Novel MASP-2 inhibitors developed via directed evolution of human TFPI1 are potent lectin pathway inhibitors.
MASP-2
complement system
complement-targeted therapy
directed evolution
innate immunity
ischemia
ischemia-reperfusion injury
lectin pathway
phage display
protease inhibitor
serine protease
serine proteinase
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
17 05 2019
17 05 2019
Historique:
received:
06
03
2019
revised:
28
03
2019
pubmed:
7
4
2019
medline:
18
12
2019
entrez:
7
4
2019
Statut:
ppublish
Résumé
The lectin pathway (LP) of the complement system is an important antimicrobial defense mechanism, but it also contributes significantly to ischemia reperfusion injury (IRI) associated with myocardial infarct, stroke, and several other clinical conditions. Mannan-binding lectin-associated serine proteinase 2 (MASP-2) is essential for LP activation, and therefore, it is a potential drug target. We have previously developed the first two generations of MASP-2 inhibitors by
Identifiants
pubmed: 30952698
pii: S0021-9258(20)36375-4
doi: 10.1074/jbc.RA119.008315
pmc: PMC6527154
pii:
doi:
Substances chimiques
Lipoproteins
0
Peptides
0
Serine Proteinase Inhibitors
0
lipoprotein-associated coagulation inhibitor
0
ecallantide
5Q6TZN2HNM
MASP2 protein, human
EC 3.4.21.-
Mannose-Binding Protein-Associated Serine Proteases
EC 3.4.21.-
Masp2 protein, rat
EC 3.4.21.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
8227-8237Informations de copyright
© 2019 Szakács et al.
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