Proteomics

Dataset Information

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):

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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