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BMP1/Tolloid-like substrates by iTRAQ degradomics

ABSTRACT: In this study, we used an iTRAQ-based quantitative proteomic approach to reveal the release of proteolytic fragments from the cell surface or the ECM by BMP-1. Thirty-seven extracellular proteins were found in significantly higher or lower amounts in the conditioned medium of HT1080 cells overexpressing BMP-1 and thus, could be considered as candidate substrates. Strikingly, three of these new candidates (betaglycan, CD109 and neuropilin-1) were TGF-Beta co-receptors, also acting as antagonists when released from the cell surface, and were chosen for further substrate validation.

INSTRUMENT(S): QSTAR

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Fibroblast

SUBMITTER: Frederic DELOLME

LAB HEAD: Frederic Delolme

PROVIDER: PXD000786 | Pride | 2014-09-29

REPOSITORIES: Pride

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Publications

Proteolytic control of TGF-β co-receptor activity by BMP-1/tolloid-like proteases revealed by quantitative iTRAQ proteomics.

Delolme Frédéric F Anastasi Cyril C Alcaraz Lindsay B LB Mendoza Valentin V Vadon-Le Goff Sandrine S Talantikite Maya M Capomaccio Robin R Mevaere Jimmy J Fortin Laëtitia L Mazzocut Dominique D Damour Odile O Zanella-Cléon Isabelle I Hulmes David J S DJ Overall Christopher M CM Valcourt Ulrich U Lopez-Casillas Fernando F Moali Catherine C

Cellular and molecular life sciences : CMLS 20140927 5

The metalloproteinase BMP-1 (bone morphogenetic protein-1) plays a major role in the control of extracellular matrix (ECM) assembly and growth factor activation. Most of the growth factors activated by BMP-1 are members of the TGF-β superfamily known to regulate multiple biological processes including embryonic development, wound healing, inflammation and tumor progression. In this study, we used an iTRAQ (isobaric tags for relative and absolute quantification)-based quantitative proteomic appro ...[more]

PMID: 25260970

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