Capsazepine reversible inhibition of opioid receptors by capsaicin
-
1
Institute of Biochemistry, Hungarian Academy of Sciences, Hungary
Capsaicin inhibited the binding of endogenous opioid and opioid-like ligands (endomorphin-1, nociceptin and dynorphin-(1-17) in rat brain membrane preparations in vitro. The affinity decrease was most pregnant using endomorphin-1, followed by nociceptin and dynorphin. The inhibition of capsaicin on opioid binding was not observed using non endogenous peptides and synthetic ligands (DAMGO, morphine, naloxone). In the [3H]endomorphin binding assay capsazepine antagonized the inhibitory effect of capsaicin in rat brain membranes, which suggests that capsaicin acts on opioid receptors through the vanilloid receptor (TRPV1). In Chinese hamster ovary cells stable expressing -opioid receptors and lacking TRPV1 receptors, the inhibitory effect of capsaicin on the binding of [3H]endomorphin-1 was not present. It was concluded that the inhibitory effect of capsaicin on the affinity of opioid endogenous peptides in rat brain membrane preparations is not a direct effect, but indirectly other intermediate factors like protein kinases play an important role.
Conference:
12th Meeting of the Hungarian Neuroscience Society, Budapest, Hungary, 22 Jan - 24 Jan, 2009.
Presentation Type:
Poster Presentation
Topic:
Pathophysiology and neurology - non-degenerative disorders
Citation:
Wollemann
M,
Ioja
E and
Benyhe
S
(2009). Capsazepine reversible inhibition of opioid receptors by capsaicin.
Front. Syst. Neurosci.
Conference Abstract:
12th Meeting of the Hungarian Neuroscience Society.
doi: 10.3389/conf.neuro.01.2009.04.120
Copyright:
The abstracts in this collection have not been subject to any Frontiers peer review or checks, and are not endorsed by Frontiers.
They are made available through the Frontiers publishing platform as a service to conference organizers and presenters.
The copyright in the individual abstracts is owned by the author of each abstract or his/her employer unless otherwise stated.
Each abstract, as well as the collection of abstracts, are published under a Creative Commons CC-BY 4.0 (attribution) licence (https://creativecommons.org/licenses/by/4.0/) and may thus be reproduced, translated, adapted and be the subject of derivative works provided the authors and Frontiers are attributed.
For Frontiers’ terms and conditions please see https://www.frontiersin.org/legal/terms-and-conditions.
Received:
04 Mar 2009;
Published Online:
04 Mar 2009.
*
Correspondence:
Sándor Benyhe, Institute of Biochemistry, Hungarian Academy of Sciences, Szeged, Hungary, benyhe@brc.hu