NDLI: Participation of the second extracellular loop of claudin-5 in paracellular tightening against ions, small and large molecules

Content Provider	Springer Nature Link
Author	Piehl, Christian Piontek, Jörg Cording, Jimmi Wolburg, Hartwig Blasig, Ingolf E.
Copyright Year	2010
Abstract	Tight junctions control paracellular permeability. Here, we analyzed the impact of residues in the second extracellular loop (ECL2) of mouse claudin-5 on paracellular permeability. Stable expression of claudin-5wild type in MDCK-II cells—but not that of mutants R145A, Y148A, Y158A or E159Q—increased transepithelial electrical resistance and decreased fluorescein permeation. Expression of claudin-5Y148A, Y158A or E159Q enhanced permeability of FITC-dextran10 kDa, which was unchanged in cells expressing claudin-5wild type or claudin-5R145A. In contrast, targeting to tight junctions, strand morphology and tight junction assembly were unchanged. It is concluded that R145 is unessential for trans-interaction of claudin-5, but necessary for tightening against small solutes and ions. The highly conserved residues Y148, Y158 and E159 in ECL2 of claudin-5 contribute to homo- and/or heterophilic trans-interaction between classic claudins and thereby tighten the paracellular space against ions, small and large molecules. These results provide novel insights into the molecular function of tight junctions.
Starting Page	2131
Ending Page	2140
Page Count	10
File Format	PDF
ISSN	1420682X
Journal	Cellular and Molecular Life Sciences
Volume Number	67
Issue Number	12
e-ISSN	14209071
Language	English
Publisher	SP Birkhäuser Verlag Basel
Publisher Date	2010-03-24
Publisher Place	Basel
Access Restriction	Subscribed
Subject Keyword	Claudin Tight junction Paracellular permeability Transmembrane protein Protein–protein interaction Biochemistry Life Sciences Biomedicine general Cell Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology Molecular Medicine Pharmacology Cellular and Molecular Neuroscience

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