Proteomics

Dataset Information

0

Substrate identification of ADAMTS16

ABSTRACT: Secreted and cell-surface proteases are major mediators of extracellular matrix remodelling, but their mechanisms and regulatory impact are poorly understood. We developed a mass spectrometry approach using cell free ECM produced by mouse Balb/c 3T3 cells in vitro to identify fibronectin as a novel substrate of the secreted metalloprotease ADAMTS16. ADAMTS16 cleaves fibronectin between its (I)5 and (I)6 modules, releasing the N-terminal 30kDa heparin-binding domain essential for fibronectin assembly.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human) Mus Musculus (mouse)

TISSUE(S): Permanent Cell Line Cell, Cell Culture, Fibroblast

DISEASE(S): Disease Free

SUBMITTER: Rahel Schnellmann  

LAB HEAD: Suneel S. Apte

PROVIDER: PXD007284 | Pride | 2018-04-23

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
140730mouseMatrix2_ADAMTS16-shsuppl.information_s04.raw Raw
140730mouseMatrix2_AdamTS16-sh-EAsuppl.information_s05.raw Raw
140730mouseMatrix2_vectorsuppl.information_s06.raw Raw
150224_LysC-Tryp_ADAMTS16-sh-EA_s02.raw Raw
150224_LysC-Tryp_ADAMTS16-sh_s01.raw Raw
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Publications

A Selective Extracellular Matrix Proteomics Approach Identifies Fibronectin Proteolysis by A Disintegrin-like and Metalloprotease Domain with Thrombospondin Type 1 Motifs (ADAMTS16) and Its Impact on Spheroid Morphogenesis.

Schnellmann Rahel R   Sack Ragna R   Hess Daniel D   Annis Douglas S DS   Mosher Deane F DF   Apte Suneel S SS   Chiquet-Ehrismann Ruth R  

Molecular & cellular proteomics : MCP 20180418 7

Secreted and cell-surface proteases are major mediators of extracellular matrix (ECM) turnover, but their mechanisms and regulatory impact are poorly understood. We developed a mass spectrometry approach using a cell-free ECM produced <i>in vitro</i> to identify fibronectin (FN) as a novel substrate of the secreted metalloprotease ADAMTS16. ADAMTS16 cleaves FN between its (I)<sub>5</sub> and (I)<sub>6</sub> modules, releasing the N-terminal 30 kDa heparin-binding domain essential for FN self-ass  ...[more]

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