Sander Guy R, Cummins Adrian G, Henshall Tanya, Powell Barry C
Tissue Development and Repair, Epithelial Biology Laboratory, Child Health Research Institute, 72 King William Road, North Adelaide, SA 5006, Australia.
FEBS Lett. 2005 Aug 29;579(21):4851-5. doi: 10.1016/j.febslet.2005.07.066.
Coeliac disease is a chronic enteropathy caused by the ingestion of wheat gliadin and other cereal prolamines derived from rye and barley. In the present work, we investigated the mechanisms underlying altered barrier function properties exerted by gliadin-derived peptides in human Caco-2 intestinal epithelial cells. We demonstrate that gliadin alters barrier function almost immediately by decreasing transepithelial resistance and increasing permeability to small molecules (4 kDa). Gliadin caused a reorganisation of actin filaments and altered expression of the tight junction proteins occludin, claudin-3 and claudin-4, the TJ-associated protein ZO-1 and the adherens junction protein E-cadherin.
乳糜泻是一种由摄入小麦醇溶蛋白以及其他源自黑麦和大麦的谷物醇溶蛋白引起的慢性肠病。在本研究中，我们探究了醇溶蛋白衍生肽在人Caco-2肠上皮细胞中改变屏障功能特性的潜在机制。我们证明，醇溶蛋白几乎能立即通过降低跨上皮电阻和增加对小分子（4 kDa）的通透性来改变屏障功能。醇溶蛋白导致肌动蛋白丝重组，并改变了紧密连接蛋白闭合蛋白、闭合蛋白-3和闭合蛋白-4、TJ相关蛋白ZO-1以及黏附连接蛋白E-钙黏蛋白的表达。
