title: Occludin and claudins in tight-junction strands: leading or supporting players?
abstract: Tight junctions have attracted much interest from cell biologists, especially electron microscopists, since on freeze-fracture electron microscopy they appear as a well-developed network of continuous, anastomosing intramembranous strands (tight-junction strands). These strands might be directly involved in the 'barrier' as well as 'fence' functions in epithelial and endothelial cell sheets, but until recently little was known of their constituents. This review discusses current understanding of the molecular architecture of tight-junction strands, focusing on the recent discovery of two distinct types of tight-junction-specific integral membrane proteins, occludin and claudins.
authors.affiliation: Dept of Cell Biology, Faculty of Medicine, Kyoto University, Sakyo-ku, Kyoto 606, Japan. htsukita@mfour.med.kyoto-u.ac.jp
authors.forename: S
authors.initials: S
authors.lastname: Tsukita
authors.forename: M
authors.initials: M
authors.lastname: Furuse
mesh_terms: D000818:Animals; D002874:Chromosome Mapping; D062445:Claudin-1; D057167:Claudins; D005614:Freeze Fracturing; D006801:Humans; D008565:Membrane Proteins / Q000235:genetics / Q000502:physiology* / Q000648:ultrastructure; D008854:Microscopy, Electron; D005810:Multigene Family; D062793:Occludin; D019108:Tight Junctions / Q000502:physiology* / Q000648:ultrastructure*
chemical_list: C568108:CLDN1 protein, human; C491875:CLDN2 protein, human; D062445:Claudin-1; D057167:Claudins; D008565:Membrane Proteins; C568985:OCLN protein, human; D062793:Occludin