Abstract
Cowhage spicules provide an important model for histamine-independent itch. We determined that the active component of cowhage, termed mucunain, is a novel cysteine protease. We isolated mucunain and demonstrate that both native and recombinant mucunain evoke the same quality of itch in humans. We also show that mucunain is a ligand for protease-activated receptors two and four. These results support and expand the relationship between proteases, protease-activated receptors, and itch.
Publication types
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Comparative Study
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Cysteine Endopeptidases / isolation & purification
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Cysteine Endopeptidases / metabolism*
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Cysteine Endopeptidases / toxicity
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HeLa Cells
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Humans
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Ligands
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Mucuna / enzymology*
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Mucuna / metabolism
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Plant Extracts / isolation & purification
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Plant Extracts / metabolism
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Plant Extracts / toxicity
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Plant Structures / enzymology
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Plant Structures / toxicity
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Pruritus / chemically induced
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Pruritus / enzymology*
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Receptors, Proteinase-Activated / metabolism*
Substances
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Ligands
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Plant Extracts
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Receptors, Proteinase-Activated
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Cysteine Endopeptidases