Dynorphin A(1-17) biotransformation in striatum of freely moving rats using microdialysis and matrix-assisted laser desorption/ionization mass spectrometry.

Abstract:

:The biotransformation of the opioid peptide dynorphin A(1-17) was investigated in striatum of freely moving Fischer rats, by direct infusion of this peptide, followed by recovery of the resulting biotransformation products via microdialysis and identification using matrix-assisted laser desorption/ionization mass spectrometry. The observed peptides are consistent with enzymatic cleavage at the Arg7-Ile8 position of dynorphin A(1-17), followed by terminal degradation of the resulting dynorphin A(1-7) and dynorphin A(8-17) peptides. Unexpectedly, novel post-translational modifications were found on C-terminal fragments of dynorphin A(1-17). Using tandem mass spectrometry, a covalent modification of mass 172 Da, the nature of which is not understood, was found on the tryptophan residue of C-terminal fragments (Trp14). Additional modifications, of mass 42 and 113 Da, were also found on the N-terminus (Ile8 or Pro10) of these same C-terminal fragments. The role of these modifications of C-terminal fragments has not yet been characterized.

journal_name

J Neurochem

authors

Reed B,Zhang Y,Chait BT,Kreek MJ

doi

10.1046/j.1471-4159.2003.01859.x

keywords:

subject

Has Abstract

pub_date

2003-08-01 00:00:00

pages

815-23

issue

4

eissn

0022-3042

issn

1471-4159

pii

1859

journal_volume

86

pub_type

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