Abstract
We have previously shown that a novel C1s-like serine protease termed MBP-associated serine protease (MASP) is responsible for activation of the complement cascade initiated by mannose-binding protein (MBP). In this communication, we report that MASP is unique in having the proteolytic capacity to cleave C3 with subsequent activation of the alternative pathway, a capacity which C1s lacks.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Carrier Proteins / immunology
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Carrier Proteins / pharmacology*
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Complement Activation / drug effects*
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Complement C1s / pharmacology
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Complement C3 / metabolism*
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Humans
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Hydrolysis / drug effects
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Lectins / immunology*
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Mannose*
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Mannose-Binding Lectins
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Mannose-Binding Protein-Associated Serine Proteases
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Serine Endopeptidases / immunology
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Serine Endopeptidases / pharmacology*
Substances
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Carrier Proteins
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Complement C3
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Lectins
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Mannose-Binding Lectins
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Mannose-Binding Protein-Associated Serine Proteases
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Serine Endopeptidases
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Complement C1s
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Mannose