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Ovaj protein je član familije rodopsinu -sličnih G protein-spregnutih receptora . GPR30 vezuje estrogen , što dovodi do mobilizacije intracelularnog kalcijuma i sinteze fosfatidilinozitol (3,4,5)-trisfosfata u nukleusu . Ovaj protein učestvuje u brzim negenomskim signalnim eventima. Alternativne transkripcione splajsne varijante koje kodiraju isti protein su bile karakterisane. [6] The distribution of GPR30 is well established in the rodent, with high expression observed in the hypothalamus, pituitary gland, adrenal medulla, kidney medulla and developing follicles of the ovary. [7]

The waveform of receptor-mediated responses plays an important role in shaping the neuronal signal. Interestingly, the kinetics of the GABA response are also different for the receptors formed by each individual subunits. Current-trace responses to application of 10 m M GABA are illustrated in Fig. 5. These recordings indicate that there are significant differences in the kinetics of the GABA responses from Xenopus oocytes depending on which white perch GABA r subunit is expressed. To quantitate the kinetics of the GABA response, the offset GABA responses (current traces after GABA application is terminated) were replotted on a semi-logarithmic scale, with the amplitudes normalized to their initial values (Fig. 6). In each case, the data were fit by a straight line, indicating that offset responses can be described by a single exponential function. The slope of the line represents the time constant of the decay and shows that the receptors formed by the various r subunits exhibit significant differences in their response kinetics. The average time constants of offset responses elicited from receptors formed by various white perch GABA r subunits are shown in the bar graph in Fig. 6C. There are consistent differences between the response kinetics of the two receptor families and between their subgroups. For example, the responses from r 1 receptors were significantly slower than those of r 2 receptors. Such difference in the response kinetics among r 1 and r 2 receptors are determined, in large part, by a single residue at the second transmembrane domain of the subunits (Qian et al., 1999). This dichotomy among r 1 and r 2 subunits is well conserved in all species where GABA r subunits have been cloned. r 1 subunits, which have a proline at the residue site, combine to make a receptor with slower kinetics; whereas r 2 subunits, which contain a serine at the residue site, form receptors with faster response rate. Thus, receptors made of human r 1 subunits exhibit slower response kinetics than receptors made of r 2 subunits (Enz and Cutting, 1999). The kinetic differences among the receptors formed by various GABA r subunits could provide building blocks for the nevous system to construct different types of signal filters, and different types of neuronal signalling in the nervous system.

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