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J Biol Chem, Vol. 273, Issue 44, 28568-28575, October 30, 1998

Identification of Three Isoforms for the Na⁺-dependent Phosphate Cotransporter (NaPi-2) in Rat Kidney

From the Department of Clinical Nutrition, School of Medicine, Tokushima University, Tokushima 770, Japan

We have isolated three unique NaPi-2-related protein cDNAs (NaPi-2, NaPi-2, and NaPi-2) from a rat kidney library. NaPi-2 cDNA encodes 337 amino acids which have high homology to the N-terminal half of NaPi-2 containing 3 transmembrane domains. NaPi-2 encodes 327 amino acids which are identical to the N-terminal region of NaPi-2 containing 4 transmembrane domains, whereas the 146 amino acids in the C-terminal region are completely different. In contrast, NaPi-2 encodes 268 amino acids which are identical to the C-terminal half of NaPi-2. An analysis of phage and cosmid clones indicated that the three related proteins were produced by alternative splicing in the NaPi-2 gene. In a rabbit reticulocyte lysate system, NaPi-2 , , and  were found to be 36, 36, and 29 kDa amino acid polypeptides, respectively. NaPi-2 and NaPi-2 were glycosylated and revealed to be 45- and 35-kDa proteins, respectively. In isolated brush-border membrane vesicles, an N-terminal antibody was reacted with 45- and 40-kDa, and a C-terminal antibody was reacted with 37-kDa protein. The sizes of these proteins corresponded to those in glycosylated forms.

A functional analysis demonstrated that NaPi-2 and -2 markedly inhibited NaPi-2 activity in Xenopus oocytes. The results suggest that these short isoforms may function as a dominant negative inhibitor of the full-length transporter.

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