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Am J Physiol Regul Integr Comp Physiol 281: R1994-R2003, 2001;
0363-6119/01 $5.00
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Vol. 281, Issue 6, R1994-R2003, December 2001

Cloning and functional expression of an MIP (AQP0) homolog from killifish (Fundulus heteroclitus) lens

Leila V. Virkki, Gordon J. Cooper, and Walter F. Boron

Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, Connecticut 06520-8026

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 ~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 ~25%. MIPfun is not permeable to glycerol, urea, or formic acid but is weakly permeable to CO2.

major intrinsic protein; aquaporin; glycerol; urea; water permeability


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