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http://purl.uniprot.org/citations/11527969http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11527969http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11527969http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/11527969http://www.w3.org/2000/01/rdf-schema#comment"Mannan-binding lectin (MBL)-associated serine proteases-1 and 2 (MASP-1 and MASP-2) are homologous modular proteases that each interact with MBL, an oligomeric serum lectin involved in innate immunity. To precisely determine their substrate specificity, human MASP-1 and MASP-2, and fragments from their catalytic regions were expressed using a baculovirus/insect cells system. Recombinant MASP-2 displayed a rather wide, C1s-like esterolytic activity, and specifically cleaved complement proteins C2 and C4, with relative efficiencies 3- and 23-fold higher, respectively, than human C1s. MASP-2 also showed very weak C3 cleaving activity. Recombinant MASP-1 had a lower and more restricted esterolytic activity. It showed marginal activity toward C2 and C3, and no activity on C4. The enzymic activity of both MASP-1 and MASP-2 was specifically titrated by C1 inhibitor, and abolished at a 1:1 C1 inhibitor:protease ratio. Taken together with previous findings, these and other data strongly support the hypothesis that MASP-2 is the protease that, in association with MBL, triggers complement activation via the MBL pathway, through combined self-activation and proteolytic properties devoted to C1r and C1s in the C1 complex. In view of the very low activity of MASP-1 on C3 and C2, our data raise questions about the implication of this protease in complement activation."xsd:string
http://purl.uniprot.org/citations/11527969http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m105934200"xsd:string
http://purl.uniprot.org/citations/11527969http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m105934200"xsd:string
http://purl.uniprot.org/citations/11527969http://purl.uniprot.org/core/author"Thielens N.M."xsd:string
http://purl.uniprot.org/citations/11527969http://purl.uniprot.org/core/author"Thielens N.M."xsd:string
http://purl.uniprot.org/citations/11527969http://purl.uniprot.org/core/author"Arlaud G.J."xsd:string
http://purl.uniprot.org/citations/11527969http://purl.uniprot.org/core/author"Arlaud G.J."xsd:string
http://purl.uniprot.org/citations/11527969http://purl.uniprot.org/core/author"Bally I."xsd:string
http://purl.uniprot.org/citations/11527969http://purl.uniprot.org/core/author"Bally I."xsd:string
http://purl.uniprot.org/citations/11527969http://purl.uniprot.org/core/author"Rossi V."xsd:string
http://purl.uniprot.org/citations/11527969http://purl.uniprot.org/core/author"Rossi V."xsd:string
http://purl.uniprot.org/citations/11527969http://purl.uniprot.org/core/author"Jensenius J.C."xsd:string
http://purl.uniprot.org/citations/11527969http://purl.uniprot.org/core/author"Jensenius J.C."xsd:string
http://purl.uniprot.org/citations/11527969http://purl.uniprot.org/core/author"Cseh S."xsd:string
http://purl.uniprot.org/citations/11527969http://purl.uniprot.org/core/author"Cseh S."xsd:string
http://purl.uniprot.org/citations/11527969http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11527969http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11527969http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11527969http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11527969http://purl.uniprot.org/core/pages"40880-40887"xsd:string
http://purl.uniprot.org/citations/11527969http://purl.uniprot.org/core/pages"40880-40887"xsd:string
http://purl.uniprot.org/citations/11527969http://purl.uniprot.org/core/title"Substrate specificities of recombinant mannan-binding lectin-associated serine proteases-1 and -2."xsd:string