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. A claudin with unknown function and tissue distribution is claudin-17. We characterized claudin-17 by overexpression and knock-down in two renal cell lines. Overexpression in MDCK C7 cell layers caused a threefold increase in paracellular anion permeability and switched these cells from cation- to anion-selective. Knockdown in LLC-PK(1) cells indorsed the finding of claudin-17-based anion channels. Mutagenesis revealed that claudin-17 anion selectivity critically depends on a positive charge at position 65. Claudin-17 expression was found in two organs: marginal in brain but abundant in kidney, where expression was intense in proximal tubules and gradually decreased towards distal segments. As claudin-17 is predominantly expressed in proximal nephrons, which exhibit substantial, though molecularly not defined, paracellular chloride reabsorption, we suggest that claudin-17 has a unique physiological function in this process. In conclusion, claudin-17 forms channels within tight junctions with distinct anion preference.     

The mechanism of the lead tetraacetate oxidation of a B-norsteroid

Zusammenfassung Für die Bildung neuartiger Oxydationsprodukte, die bei der Reaktion eines B-Norsteroidalkohols mit Blei-tetraacetat entstehen, werden zwei Mechanismen vorgeschlagen: Die bekannte Spaltungs-Additions-Reaktion eines Alkoxy Radikals und die bisher unbekannte Umlagerung eines Alkyl-tertiäralkoxy Radikals.     

A cautionary note on pentacyanoammonioferrate use for determining L-canavanine occurrence in biological materials

Summary Caution must be taken in the prevelant use of the pentacyanoammonioferrate reagent for the detection of L-canavanine in biological materias. This reagent reacts with L-histidine at neutral pH to form a pentacyanoammonioferate-histidine complex that is mistaken readily for its canavanine-containing counterpart.This work was supported by a grant from the National Science Foundation (PCM-78-20167). This is publication number 81-7-199 of the Kentucky Agriculatural Experiment Station, Lexington