TRANSDUCTION IN TASTE RECEPTOR-CELLS REQUIRES CAMP-DEPENDENT PROTEIN-KINASE
TRANSDUCTION IN TASTE RECEPTOR-CELLS REQUIRES CAMP-DEPENDENT PROTEIN-KINASE
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DOI：
10.1038/331351a0
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发表时间：
1988-01-28
期刊：
影响因子：
64.8
通讯作者：
LINDEMANN, B
中科院分区：
文献类型：
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作者：
AVENET, P;HOFMANN, F;LINDEMANN, B
在味觉化学感受中，环磷酸腺苷（cAMP）似乎是将刺激的接收耦合到反应的产生的细胞内信使之一。最近发现甜味剂引起GTP依赖性cAMP 1的产生，这提出了一个问题，即这种胞质信使如何在味觉受体细胞膜上起作用。我们已经表明，cAMP导致这些细胞中的大量去极化2。在这里，我们显示与全细胞记录和内而外的膜补丁，cAMP引起的去极化是占cAMP依赖性蛋白激酶，主要是44 pS电导失活钾通道的行动。因此，味觉细胞的细胞内信号传导不同于嗅觉3和感光细胞4，5，其中环核苷酸通过与它们结合而不是通过诱导它们的磷酸化来控制非特异性通道。
In taste chemoreception, cyclic adenosine monophosphate (cAMP) appears to be one of the intracellular messengers coupling reception of stimulus to the generation of the response. The recent finding that sweet agents cause a GTP-dependent generation of cAMP1poses the question of how this cytosolic messenger acts at the membrane of taste receptor cells. We have shown that cAMP causes a substantial depolarization in these cells2. Here we show with whole-cell recordings and inside-out membrane patches that the depolarization caused by cAMP is accounted for by the action of cAMP-dependent protein kinase, which inactivates potassium channels predominantly of 44 pS conductance. Thus, intracellular signalling of the gustatory cells differs from that of olfactory3and photoreceptor cells4,5, where cyclic nucleotides control unspecific channels by binding to them rather than by inducing their phosphorylation.