Paracellin-1, a renal tight junction protein required for paracellular Mg2+ resorption
Paracellin-1, a renal tight junction protein required for paracellular Mg2+ resorption
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DOI：
10.1126/science.285.5424.103
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发表时间：
1999-07-02
期刊：
影响因子：
56.9
通讯作者：
Lifton, RP
中科院分区：
文献类型：
--
作者：
Simon, DB;Lu, Y;Lifton, RP
上皮允许选择性和调节流量从顶端到基底外侧表面的跨细胞通道通过细胞或细胞间的细胞旁流量。紧密连接构成了细胞旁传导的屏障，然而，对介导细胞旁通透性的特定分子知之甚少。肾镁离子（Mg 2+）再吸收主要通过Henle（TAL）的粗升支中的细胞旁传导发生。在此，定位克隆已经鉴定了导致肾Mg 2+消耗的人类基因paracellin-1（PCLN-1）突变。PCLN-1位于TAL的紧密连接中，并且与紧密连接蛋白的claudin家族相关。这些研究结果提供了深入了解Mg 2+稳态，证明了紧密连接蛋白在人类疾病中的作用，并确定了选择性细胞旁电导的重要组成部分。
Epithelia permit selective and regulated flux from apical to basolateral surfaces by transcellular passage through cells or paracellular flux between cells. Tight junctions constitute the barrier to paracellular conductance; however, Little is known about the specific molecules that mediate paracellular permeabilities. Renal magnesium ion (Mg2+) resorption occurs predominantly through a paracellular conductance in the thick ascending limb of Henle (TAL), Here, positional cloning has identified a human gene, paracellin-1 (PCLN-1), mutations in which cause renal Mg2+ wasting. PCLN-1 is Located in tight junctions of the TAL and is related to the claudin family of tight junction proteins. These findings provide insight into Mg2+ homeostasis, demonstrate the role of a tight junction protein in human disease, and identify an essential component of a selective paracellular conductance.