Literature DB >> 11852079

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

K Dawn Drake1, Diana Schuette, Ana B Chepelinsky, Tim J C Jacob, M James C Crabbe, Tim J Jacob.   

Abstract

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.

Entities:  

Mesh:

Substances:

Year:  2002        PMID: 11852079     DOI: 10.1016/s0014-5793(02)02284-6

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  2 in total

Review 1.  Invertebrate aquaporins: a review.

Authors:  Ewan M Campbell; Andrew Ball; Stefan Hoppler; Alan S Bowman
Journal:  J Comp Physiol B       Date:  2008-07-02       Impact factor: 2.200

2.  The effect of the interaction between aquaporin 0 (AQP0) and the filensin tail region on AQP0 water permeability.

Authors:  Yosuke Nakazawa; Mikako Oka; Katsuya Furuki; Akiko Mitsuishi; Emi Nakashima; Makoto Takehana
Journal:  Mol Vis       Date:  2011-12-13       Impact factor: 2.367

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.