Abstract
Like many other seven transmembrane G-protein coupled receptors (GPCRs), the human mu-opioid receptor (hMOR) interacts with multiple members of the pertussis toxin-sensitive Gi and Go protein families, to regulate adenylyl cyclase, Ca2+ and K+ channels. Notably, opioid agonists represent the most powerful analgesic drugs for the clinical management of pain, through binding opioid receptors. However, not all agonists exert the same level of effect.Plasma membranes are organized into specialized micro-domains differing in composition, biological function and physical properties. In recent years, detergent resistant membranes (DRM) are thought to serve as molecular sorting platforms to concentrate signalling molecules (e.g. opioid receptors) based on membrane fractionation and cholesterol depletion experiments. It remains unclear whether membrane organization with detergent has an effect on hMOR localization.Here we track active hMOR and lipid composition in isopycnic membrane fractions in the presence and absence of CHAPS detergent. hMOR activity was assessed using a modified binding assay. The relative amount of lipid raft marker (flotillin-1), actin and G-proteins were assessed by Western blot analysis. The data show the effects of detergent on receptor distribution. Relocation of the hMOR receptor in the membrane indicates an additional level regulation at the cell membrane.
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