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pH‐Dependent channel activity of heterologously‐expressed main intrinsic protein (MIP) from rat lens
Author(s) -
Drake K.Dawn,
Schuette Diana,
Chepelinsky Ana B,
Jacob Tim J,
Crabbe M.James C
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02284-6
Subject(s) - spodoptera , patch clamp , ion channel , effector , cell culture , conductance , microbiology and biotechnology , biophysics , sf9 , membrane potential , chemistry , biology , biochemistry , recombinant dna , gene , receptor , genetics , mathematics , combinatorics
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.