4.7 Article

Mass Spectrometry-Based Atlas of Extracellular Matrix Proteins across 25 Mouse Organs

Journal

JOURNAL OF PROTEOME RESEARCH
Volume 22, Issue 3, Pages 790-801

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/acs.jproteome.2c00526

Keywords

extracellular matrix; matrisome; tandem mass spectrometry; collagen; proteomics; ECM atlas

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The extracellular matrix (ECM) is a critical component of multicellular organisms involved in essential biological processes. By applying an optimized ECM extraction method, the matrisome of 25 organs was analyzed. It was found that tissue matrices are composed of a shared set of ECM proteins, but with varying abundance levels. Network analysis revealed related ECM protein networks across different tissues, including basement membrane and collagen subtypes.
The extracellular matrix (ECM) is a critical non-cellular component of multicellular organisms containing a variety of proteins, glycoproteins, and proteoglycans which have been implicated in a wide variety of essential biological processes, including development, wound healing, and aging. Due to low solubility, many ECM proteins have been underrepresented in previous proteomic datasets. Using an optimized three-step decellularization and ECM extraction method involving chaotrope extraction and digestion via hydroxylamine hydrochloride, we have generated coverage of the matrisome across 25 organs. We observe that the top 100 most abundant proteins from the ECM fractions of all tissues are generally present in all tissues, indicating that tissue matrices are principally composed of a shared set of ECM proteins. However, these proteins vary up to 4000-fold between tissues, resulting in highly unique matrix profiles even with the same primary set of proteins. A data reduction approach was used to reveal related networks of expressed ECM proteins across varying tissues, including basement membrane and collagen subtypes.

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