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- W2034652230 startingPage "69" @default.
- W2034652230 abstract "MASP-1 is a versatile serine protease that cleaves a number of substrates in human blood. In recent years it became evident that besides playing a crucial role in complement activation MASP-1 also triggers other cascade systems and even cells to mount a more powerful innate immune response. In this review we summarize the latest discoveries about the diverse functions of this multi-faceted protease. Recent studies revealed that among MBL-associated serine proteases, MASP-1 is the one responsible for triggering the lectin pathway via its ability to rapidly autoactivate then cleave MASP-2, and possibly MASP-3. The crystal structure of MASP-1 explains its more relaxed substrate specificity compared to the related complement enzymes. Due to the relaxed specificity, MASP-1 interacts with the coagulation cascade and the kinin generating system, and it can also activate endothelial cells eliciting pro-inflammatory signaling." @default.
- W2034652230 created "2016-06-24" @default.
- W2034652230 creator A5024701852 @default.
- W2034652230 creator A5034766496 @default.
- W2034652230 creator A5051500239 @default.
- W2034652230 creator A5051618397 @default.
- W2034652230 creator A5065944362 @default.
- W2034652230 creator A5022827897 @default.
- W2034652230 date "2014-10-01" @default.
- W2034652230 modified "2023-10-15" @default.
- W2034652230 title "Multiple roles of complement MASP-1 at the interface of innate immune response and coagulation" @default.
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- W2034652230 doi "https://doi.org/10.1016/j.molimm.2014.05.013" @default.
- W2034652230 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24935208" @default.
- W2034652230 hasPublicationYear "2014" @default.
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