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Three experiments examined the effect of acute naltrexone treatment on both taste reactivity and consumption of ethanol in high ethanol-preferring rat lines: Alko Alcohol-Accepting (AA) rats (Experiments 1 and 2) and Alcohol-Preferring (P) rats (Experiment 3). A 3.0 mg/kg naltrexone dose was ineffective at altering ethanol palatability for either line, whereas 7.5 mg/kg was effective at reducing palatability of 10% ethanol for AA, but not P, rats, as reflected by both a decrease in ingestive responding and an increase in aversive responding. The effects of naltrexone on ethanol consumption were quite consistent: At both dosages, acute naltrexone treatment significantly decreased consumption of 10% ethanol. Termination of naltrexone resulted in an immediate increase in ethanol consumption to control levels. Results show that ethanol palatability and consumption can be dissociated in the rat and that the organization of opioidergic mechanisms that mediate ethanol responses may vary between rat lines. (PsycINFO Database Record (c) 2010 APA, all rights reserved)  相似文献   
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Golden hamsters (Mesocricetus auratus) and dwarf hamsters (Phodopus campbelli) interacted with a conspecific demonstrator that had recently consumed a flavored food. When given a choice between their demonstrator's flavor and another flavor, the dwarf hamsters preferred the flavor their demonstrator had eaten. Golden hamsters did not prefer their demonstrators' diets when the demonstrators were unrelated adults or littermates, but they did when the demonstrator was their mother. Videotaping the interactions between demonstrators and observers revealed that adult golden hamsters did not investigate foods hoarded by their demonstrators whereas dwarf hamsters did. These results are interpreted in terms of the stimuli that activate feeding behavior systems in these 2 hamster species. (PsycINFO Database Record (c) 2010 APA, all rights reserved)  相似文献   
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ETR1 represents a prototypical ethylene receptor. Homologues of ETR1 have been identified in Arabidopsis as well as in other plant species, indicating that ethylene perception involves a family of receptors and that the mechanism of ethylene perception is conserved in plants. The amino-terminal half of ETR1 contains a hydrophobic domain responsible for ethylene binding and membrane localization. The carboxyl-terminal half of the polypeptide contains domains with homology to histidine kinases and response regulators, signaling motifs originally identified in bacteria. The putative histidine kinase domain of ETR1 was expressed in yeast as a fusion protein with glutathione S-transferase and affinity purified. Autophosphorylation of the purified fusion protein was observed on incubation with radiolabeled ATP. The incorporated phosphate was resistant to treatment with 3 M NaOH, but was sensitive to 1 M HCl, consistent with phosphorylation of histidine. Autophosphorylation was abolished by mutations that eliminated either the presumptive site of phosphorylation (His-353) or putative catalytic residues within the kinase domain. Truncations were used to delineate the region required for histidine kinase activity. An examination of cation requirements indicated that ETR1 requires Mn2+ for autophosphorylation. These results demonstrate that higher plants contain proteins with histidine kinase activity. Furthermore, these results indicate that aspects of ethylene signaling may be regulated by changes in histidine kinase activity of the receptor.  相似文献   
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