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Journal of Environmental Analytical Chemistry

Journal of Environmental Analytical Chemistry

ISSN: 2380-2391

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G-protein coupled receptors (GPCRs) are the largest family of signaling proteins that are responsible for information input from the extracellular environment. The plasma membrane in which GPCRs reside usually carries an electrostatic membrane potential (DW). This potential and its disparity in some cell types are important for cellular functions, including GPCR signaling (Mahaut-Smith et al. 2008; Zhang et al. 2014). The occurrence of membrane potential-sensitivity signaling has been observed in many GPCRs, including the M2 receptor (Ben-Chaim et al. 2003), P2Y1 (Gurung et al. 2008), the a2A-adrenoceptor (Rinne et al. 2013), the b1-adrenoceptor (Birk et al. 2015), the dopamine D2 receptor (Sahlholm et al. 2008), and therefore the histamine H3 receptor (Sahlholm et al. 2012). The signaling capacity of a GPCR changes when the membrane potential is experimentally modulated. A question often raised is what and where is that the voltage sensor? Researchers would like to know which amino acid residue(s) in the GPCR molecule is responsible for DW-sensitivity. In general, a selected binding-GPCR pair is often considered as a singular system that has different thermodynamic parameters and pharmacological properties from other ligand-GPCR combinations (Masuho et al. 2015). In real in vivo situations, such systems are necessarily coupled with each other and with upstream and downstream networks, and their thermodynamic parameters can be influenced strongly by the environment, including DW. In the following report, we'll first discuss the thermodynamics of an isolated GPCR activation process consistent with the classical view of ligand-receptor equilibrium, then plan to address the above questions about DW-sensitivity.

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