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Serine protease‐induced decrease in epithelial ion permeability is dependent on an intact actin cytoskeleton
Author(s) -
Swystun Veronica,
MacNaughton Wallace K.
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.1214.2
Subject(s) - adherens junction , paracellular transport , actin cytoskeleton , microbiology and biotechnology , cytoskeleton , proteases , tight junction , actin , chemistry , transcellular , intracellular , biology , biochemistry , permeability (electromagnetism) , cell , cadherin , enzyme , membrane
The serine proteases trypsin, chymotrypsin and elastase induce a sustained increase in transepithelial electrical resistance (R TE ) when applied to the apical surface of polarised epithelial cell monolayers that is reflected by decreases in Na+ and Cl− paracellular permeabilities. Paracellular permeability is controlled at the intercellular tight junctions and the adherens junctions, with the epithelial actin cytoskeleton linked to proteins comprising both. We show that manipulation of the actin cytoskeleton with latruculin B and jasplakinolide reduces the protease‐induced increase in R TE by 92 ± 5 and 50 ± 8% respectively. Immunocytostaining for F‐ and G‐ actin indicate a shift in the filamentous actin pool. Inhibition of Rho kinases decreased baseline R TE but did not inhibit the protease‐induced increase in R TE .