A peptide from the Drosophila Shaker K+ channel inhibits a voltage-gated K+ channel in basolateral membranes of Necturus enterocytes.
A peptide from the Drosophila Shaker K+ channel inhibits a voltage-gated K+ channel in basolateral membranes of Necturus enterocytes.
复制标题
来自果蝇 Shaker K 通道的肽可抑制 Necturus 肠细胞基底外侧膜中的电压门控 K 通道。
DOI：
10.1073/pnas.89.5.1770
复制
发表时间：
1992
影响因子：
11.1
通讯作者：
Schultz,SG
中科院分区：
文献类型：
--
作者：
Dubinsky,WP;Mayorga-Wark,O;Schultz,SG
由果蝇Shaker K+通道的前22个氨基酸残基组成的合成肽在加入到浸浴该通道内表面的溶液中时抑制在平面磷脂双层中重构的Necturus肠细胞的基底外侧膜囊泡中的电压门控K+通道，但在加入到浸浴其外表面的溶液中时不抑制。其中7位的亮氨酸被苯丙氨酸取代的修饰肽也是有效的抑制剂，但用赖氨酸或谷氨酸取代亮氨酸-7，或用胰蛋白酶消化，使肽无效;用甘氨酸取代亮氨酸-7显著降低但不消除肽作为抑制剂的有效性。这些结果与Shaker K+通道+ADHoshi，T.，Zagotta，W.N. & Aldrich，R.W.（1990）Science 250，533-538;和Zagotta，W.N.，Hoshi，T. & Aldrich，R.W.（1990）Science 250，568-571. BD和建议，在Necturus K+通道的内表面的受体的分子解剖结构与肽相互作用，从而抑制该通道可能是类似的Shaker K+通道。
A synthetic peptide composed of the first 22 amino acid residues of the Drosophila Shaker K+ channel inhibits a voltage-gated K+ channel in basolateral membrane vesicles from Necturus enterocytes reconstituted in planar phospholipid bilayers when added to the solution bathing the inner surface of this channel but not when added to the solution bathing its outer surface. A modified peptide in which the leucine in the 7 position is replaced with phenylalanine is also an effective inhibitor, but replacement of the leucine-7 with lysine or glutamate, or digestion with trypsin, renders the peptide ineffective; replacement of the leucine-7 with glycine markedly reduces but does not abolish the effectiveness of the peptide as an inhibitor. These results are analogous to those reported for the Shaker K+ channel +ADHoshi, T., Zagotta, W.N. & Aldrich, R.W. (1990) Science 250, 533-538; and Zagotta, W.N., Hoshi, T. & Aldrich, R.W. (1990) Science 250, 568-571.+BD and suggest that the molecular anatomy of the receptor at the inner face of the Necturus K+ channel with which the peptide interacts to bring about inhibition of that channel may be similar to that of the Shaker K+ channel.