Dataset Information

TFMI-3 plasma pull-down - MASP-3 is the exclusive pro-factor D activator in resting blood: the lectin and the alternative complement pathways are fundamentally linked

ABSTRACT: MASP-3 is the third protease of the lectin pathway of the complement system, but its biological function has remained obscure. To elucidate its role in complement activation, we developed a specific MASP-3 inhibitor (named TFMI-3). In this work we unambiguously demonstrate that MASP-3 acts as the exclusive pro-FD activator in resting blood.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Plasma

SUBMITTER: Elod Kortvely

LAB HEAD: Marius Ueffing

PROVIDER: PXD003666 | Pride | 2016-08-24

REPOSITORIES: Pride

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			Action	DRS
	ELK2044-S02-A-1.raw	Raw
	ELK2044-S02-A-1.raw (F005223).mzid_ELK2044-S02-A-1.raw_(F005223).pride.mgf.gz	Mzid
	ELK2044-S02-A-1.raw (F005223).pride.mztab.gz	Mztab
	ELK2044-S02-A-1.rawF005223.mzid.gz	Mzid
	ELK2044-S02-A-1.rawF005223.mzid_ELK2044-S02-A-1.raw_F005223.MGF	Mzid

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Publications

MASP-3 is the exclusive pro-factor D activator in resting blood: the lectin and the alternative complement pathways are fundamentally linked.

Dobó József J Szakács Dávid D Oroszlán Gábor G Kortvely Elod E Kiss Bence B Boros Eszter E Szász Róbert R Závodszky Péter P Gál Péter P Pál Gábor G

Scientific reports 20160818

MASP-3 was discovered 15 years ago as the third mannan-binding lectin (MBL)-associated serine protease of the complement lectin pathway. Lacking any verified substrate its role remained ambiguous. MASP-3 was shown to compete with a key lectin pathway enzyme MASP-2 for MBL binding, and was therefore considered to be a negative complement regulator. Later, knock-out mice experiments suggested that MASP-1 and/or MASP-3 play important roles in complement pro-factor D (pro-FD) maturation. However, st ...[more]

PMID: 27535802

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