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Identification of bikunin as an endogenous inhibitor of dynorphin convertase in human cerebrospinal fluid
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2006 (English)In: The FEBS Journal, ISSN 1742-464X, E-ISSN 1742-4658, Vol. 273, no 22, 5113-5120 p.Article in journal (Refereed) Published
Abstract [en]

Dynorphin-converting enzymes constitute a group of peptidases capable of converting dynorphins to enkephalins. Through the action of these enzymes, the dynorphin-related peptides bind to delta-opioid instead of kappa-opioid receptors, leading to a change in the biological function of the neuropeptides. In this article, we describe the identification of the protein bikunin as an endogenous, competitive inhibitor of a dynorphin-converting enzyme in human cerebrospinal fluid. This protein is present together with its target enzyme in the same body fluids. The K-M value of the convertase was found to be 9 mu M, and the K-i value of the inhibitor was 1.7 nM. The finding indicates that bikunin may play a significant role as a regulatory mechanism of neuropeptides, where one bioactive peptide is converted to a shorter sequence, which in turn, can affect the action of its longer form.

Place, publisher, year, edition, pages
2006. Vol. 273, no 22, 5113-5120 p.
Keyword [en]
bikunin, cerebrospinal fluid, dynorphin conversion, inhibition, opioids
National Category
Medical and Health Sciences
URN: urn:nbn:se:uu:diva-22543DOI: 10.1111/j.1742-4658.2006.05508.xISI: 000241674500010PubMedID: 17087727OAI: oai:DiVA.org:uu-22543DiVA: diva2:50316
Available from: 2007-03-03 Created: 2007-03-03 Last updated: 2011-05-17Bibliographically approved

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Nyberg, FredFries, Erik
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Department of Pharmaceutical BiosciencesDepartment of Medical Biochemistry and Microbiology
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