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- W2050525037 abstract "The occludin-like proteins belong to a family of tetraspan transmembrane proteins carrying a marvel domain. The intrinsic function of the occludin family is not yet clear. Occludin is a unique marker of any tight junction and is found in polarized endothelial and epithelial tissue barriers, at least in the adult vertebrate organism. Occludin is able to oligomerize and to form tight junction strands by homologous and heterologous interactions, but has no direct tightening function. Its oligomerization is affected by pro- and antioxidative agents or processes. Phosphorylation of occludin has been described at multiple sites and is proposed to play a regulatory role in tight junction assembly and maintenance and, hence, to influence tissue barrier characteristics. Redox-dependent signal transduction mechanisms are among the pathways modulating occludin phosphorylation and function. This review discusses the novel concept that occludin plays a key role in the redox regulation of tight junctions, which has a major impact in pathologies related to oxidative stress and corresponding pharmacologic interventions." @default.
- W2050525037 created "2016-06-24" @default.
- W2050525037 creator A5013376407 @default.
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- W2050525037 creator A5074658182 @default.
- W2050525037 creator A5077283478 @default.
- W2050525037 creator A5083892884 @default.
- W2050525037 date "2011-09-01" @default.
- W2050525037 modified "2023-10-16" @default.
- W2050525037 title "Occludin protein family: oxidative stress and reducing conditions." @default.
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