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Departments of Internal Medicine and Cell Biology, Yale School of Medicine, New Haven, Connecticut.
Correspondence to Dr. James M. Anderson, 1080 LMP, Department of Internal Medicine, Yale School of Medicine, 333 Cedar Street, New Haven, CT 06520. Phone: 203-785-7312; Fax: 203-785-7273; E-mail: james.anderson{at}yale.edu
Abstract. Three types of transmembrane proteins have been identified within the tight junction, but it remains to be determined how they provide the molecular basis for regulating the paracellular permeability for water, solutes, and immune cells. Several of these proteins localize specifically within the continuous cell-to-cell contacts of the tight junction. One of these, occludin, is a cell adhesion molecule that has been demonstrated to influence ion and solute permeability. The claudins are a family of four-membrane spanning proteins; unexpectedly, other members of this family have already been characterized without recognizing their relationship to tight junctions. Junction adhesion molecule, the most recently identified tight junction component, is a member of the Ig superfamily and influences the paracellular transmigration of immune cells. A plaque of cytoplasmic proteins under the junction may be responsible for scaffolding the transmembrane proteins, creating a link to the perijunctional actin cytoskeleton and transducing regulatory signals that control the paracellular barrier.
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