The Na-P cotransporter PiT-2 (SLC20A2) is expressed in the apical membrane of rat renal proximal tubules and regulated by dietary P
American Journal of Physiology - Renal Physiology, ISSN: 1522-1466, Vol: 296, Issue: 4, Page: F691-9
2009
- 150Citations
- 82Captures
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Metrics Details
- Citations150
- Citation Indexes149
- 149
- CrossRef119
- Policy Citations1
- Policy Citation1
- Captures82
- Readers82
- 82
Article Description
The principal mediators of renal phosphate (P) reabsorption are the SLC34 family proteins NaPi-IIa and NaPi-IIc, localized to the proximal tubule (PT) apical membrane. Their abundance is regulated by circulatory factors and dietary P. Although their physiological importance has been confirmed in knockout animal studies, significant P reabsorptive capacity remains, which suggests the involvement of other secondary-active P transporters along the nephron. Here we show that a member of the SLC20 gene family (PiT-2) is localized to the brush-border membrane (BBM) of the PT epithelia and that its abundance, confirmed by Western blot and immunohistochemistry of rat kidney slices, is regulated by dietary P . In rats treated chronically on a high-P (1.2%) diet, there was a marked decrease in the apparent abundance of PiT-2 protein in kidney slices compared with those from rats kept on a chronic low-P (0.1%) diet. In Western blots of BBM from rats that were switched from a chronic low- to high-P diet, NaPi-IIa showed rapid downregulation after 2 h; PiT-2 was also significantly downregulated at 24 h and NaPi-IIc after 48 h. For the converse dietary regime, NaPi-IIa showed adaptation within 8 h, whereas PiT-2 and NaPi-IIc showed a slower adaptive trend. Our findings suggest that PiT-2, until now considered as a ubiquitously expressed P housekeeping transporter, is a novel mediator of P reabsorption in the PT under conditions of acute P deprivation, but with a different adaptive time course from NaPi-IIa and NaPi-IIc. Copyright © 2009 the American Physiological Society.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=65949096839&origin=inward; http://dx.doi.org/10.1152/ajprenal.90623.2008; http://www.ncbi.nlm.nih.gov/pubmed/19073637; https://www.physiology.org/doi/10.1152/ajprenal.90623.2008; https://www.zora.uzh.ch/id/eprint/9758; http://ajprenal.physiology.org/cgi/doi/10.1152/ajprenal.90623.2008; http://ajprenal.physiology.org/content/296/4/F691; http://dx.doi.org/10.5167/uzh-9758; https://dx.doi.org/10.5167/uzh-9758; https://www.zora.uzh.ch/id/eprint/9758/; http://ajprenal.physiology.org/content/296/4/f691; http://ajprenal.physiology.org/content/296/4/f691.abstract; http://ajprenal.physiology.org/content/ajprenal/296/4/F691.full.pdf; https://www.zora.uzh.ch/id/eprint/9758/12/9758_2008_2009_V.pdf; http://ajprenal.physiology.org/lookup/doi/10.1152/ajprenal.90623.2008
American Physiological Society
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