AJP - Renal Watch the video to learn how APS reaches out to developing nations.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Am J Physiol Renal Physiol 293: F643-F654, 2007. First published June 20, 2007; doi:10.1152/ajprenal.00228.2007
0363-6127/07 $8.00
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
293/3/F643    most recent
00228.2007v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Web of Science (20)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Virkki, L. V.
Right arrow Articles by Forster, I. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Virkki, L. V.
Right arrow Articles by Forster, I. C.

INVITED REVIEW

Phosphate transporters: a tale of two solute carrier families

Leila V. Virkki, Jürg Biber, Heini Murer, and Ian C. Forster

Institute of Physiology and Center for Integrative Human Physiology (ZIHP), University of Zurich, Zurich, Switzerland

Submitted 16 May 2007 ; accepted in final form 14 June 2007

Phosphate is an essential component of life and must be actively transported into cells against its electrochemical gradient. In vertebrates, two unrelated families of Na+-dependent Pi transporters carry out this task. Remarkably, the two families transport different Pi species: whereas type II Na+/Pi cotransporters (SCL34) prefer divalent HPO42–, type III Na+/Pi cotransporters (SLC20) transport monovalent H2PO4. The SCL34 family comprises both electrogenic and electroneutral members that are expressed in various epithelia and other polarized cells. Through regulated activity in apical membranes of the gut and kidney, they maintain body Pi homeostasis, and in salivary and mammary glands, liver, and testes they play a role in modulating the Pi content of luminal fluids. The two SLC20 family members PiT-1 and PiT-2 are electrogenic and ubiquitously expressed and may serve a housekeeping role for cell Pi homeostasis; however, also more specific roles are emerging for these transporters in, for example, bone mineralization. In this review, we focus on recent advances in the characterization of the transport kinetics, structure-function relationships, and physiological implications of having two distinct Na+/Pi cotransporter families.

phosphate; cotransport; electrophysiology; structure-function



Address for reprint requests and other correspondence: I. C. Forster, Institute of Physiology, Univ. of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland (e-mail: Iforster{at}access.uzh.ch)




This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
L. Beck, C. Leroy, C. Salaun, G. Margall-Ducos, C. Desdouets, and G. Friedlander
Identification of a Novel Function of PiT1 Critical for Cell Proliferation and Independent of Its Phosphate Transport Activity
J. Biol. Chem., November 6, 2009; 284(45): 31363 - 31374.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. B. Farrell, G. E. Tusnady, and M. V. Eiden
New Structural Arrangement of the Extracellular Regions of the Phosphate Transporter SLC20A1, the Receptor for Gibbon Ape Leukemia Virus
J. Biol. Chem., October 23, 2009; 284(43): 29979 - 29987.
[Abstract] [Full Text] [PDF]


Home page
J. Physiol.Home page
S. Eskandari
Remarkable commonalities of electrogenic and electroneutral Na+\#8211;phosphate cotransporters
J. Physiol., September 1, 2009; 587(17): 4131 - 4132.
[Full Text] [PDF]


Home page
J. Physiol.Home page
C. Ghezzi, H. Murer, and I. C. Forster
Substrate interactions of the electroneutral Na+-coupled inorganic phosphate cotransporter (NaPi-IIc)
J. Physiol., September 1, 2009; 587(17): 4293 - 4307.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Renal Physiol.Home page
S. Y. Breusegem, H. Takahashi, H. Giral-Arnal, X. Wang, T. Jiang, J. W. Verlander, P. Wilson, S. Miyazaki-Anzai, E. Sutherland, Y. Caldas, et al.
Differential regulation of the renal sodium-phosphate cotransporters NaPi-IIa, NaPi-IIc, and PiT-2 in dietary potassium deficiency
Am J Physiol Renal Physiol, August 1, 2009; 297(2): F350 - F361.
[Abstract] [Full Text] [PDF]


Home page
pdiHome page
C. P. Schmitt, D. Borzych, B. Nau, E. Wuhl, A. Zurowska, and F. Schaefer
DIALYTIC PHOSPHATE REMOVAL: A MODIFIABLE MEASURE OF DIALYSIS EFFICACY IN AUTOMATED PERITONEAL DIALYSIS
Perit. Dial. Int., July 1, 2009; 29(4): 465 - 471.
[Abstract] [Full Text] [PDF]


Home page
Arterioscler. Thromb. Vasc. Bio.Home page
R. Villa-Bellosta and V. Sorribas
Phosphonoformic Acid Prevents Vascular Smooth Muscle Cell Calcification by Inhibiting Calcium-Phosphate Deposition
Arterioscler Thromb Vasc Biol, May 1, 2009; 29(5): 761 - 766.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Renal Physiol.Home page
R. Villa-Bellosta, S. Ravera, V. Sorribas, G. Stange, M. Levi, H. Murer, J. Biber, and I. C. Forster
The Na+-Pi cotransporter PiT-2 (SLC20A2) is expressed in the apical membrane of rat renal proximal tubules and regulated by dietary Pi
Am J Physiol Renal Physiol, April 1, 2009; 296(4): F691 - F699.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Renal Physiol.Home page
O. W. Moe
PiT-2 Coming Out of the Pits
Am J Physiol Renal Physiol, April 1, 2009; 296(4): F689 - F690.
[Full Text] [PDF]


Home page
Am. J. Physiol. Cell Physiol.Home page
R. Villa-Bellosta and V. Sorribas
Different effects of arsenate and phosphonoformate on Pi transport adaptation in opossum kidney cells
Am J Physiol Cell Physiol, January 1, 2009; 297(3): C516 - C525.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online
Copyright © 2007 by the American Physiological Society.