Hiroyasu Tsukaguchi

TL;DR: It is found that SVCT1 and SVCT2 each mediate concentrative, high-affinity L-ascorbic acid transport that is stereospecific and is driven by the Na+ electrochemical gradient.

TL;DR: The properties of a calcium transport protein (CaT1) cloned from rat duodenum using an expression cloning strategy in Xenopus laevis oocytes are reported, which likely plays a key role in the intestinal uptake of calcium.

TL;DR: The expression cloning of a liver cDNA encoding a unique promiscuous solute channel (AQP9) that confers high permeability for both solute and water is reported, defining a new evolutionary branch of the major intrinsic protein family of aquaporin proteins and describing a previously unknown mechanism by which a large variety of solutes and water can pass through a single pore.

TL;DR: The data show that hAQP9 serves as a promiscuous solute channel expressed in both liver and peripheral leukocytes, where it is ideally suited to transport of metabolites and/or nutrients into and out of these cells.

TL;DR: The molecular cloning of a novel human cDNA encoding a vitamin C transporter SVCT1 is described and it is demonstrated that the human SLC23A1 gene product is a related high-affinity l-ascorbic acid transporter (SVCT2) that is widely distributed in brain, retina, and a host of endocrine and neuroendocrine tissues.