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PNPs N-terminomics - Determination of the substrate repertoire of ADAMTS2, 3, and 14 significantly broadens their functions and identifies extracellular matrix organization and TGF-β signaling as primary targets

ABSTRACT: N-terminomics (iTRAQ-TAILS) applied to the ADAMTS2, 3 and 14.

INSTRUMENT(S): QSTAR, Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Fibroblast

SUBMITTER: Mourad Bekhouche

LAB HEAD: Alain Colige

PROVIDER: PXD002354 | Pride | 2016-01-12

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	TS14_F1.dat-pride.pride.mgf.gz	Mgf
	TS14_F1.dat-pride.pride.mztab.gz	Mztab
	TS14_F1.dat-pride.xml.gz	Xml
	TS14_F1.raw	Raw
	TS14_F2.dat-pride.pride.mgf.gz	Mgf

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Publications

Determination of the substrate repertoire of ADAMTS2, 3, and 14 significantly broadens their functions and identifies extracellular matrix organization and TGF-β signaling as primary targets.

Bekhouche Mourad M Leduc Cedric C Dupont Laura L Janssen Lauriane L Delolme Frederic F Vadon-Le Goff Sandrine S Smargiasso Nicolas N Baiwir Dominique D Mazzucchelli Gabriel G Zanella-Cleon Isabelle I Dubail Johanne J De Pauw Edwin E Nusgens Betty B Hulmes David J S DJ Moali Catherine C Colige Alain A

FASEB journal : official publication of the Federation of American Societies for Experimental Biology 20160106 5

A disintegrin and metalloproteinase with thrombospondin type I motif (ADAMTS)2, 3, and 14 are collectively named procollagen N-proteinases (pNPs) because of their specific ability to cleave the aminopropeptide of fibrillar procollagens. Several reports also indicate that they could be involved in other biological processes, such as blood coagulation, development, and male fertility, but the potential substrates associated with these activities remain unknown. Using the recently described N-termi ...[more]

PMID: 26740262

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