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Investigation of receptor binding and functional characteristics of hemopressin(1–7)

Szabolcs, Dvorácskó and Csaba, Tömböly and Róbert, Berkecz and Attila, Keresztes (2016) Investigation of receptor binding and functional characteristics of hemopressin(1–7). NEUROPEPTIDES, 58. pp. 15-22. ISSN 0143-4179

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Abstract

The orally active, α-hemoglobin derived hemopressin (PVNFKFLSH, Hp(1–9)) and its truncated (PVNFKFL, Hp(1–7) and PVNFKF, Hp(1–6)) and extended ((R)VDPVNFKFLSH, VD-Hp(1–9) and RVD-Hp(1–9)) derivatives have been postulated to be the endogenous peptide ligands of the cannabinoid receptor type 1 (CB1). In an attempt to create a versatile peptidic research tool for the direct study of the CB1 receptor–peptide ligand interactions, Hp(1–7)was radiolabeled and in vitro characterized in rat and CB1 knockoutmouse brain membrane homogenates. In saturation and competition radioligand binding studies, [3H]Hp(1–7) labeledmembrane receptors with high densities and displayed specific binding to a receptor protein, but seemingly not to the cannabinoid type 1, in comparison the results with the prototypic JWH-018, AM251, rimonabant, Hp(1–9) and RVDHp( 1–9) (pepcan 12) ligands in both rat brain and CB1 knockoutmouse brain homogenates. Furthermore, functional [35S]GTP γS binding studies revealed that Hp(1–7) and Hp(1–9) only weakly activated G-proteins in both brainmembrane homogenates. Based on our findings and the latest literature data,we assume that the Hp(1–7) peptide fragmentmay be an allosteric ligand or indirect regulator of the endocannabinoid systemrather than an endogenous ligand of the CB1 receptor.

Item Type: Article
Subjects: Q Science / természettudomány > QD Chemistry / kémia
Depositing User: Dr. Róbert Berkecz
Date Deposited: 02 Oct 2017 07:58
Last Modified: 02 Oct 2017 07:58
URI: http://real.mtak.hu/id/eprint/64738

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