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• W2017579424 abstract "We expressed human endothelin receptors, ETA and ETB, in insect Sf9 cells infected by recombinant baculoviruses that contained the respective cDNAs. Ligand-binding experiments showed that the two expressed receptors have the same affinities as observed for the receptors in mammalian cells, i.e. the ETA receptor showed an affinity order of ET-1≥ET-21≫ET-3, and the ETa receptor remained nonselective for three isopeptide ligands. The ETB receptor was purified by affinity chromatography with K9-biotinyl-ET-1 without losing the ligand-binding activity from the membrane of infected Sf9 cells. Protein chemical analysis of the purified ETB receptor showed that it is glycosylated, and that the N-terminal 38-amino-acid peptide is susceptible to proteolytic digestion, resulting in a small 35-kDa receptor like that found in the human placenta. Surprisingly, the infected and unlysed cells showed a strong intracellular Ca2+ concentration increase ([Ca2+]i), which was generated by a unique signal-transduction pathway consisting of the insect GTP-binding protein and human endothelin receptors expressed in the late phase of virus infection. Due mainly to an efficient expression (over 200000 receptors/cell), to a low background owing to no endogenous homolog receptor in insect Sf9 cells, and to a sensitive fluorescent reagent Fura-2, this insect Sf9 cell system can detect the [Ca2+]i induced by picomolar levels of endothelin-receptor. We propose that this highly sensitive system be used to screen for potential antagonists/agonists of endothelin receptors." @default.
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• W2017579424 date "1997-11-01" @default.
• W2017579424 modified "2023-09-25" @default.
• W2017579424 title "Human Endothelin Receptors ETA and ETB Expressed in Baculovirus-Infected Insect Cells. Direct Application for Signal Transduction Analysis" @default.
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• W2017579424 doi "https://doi.org/10.1111/j.1432-1033.1997.00803.x" @default.
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