期刊
AMERICAN JOURNAL OF PHYSIOLOGY-REGULATORY INTEGRATIVE AND COMPARATIVE PHYSIOLOGY
卷 281, 期 6, 页码 R1994-R2003出版社
AMER PHYSIOLOGICAL SOC
DOI: 10.1152/ajpregu.2001.281.6.R1994
关键词
major intrinsic protein; aquaporin; glycerol; urea; water permeability
类别
资金
- NINDS NIH HHS [NS-18400] Funding Source: Medline
The major intrinsic protein (MIP) of lens fiber cells is a member of the aquaporin (AQP) water channel family. The protein is expressed at very high levels in lens fiber cells, but its physiological function is unclear. By homology to known AQPs, we have cloned a full-length cDNA encoding an MIP from the lens of killifish (Fundulus heteroclitus). The predicted protein (263 amino acids; GenBank accession no. AF191906) shows 77% identity to amphibian MIPs, 70% identity to mammalian MIPs, and 46% identity to mammalian AQP1. Expression of MIPfun in Xenopus laevis oocytes causes an similar to 40-fold increase in oocyte water permeability. This stimulation is comparable to that seen with AQP1 and substantially larger than that seen with other MIPs. The mercurials HgCl2 and p-chloromercuribenzenesulfonate inhibit the water permeability of MIPfun by similar to 25%. MIPfun is not permeable to glycerol, urea, or formic acid but is weakly permeable to CO2.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据