Paracellin-1, a renal tight junction protein required for paracellular Mg2+ resorption.

Article Details

Citation

Simon DB, Lu Y, Choate KA, Velazquez H, Al-Sabban E, Praga M, Casari G, Bettinelli A, Colussi G, Rodriguez-Soriano J, McCredie D, Milford D, Sanjad S, Lifton RP

Paracellin-1, a renal tight junction protein required for paracellular Mg2+ resorption.

Science. 1999 Jul 2;285(5424):103-6. doi: 10.1126/science.285.5424.103.

PubMed ID
10390358 [ View in PubMed
]
Abstract

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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Claudin-16Q9Y5I7Details