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The 84-kDa Form of Human Matrix Metalloproteinase-9 Degrades Substance P and Gelatin by Jon R. Backstrom; Zoltán A. Tökés is a Neuroscience article available to read on EtoBox.

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Abstract: Matrix metalloproteinase‐9 (MMP‐9) is secreted from cells and, once activated, is thought to degrade collagen in the extracellular matrix. Because collagen is not readily localized where neurons have been shown to produce MMP‐9 in the human brain, the ability of this enzyme to degrade bioactive peptides was investigated with representative tachykinin peptides [substance P (SP), neurokinin A, neurokinin B, and kassinin]. Latent MMP‐9 (94 kDa) was purified from the human cell line HL‐60 and converted to an intermediary active form (84 kDa) with __p__‐aminophenylmercuric acetate. This active form of MMP‐9 degraded SP with a __k__~cat~/__K__~m~ of 170 m__M__^−1^ min^−1^, which is 30‐fold greater than the previously reported value for a representative collagen‐derived peptide. The major digestion products were identified as SP~1–6~ and SP~7–11~, which were derived from cleavage of the Gln^6^‐Phe^7^ bond. Minor products were also generated from cleavage of the Gly^9^‐Leu^10^ bond. The other representative tachykinin peptides were cleaved at rates >10‐fold slower than that of SP. The 84‐kDa peptidase was also active as a gelatinase. Longer treatment of MMP‐9 with __p__‐aminophen

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Author

Jon R. Backstrom; Zoltán A. Tökés

Publisher

John Wiley and Sons; Wiley (Blackwell Publishing); Blackwell Publishing Inc.; Wiley (ISSN 0022-3042)

Published

1995

Language

EN

Field

Neuroscience (Life Sciences)