RESUMO
Role of serotonin in olfactory recognition was tested by depleting the olfactory bulb serotonin during postnatal day (PND) 1 - 4 following administration of 5,7-dihydroxytryptamine. Significant difference in the olfactory recognition test was observed during PND5-7; control pups successfully recognized and oriented towards their mother; whereas treated pups failed to recognize their mother odour. Later on, during PND12-14, both group of pups responded equally in the recognition test. Levels of olfactory bulb serotonin were depleted (53.3%) in the treated pups on PND-8, which was restored on PND-14 with only 15% variation. Further analysis demonstrated that depletion of serotonin in olfactory bulb did not affect the normal suckling and weight gain, it only modulates olfactory recognition.
Assuntos
Odorantes , Bulbo Olfatório/metabolismo , Serotonina/metabolismo , 5,7-Di-Hidroxitriptamina/farmacologia , Animais , Animais Recém-Nascidos , Animais Lactentes , Peso Corporal/efeitos dos fármacos , Feminino , Masculino , Bulbo Olfatório/efeitos dos fármacos , Gravidez , Ratos , Ratos Wistar , Serotoninérgicos/farmacologia , Fatores de TempoRESUMO
In all genome-sequencing projects completed to date, a considerable number of 'gaps' have been found in the biochemical pathways of the respective species. In many instances, missing enzymes are displaced by analogs, functionally equivalent proteins that have evolved independently and lack sequence and structural similarity. Here we fill such gaps by analyzing anticorrelating occurrences of genes across species. Our approach, applied to the thiamin biosynthesis pathway comprising approximately 15 catalytic steps, predicts seven instances in which known enzymes have been displaced by analogous proteins. So far we have verified four predictions by genetic complementation, including three proteins for which there was no previous experimental evidence of a role in the thiamin biosynthesis pathway. For one hypothetical protein, biochemical characterization confirmed the predicted thiamin phosphate synthase (ThiE) activity. The results demonstrate the ability of our computational approach to predict specific functions without taking into account sequence similarity.