Am J Physiol Cell Physiol Ad Instruments
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Am J Physiol Cell Physiol 279: C1135-C1143, 2000;
0363-6143/00 $5.00
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
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 (17)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bai, L.
Right arrow Articles by Ghishan, F. K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bai, L.
Right arrow Articles by Ghishan, F. K.
Vol. 279, Issue 4, C1135-C1143, October 2000

Cloning and characterization of a type III Na-dependent phosphate cotransporter from mouse intestine

Liqun Bai, James F. Collins, and Fayez K. Ghishan

Departments of Pediatrics and Physiology, Steele Memorial Children's Research Center, University of Arizona Health Sciences Center, Tucson, Arizona 85724

Intestinal and renal absorption of inorganic phosphate (Pi) is critical for phosphate homeostasis in mammals. We have isolated a cDNA that encodes a type III Na-dependent phosphate cotransporter from mouse small intestine (mPit-2). The nucleotide sequence of mPit-2 predicts a protein of 653 amino acids with at least 10 putative transmembrane domains. Kinetic studies, carried out in Xenopus oocytes, showed that mPit-2 cRNA induces significant Na-dependent Pi uptake with an apparent Michaelis constant (Km) for phosphate of 38 µM. The transport of phosphate by mPit-2 is inhibited at high pH. Northern blot analysis demonstrated the presence of mPit-2 mRNA in various tissues, including intestine, kidney, heart, liver, brain, testis, and skin. The highest expression of mPit-2 in the intestine was found in the jejunum. In situ hybridization revealed that mPit-2 mRNA is expressed throughout the vertical crypt-villus axis of the intestinal epithelium. The presence of mPit-2 in the mouse intestine and its unique transport characteristics suggest that multiple Na-dependent cotransporters may contribute to phosphate absorption in the mammalian small intestine.

Na-Pi-III; amphotropic murine retrovirus receptor; Ram-1; sodium-dependent phosphate cotransporter; sodium-phosphate transporter; Pit-2


This article has been cited by other articles:


Home page
Am. J. Physiol. Renal Physiol.Home page
H. Giral, Y. Caldas, E. Sutherland, P. Wilson, S. Breusegem, N. Barry, J. Blaine, T. Jiang, X. X. Wang, and M. Levi
Regulation of rat intestinal Na-dependent phosphate transporters by dietary phosphate
Am J Physiol Renal Physiol, November 1, 2009; 297(5): F1466 - F1475.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Gastrointest. Liver Physiol.Home page
H. Chen, H. Xu, J. Dong, J. Li, and F. K. Ghishan
Tumor necrosis factor-alpha impairs intestinal phosphate absorption in colitis
Am J Physiol Gastrointest Liver Physiol, April 1, 2009; 296(4): G775 - G781.
[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
L. V. Virkki, J. Biber, H. Murer, and I. C. Forster
Phosphate transporters: a tale of two solute carrier families
Am J Physiol Renal Physiol, September 1, 2007; 293(3): F643 - F654.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Cell Physiol.Home page
S. Ravera, L. V. Virkki, H. Murer, and I. C. Forster
Deciphering PiT transport kinetics and substrate specificity using electrophysiology and flux measurements
Am J Physiol Cell Physiol, August 1, 2007; 293(2): C606 - C620.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Cell Physiol.Home page
P. Bottger, S. E. Hede, M. Grunnet, B. Hoyer, D. A. Klaerke, and L. Pedersen
Characterization of transport mechanisms and determinants critical for Na+-dependent Pi symport of the PiT family paralogs human PiT1 and PiT2
Am J Physiol Cell Physiol, December 1, 2006; 291(6): C1377 - C1387.
[Abstract] [Full Text] [PDF]


Home page
Exp PhysiolHome page
J. Marks, S. K. Srai, J. Biber, H. Murer, R. J. Unwin, and E. S. Debnam
Intestinal phosphate absorption and the effect of vitamin D: a comparison of rats with mice
Exp Physiol, May 1, 2006; 91(3): 531 - 537.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online