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G coupled receptor

Ironically, it was only after three cysteinyl leukotriene antagonists had been approved for clinical use that the two currently known cysteinyl leukotriene receptors were identified molecularly. However, two receptors were proposed earlier by Labat et al. (96). The receptors were proposed to be seven transmembrane G-coupled receptors by several groups... [Pg.209]

Determination of the mechanisms by which individual G proteins or subsets of G proteins differentially couple to G protein-coupled receptors is obviously of fundamental significance to any understanding of the selectivity of cell signaling processes. This fidelity of interaction depends critically upon the ability of the receptors to discriminate between the structural features of different Ga subunits. Multiple regions of this subunit may be involved in determining selective receptor coupling. In the Ga and Ga, subunits, the N-terminus carries a distinct and conserved six-amino acid extension — MTLESI(M) and when this is deleted these subunits couple to several different G - and Gj/g-coupled receptors (Kostensis et al., 1998). [Pg.219]

The change induced in the receptor protein by interaction with its substrate, triggers a change in another protein, from a class known as G-proteins (hence the name G-coupled receptor) which is present at the inner face of the cell wall. In the case of rhodopsin, the G-protein involved is transducin. The modification of transducin in turn induces a... [Pg.249]

Extensive critical reviews aimed at analysing the numerous mathematical methods describing the complex interaction between ligand and G-coupled receptors, have been discussed in the literature. " ... [Pg.45]

B. Effects Angiotensin II is a potent arteriolar vasoconstrictor and stimulant of aldosterone release. All directly incTeases peripheral vascular resistance and, through aldosterone, causes renal sodium retention. All also facilitates the release of norepinephrine from adrenergic nerve endings via presynaptic heteroreceptor action. All of these effects are mediated by the angiotensin AT, receptor, a G, -coupled receptor. [Pg.169]

Figure 1. Model of signal transduction in the snake VN system. Ligand binding to a G-protein (G)-coupled receptor (R) activates a phosphatidyl inositol-specific phospholipase C (PLC) which, in turn, hydrolyzes phosphatidyl inositol 4,5-bisphosphate (PIP2) producing diacylglyserol (DAG) and 1,4,5-inositol trisphosphate (IP3). IP3 acts directly on IP3 receptors on the smooth endoplasmic reticulum to release calcium (Ca ) from intracellular stores and on an IP3- sensitive Ca channel in the cell membrane allowing calcium influx from the extracellular space. The elevated levels of intracellular Ca results in activation of the ryanodine receptor (RyR) on the membrane of the endoplasmic reticulum, resulting in additional Ca release from intracellular stores, a phenomenon known as calcium-induced calcium release (CICR). Intracellular Ca levels return to prestimulation levels by efflux of Ca and influx of sodium (NA ) through a NAV Ca exchanger. Figure 1. Model of signal transduction in the snake VN system. Ligand binding to a G-protein (G)-coupled receptor (R) activates a phosphatidyl inositol-specific phospholipase C (PLC) which, in turn, hydrolyzes phosphatidyl inositol 4,5-bisphosphate (PIP2) producing diacylglyserol (DAG) and 1,4,5-inositol trisphosphate (IP3). IP3 acts directly on IP3 receptors on the smooth endoplasmic reticulum to release calcium (Ca ) from intracellular stores and on an IP3- sensitive Ca channel in the cell membrane allowing calcium influx from the extracellular space. The elevated levels of intracellular Ca results in activation of the ryanodine receptor (RyR) on the membrane of the endoplasmic reticulum, resulting in additional Ca release from intracellular stores, a phenomenon known as calcium-induced calcium release (CICR). Intracellular Ca levels return to prestimulation levels by efflux of Ca and influx of sodium (NA ) through a NAV Ca exchanger.
The seven helix region of the serotonin receptor is the site of serotonin binding. The serotonin receptor is a member of the G-coupled receptor protein family. These proteins have similar structures. Their different specificities depend upon differences in primary structure at the ligand bindings site. [Pg.982]

Yet, physicochemical studies using differential scanning calorimetry, infrared spectroscopy and small-angle X-ray diffraction have shown that B[a]P incorporates into phospholipid bilayers and localizes in the most apolar region of the phospholipid matrix. This phenomenon may account for the observation of an expanded and swollen membrane [11]. We have therefore, proposed that distortion of the physiochemical properties of the adipocyte plasma membrane by B[a]P decreases the signalling capacity of G-coupled receptors intimately linked to the phospholipid bilayer, via their seven transmembrane domains. [Pg.459]


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See also in sourсe #XX -- [ Pg.8 , Pg.166 ]




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