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Transmembrane proteins of the tight junctions at the blood–brain barrier: Structural and functional aspects

2014; Elsevier BV; Volume: 38; Linguagem: Inglês

10.1016/j.semcdb.2014.11.004

1096-3634

Reiner F. Haseloff, Sophie Dithmer, Lars Winkler, Hartwig Wolburg, Ingolf E. Blasig,

Drug Transport and Resistance Mechanisms

The blood-brain barrier (BBB) is formed by microvascular endothelial cells sealed by tetraspanning tight junction (TJ) proteins, such as claudins and TAMPs (TJ-associated marvel proteins, occludin and tricellulin). Claudins are the major components of the TJs. At the BBB, claudin-5 dominates the TJs by preventing the paracellular permeation of small molecules. On the other hand, TAMPs regulate the structure and function of the TJs; tricellulin may tighten the barrier for large molecules. This review aims at integrating and summarizing the most relevant and recent work on how the BBB is influenced by claudin-1, -3, -5, -12 and the TAMPs occludin and tricellulin, all of which are four-transmembrane TJ proteins. The exact functions of claudin-1, -3, -12 and TAMPs at this barrier still need to be elucidated.