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Identification of bikunin as an endogenous inhibitor of dynorphin convertase in human cerebrospinal fluid
Author(s) -
Suder Piotr,
BierczynskaKrzysik Anna,
Kraj Agnieszka,
Brostedt Peter,
Mak Pawel,
Stawikowski Maciej,
Rolka Krzysztof,
Nyberg Fred,
Fries Erik,
Silberring Jerzy
Publication year - 2006
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2006.05508.x
Subject(s) - dynorphin , dynorphin a , opioid peptide , neuropeptide , chemistry , endogeny , receptor , enzyme , cerebrospinal fluid , biochemistry , κ opioid receptor , opioid , biology , neuroscience
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 δ‐opioid instead of κ‐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 µ m , and the K i value of the inhibitor was 1.7 n m . 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.