation and fibrosis to its full recovery. Combined analysis ofproteome, secretome, and transcriptome highlighted post-transcriptional events during tissue fibrogenesis and defined the composition of airway epithelial lining fluid. To comprehensively characterize the ECM, we developed a quantitative detergent solubility profiling (QDSP) method, which identified Emilin-2 and collagen-XXVIII as novel constituents of the provisional repair matrix. QDSP revealed which secreted proteins interact with the ECM, and showed drastically altered association of morphogens to the insoluble matrix upon injury. Thus, our proteomic systems biology study assigns proteins to tissue compartments and uncovers their dynamic regulation upon lung injury and repair, potentially contributing to the development of anti-fibrotic strategies.

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Language(s): eng - English
 Dates: 2015
 Publication Status: Published online
 Pages: 19
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000358788900006
DOI: 10 . 15252 /msb. 20156123
 Degree: -

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Title: MOLECULAR SYSTEMS BIOLOGY
Source Genre: Journal
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Publ. Info: 111 RIVER ST, HOBOKEN 07030-5774, NJ USA : WILEY-BLACKWELL
Pages: - Volume / Issue: 11 (7) Sequence Number: 819 Start / End Page: - Identifier: ISSN: 1744-4292