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- W2024249553 endingPage "295" @default.
- W2024249553 startingPage "284" @default.
- W2024249553 abstract "Elafin and SLPI are low-molecular weight proteins that were first identified as protease inhibitors in mucous fluids including lung secretions, where they help control excessive proteolysis due to neutrophil serine proteases (elastase, proteinase 3 and cathepsin G). Elafin and SLPI are structurally related in that both have a fold with a four-disulfide core or whey acidic protein (WAP) domain responsible for inhibiting proteases. Elafin is derived from a precursor, trappin-2 or pre-elafin, by proteolysis. Trappin-2, which is itself a protease inhibitor, has a unique N-terminal domain that enables it to become cross-linked to extracellular matrix proteins by transglutaminase(s). SLPI and elafin/trappin-2 are attractive candidates as therapeutic molecules for inhibiting neutrophil serine proteases in inflammatory lung diseases. Hence, they have become the WAP proteins most studied over the last decade. This review focuses on recent findings revealing that SLPI and elafin/trappin-2 have many biological functions as diverse as anti-bacterial, anti-fungal, anti-viral, anti-inflammatory and immuno-modulatory functions, in addition to their well-recognized role as protease inhibitors." @default.
- W2024249553 created "2016-06-24" @default.
- W2024249553 creator A5009419142 @default.
- W2024249553 creator A5040826567 @default.
- W2024249553 creator A5048841329 @default.
- W2024249553 creator A5069263424 @default.
- W2024249553 creator A5070290694 @default.
- W2024249553 creator A5079433845 @default.
- W2024249553 date "2008-02-01" @default.
- W2024249553 modified "2023-10-16" @default.
- W2024249553 title "Multifaceted roles of human elafin and secretory leukocyte proteinase inhibitor (SLPI), two serine protease inhibitors of the chelonianin family" @default.
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