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Differential metabolism of dynorphins in substantia nigra, striatum and hippocampus
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences. (Pharmacology)
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1997 (English)In: Peptides, ISSN 0196-9781, E-ISSN 1873-5169, Vol. 18, no 7, 949-956 p.Article in journal (Refereed) Published
Abstract [en]

To map the proteolytic enzymes metabolizing dynorphins in brain structures, size-exclusion chromatography linked to electrospray ionization mass spectrometry was used. Enzymes extracted from rat hippocampus, striatum, and substantia nigra were tested for their capability of converting dynorphin-related peptides. Dynorphin A was the most resistant to proteolytic conversion, whereas Big dynorphin and dynorphin B-29 were slowly converted to dynorphin A and dynorphins A and B, respectively. Dynorphin B and alpha-neoendorphin were the least resistant. Dynorphin B was rapidly converted to Leu-enkephalin in the striatum and hippocampus but to Leu-enkephalin-Arg6 in the substantia nigra. alpha-Neoendorphin was converted to Leu-enkephalin in all tissues investigated.

Place, publisher, year, edition, pages
1997. Vol. 18, no 7, 949-956 p.
Keyword [en]
dynorphin, enkephalin, peptidases, metabolism, HPLC, mass spectrometry
National Category
Pharmaceutical Sciences
URN: urn:nbn:se:uu:diva-50731DOI: 10.1016/S0196-9781(97)00025-9ISI: A1997YC75700006PubMedID: 9357051OAI: oai:DiVA.org:uu-50731DiVA: diva2:78640
Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-03-10Bibliographically approved

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