Acetazolamide inhibits osmotic water permeability by interaction with aquaporin-1
Acetazolamide inhibits osmotic water permeability by interaction with aquaporin-1
复制标题
Acetazolamide 通过与 aquaporin-1 相互作用抑制渗透水渗透性
DOI：
10.1016/j.ab.2006.01.003
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发表时间：
2006-03-15
影响因子：
2.9
通讯作者：
Li, XJ
中科院分区：
文献类型：
--
作者：
Gao, JW;Wang, XH;Li, XJ
Water channel proteins, known as aquaporins, are transmembrane proteins that mediate osmotic water permeability. In a previous study, we found that acetazolamide could inhibit osmotic water transportation across Xenopus oocytes by blocking the function of aquaporin-1 (AQP1). The purpose of the current study was to confirm the effect of acetazolamide on water osmotic permeability using the human embryonic kidney 293 (HEK293) cells transfected with pEGFP/AQP1 and to investigate the interaction between acetazolamide and AQP1. The fluorescence intensity of HEK293 cells transfected with pEGFP/AQP1. which corresponds to the cell volume when the cells swell in a hyposmotic solution, was recorded under confocal laser fluorescence microscopy. The osmotic water permeability was assessed by the change in the ratio of cell fluorescence to certain cell area. Acetazolamide, at concentrations of I and 10 mu M, inhibited the osmotic water permeability in HEK293 cells transfected with pEGFP/AQP1. The direct binding between acetazolamide and AQP1 was detected by surface plasmon resonance. AQP1 was prepared from rat red blood cells and immobilized on a CM5 chip. The binding assay showed that acetazolamide Could directly interact with AQP1. This study demonstrated that acetazolamide inhibited osmotic water permeability through interaction with AQP1. (c) 2006 Elsevier Inc. All rights reserved.
