Dimerization of G protein-coupled receptors: CB1 cannabinoid receptors as an example

被引：111

作者：

Wager-Miller, J

Westenbroek, R

Mackie, K

机构：

[1] Univ Washington, Dept Anesthesiol, Seattle, WA 98195 USA

[2] Univ Washington, Dept Pharmacol, Seattle, WA 98195 USA

[3] Univ Washington, Dept Physiol & Biophys, Seattle, WA 98195 USA

来源：

CHEMISTRY AND PHYSICS OF LIPIDS | 2002年 / 121卷 / 1-2期

关键词：

dimerization; G-protein; receptors;

D O I：

10.1016/S0009-3084(02)00151-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A polyclonal antibody directed towards the last 73 amino acid residues of the rat type 1 cannabinoid (CB 1) receptor strongly and exclusively labels a high molecular weight (between 160 and 200 kDa) form of the receptor in Western analysis. In contrast, a human CB1 polyclonal antibody identifies both monomeric CB1 as well as the high molecular weight form. The carboxy terminus (CT) antibody was also used in immunocytochemistry of rat hippocampal sections. Sections probed with CT antibody show intense staining of a meshwork of fibers and occasional interneurons of the stratum oriens, stratum pyramidal, and stratum radiatum of the CA1 and CA3 regions while mossy fibers and granule cells of the internal stratum appear unstained. These data provide evidence that CB 1 likely exists as a dimer in vivo and that the carboxy end of the receptor may play a role in the assembly of the oligomer. (C) 2002 Elsevier Science Ireland Ltd. All rights reserved.

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页码：83 / 89

页数：7

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