Disease relevance of Cldn16

• Claudin-16 knock-down (KD) mice exhibit chronic renal wasting of magnesium and calcium and develop renal nephrocalcinosis [1].

High impact information on Cldn16

• Thus, PCLN-1 localizes to the tight junction followed by association with ZO-1, and the PCLN-1.ZO-1 complex may play an essential role in the reabsorption of divalent cations in renal epithelial cells [2].
• However, mutants of the deletion (Delta TRV) and the alanine substitution (ARV and TRA) inhibited the association of PCLN-1 with ZO-1 [2].
• ZO-1 was co-immunoprecipitated with the wild-type PCLN-1 and the alanine substitution (TAV) mutant [2].
• In vitro binding analysis using glutathione S-transferase fusion protein showed that the C-terminal TRV sequence, especially Thr and Val residues, of PCLN-1 interacts with ZO-1 [2].
• We hypothesize that CsA reduces the expression and function of paracellin-1 and accounts for the observed renal Mg(2+) wasting [3].

Anatomical context of Cldn16

• Claudin-16 is one of the tight junction protein claudins and has been shown to contribute to reabsorption of divalent cations in the human kidney [4].
• Restricted localization of claudin-16 at the tight junction in the thick ascending limb of henle's loop together with claudins 3, 4, and 10 in bovine nephrons [4].
• The cultured cells expressed paracellin-1 and the characteristics of cTAL cells [3].

Associations of Cldn16 with chemical compounds

• Ciclosporin reduces paracellin-1 expression and magnesium transport in thick ascending limb cells [3].

Analytical, diagnostic and therapeutic context of Cldn16

• As the first step to clarify these roles, we examined the expression and distribution of claudin-16 and several other major claudin subtypes, claudins 1-4 and 10, in bovine renal tubular segments by immunofluorescence microscopy [4].
• Real-time PCR and western blotting were used to test the CsA effects on paracellin-1 expression of cultured cTAL cells [3].

References