Molecular basis of claudin-17 anion selectivity.

Claudin-17 is a paracellular channel-forming tight junction protein. Unlike the cation channels claudin-2 and -15, claudin-17 forms a distinct anion-selective channel. Aim of this study was to determine the molecular basis of channel formation and charge selectivity of this protein.

Charge-selective claudin channels.

Claudins are the main determinants of barrier properties of the tight junction. Many claudins have been shown to act by tightening the paracellular pathway, but several function as paracellular channels. While some depend on the endogenous claudin background of the analyzed cell line, for other claudins, a distinct charge-selectivity has been shown.

Claudin-17 forms tight junction channels with distinct anion selectivity.

Barrier properties of tight junctions are determined by the claudin protein family. Many claudins seal this barrier, but others form paracellular channels. Among these, no claudins with general and clear-cut anion selectivity have yet been described, while for claudin-10a and claudin-4, only circumstantial or small anion selectivities have been shown.