pH‐Dependent channel activity of heterologously‐expressed main intrinsic protein (MIP) from rat lens

FEBS Letters

Crabbe, M.James C¹  Chepelinsky, Ana B²  Schuette, Diana¹  Drake, K.Dawn¹  Jacob, Tim J³ 

[1] Division of Cell and Molecular Biology, School of Animal and Microbial Sciences, The University of Reading, P.O. Box 228, Whiteknights, Reading, Berkshire RG6 6AJ, UK;National Eye Institute, National Institutes of Health, Bethesda, MD, USA;School of Biosciences, University of Cardiff, Cardiff, UK

关键词: Baculovirus;    Mouse erythroid leukaemia cell;    Lens;    Patch clamping;    Cataract;    Eye;   

DOI  :  10.1016/S0014-5793(02)02284-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Wild-type rat lens main intrinsic protein (MIP) was heterologously expressed in the membrane of Spodoptera frugiperda (Sf21) cells using the baculovirus expression system and in mouse erythroid leukaemia cells (MEL C88). Both MEL and Sf21 cell lines expressing wild-type MIP were investigated for the conductance of ions using a whole cell patch clamp technique. An increase in conductance was seen in both expression systems, particularly on lowering the pH to 6.3. In Sf21 cells, addition of antibodies to the NPA1 box resulted in a reduction of current flow. These results suggest that MIP has pH-dependent ion channel activity, which involves the NPA1 box domain.

【 授权许可】

Unknown