4.2 Article

Galectin 9 is the sugar-regulated urate transporter/channel UAT

Journal

GLYCOCONJUGATE JOURNAL
Volume 19, Issue 7-9, Pages 491-498

Publisher

SPRINGER
DOI: 10.1023/B:GLYC.0000014078.65610.2f

Keywords

ion channel; transmembrane protein; hyperuricemia; isoforms

Funding

  1. NCRR NIH HHS [1 S10 RR0 9145] Funding Source: Medline
  2. NIDDK NIH HHS [DK52785, DK57867] Funding Source: Medline
  3. NATIONAL CENTER FOR RESEARCH RESOURCES [S10RR009145] Funding Source: NIH RePORTER
  4. NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [R01DK052785, R01DK057867] Funding Source: NIH RePORTER

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UAT, also designated galectin 9, is a multifunctional protein that can function as a urate channel/transporter, a regulator of thymocyte-epithelial cell interactions, a tumor antigen, an eosinophil chemotactic factor, and a mediator of apoptosis. We review the evidence that UAT is a transmembrane protein that transports urate, describe our molecular model for this protein, and discuss the evidence from epitope tag and lipid bilayer studies that support this model of the transporter. The properties of recombinant UAT are compared with those of urate transport into membrane vesicles derived from proximal tubule cells in rat kidney cortex. In addition, we review channel functions predicted by our molecular model that resulted in the novel finding that the urate channel activity is regulated by sugars and adenosine. Finally, the presence and possible functions of at least 4 isoforms of UAT and a closely related gene hUAT2 are discussed.

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