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- W2110656546 abstract "Claudin-5 is a protein component of many endothelial tight junctions, including those at the blood-brain barrier, a barrier that limits molecular exchanges between the central nervous system and the circulatory system. To test the contribution of claudin-5 to this barrier function of tight junctions, we expressed murine claudin-5 in Madin-Darby canine kidney II cells. The result was a fivefold increase in transepithelial resistance in claudin-5 transductants and a reduction in conductance of monovalent cations. However, the paracellular flux of neither neutral nor charged monosaccharides was significantly changed in claudin-5 transductants compared to controls. Therefore, expression of claudin-5 selectively decreased the permeability to ions. Additionally, site-directed mutations of particular amino acid residues in the first extracellular domain of claudin-5 altered the properties of the tight junctions formed in response to claudin-5 expression. In particular, the conserved cysteines were crucial: mutation of either cysteine abolishted the ability of claudin-5 to increase transepithelial resistance, and mutation of Cys(64) strikingly increased the paracellular flux of monosaccharides. These new insights into the functions of claudin-5 at the molecular level in tight junctions may account for some aspects of the blood-brain barrier's selective permeability." @default.
- W2110656546 created "2016-06-24" @default.
- W2110656546 creator A5012457054 @default.
- W2110656546 creator A5034876533 @default.
- W2110656546 creator A5039106739 @default.
- W2110656546 creator A5053341400 @default.
- W2110656546 date "2004-10-01" @default.
- W2110656546 modified "2023-10-15" @default.
- W2110656546 title "Selective Decrease in Paracellular Conductance of Tight Junctions: Role of the First Extracellular Domain of Claudin-5" @default.
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- W2110656546 doi "https://doi.org/10.1128/mcb.24.19.8408-8417.2004" @default.
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