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一种与人类D1/5受体具有高度同源性的果蝇多巴胺受体的一级结构和功能特性

Primary structure and functional characterization of a Drosophila dopamine receptor with high homology to human D1/5 receptors.

作者信息

Gotzes F, Balfanz S, Baumann A

机构信息

Institut für Biologische Informationsverarbeitung, Forschungszentrum Jülich GmbH, FRG.

出版信息

Recept Channels. 1994;2(2):131-41.

PMID:7953290
Abstract

Members of the superfamily of G-protein coupled receptors share significant similarities in sequence and transmembrane architecture. We have isolated a Drosophila homologue of the mammalian dopamine receptor family using a low stringency hybridization approach. The deduced amino acid sequence is approximately 70% homologous to the human D1/D5 receptors. When expressed in HEK 293 cells, the Drosophila receptor stimulates cAMP production in response to dopamine application. This effect was mimicked by SKF 38393, a specific D1 receptor agonist, but inhibited by dopaminergic antagonists such as butaclamol and flupentixol. In situ hybridization revealed that the Drosophila dopamine receptor is highly expressed in the somata of the optic lobes. This suggests that the receptor might be involved in the processing of visual information and/or visual learning in invertebrates.

摘要

G蛋白偶联受体超家族的成员在序列和跨膜结构上具有显著的相似性。我们使用低严谨度杂交方法分离出了哺乳动物多巴胺受体家族的果蝇同源物。推导的氨基酸序列与人D1/D5受体约70%同源。当在HEK 293细胞中表达时,果蝇受体在应用多巴胺后刺激cAMP产生。这种效应被特异性D1受体激动剂SKF 38393模拟,但被多巴胺能拮抗剂如布他拉莫和氟哌噻吨抑制。原位杂交显示果蝇多巴胺受体在视叶的胞体中高度表达。这表明该受体可能参与无脊椎动物的视觉信息处理和/或视觉学习。

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