A COMPARISON OF MYOCARDIAL ß-ADRENORECEPTOR DENSITY AND LIGAND BINDING AFFINITY AMONG SELECTED TROPICAL FISHES
In fish, the β-adrenoreceptor (β-AR) signaling pathway is known to mediate the cardiac actions of adrenaline primarily via receptors of the β2 subtype (Ask et al., 1980; Gamperl et al., 1994). Temperature acclimation can alter the response of the heart to adrenaline and some of this change has been...
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| Format: | Text |
| Language: | English |
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| Online Access: | http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.610.2187 http://www-heb.pac.dfo-mpo.gc.ca/congress/2002/Cardiovasc/Hanson.pdf |
| Summary: | In fish, the β-adrenoreceptor (β-AR) signaling pathway is known to mediate the cardiac actions of adrenaline primarily via receptors of the β2 subtype (Ask et al., 1980; Gamperl et al., 1994). Temperature acclimation can alter the response of the heart to adrenaline and some of this change has been attributed to a temperature-dependent change in cell surface β-AR density. Olsson et al. (2000) found that Bmax and Kd differed among a limited number of tropical, temperate and Antarctic teleost fish species alluding to the possibility that intrinsic differences in β-AR density and binding affinity may exist among species adapted to different temperatures. The purpose of this study was to examine interspecific variation in myocardial β-adrenoreceptor density (Bmax) and binding affinity (Kd) for ventricular tissue in 7 previously unstudied species of tropical fish. 74 Materials and Methods |
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