Jun Ichi Nezu

TL;DR: Although its subcellular localization and detailed functional characteristics are not clear at present, OCTN1 appears to be a novel proton antiporter that functions for active secretion of cationic compounds across the renal epithelial brush‐border membrane and may play a role in the renal excretion of xenobiotics and their metabolites.

TL;DR: OATP-B plays a role in the absorption of anionic compounds across the apical membrane of human intestinal epithelial cells, although it cannot be decisively concluded that pH-dependent absorption of pravastatin is determined by OATPB alone.

TL;DR: The pH-sensitive activity of human organic anion transporting polypeptide OATP-B, which is expressed at the apical membrane of human small intestinal epithelial cells, was functionally characterized and clarification of factors, such as pH, that affect the OATp-B activity is essential for an understanding of the physiological and pharmacological relevance of the transporter in the small intestine.

TL;DR: It is concluded that both Na(+)-dependent and -independent carnitine transporters, OCTN2 and OCTN3, mediate the supply of carn itine and acetylcarnitine to epididymal spermatozoa in mice.

TL;DR: It is suggested that Octn2‐type carnitine transporter is dysfunctional in hepatocytes of JVS mice, which shows systemic l‐carnitine deficiency in these mice.