Identification of Three Isoforms for the Na+-dependent Phosphate Cotransporter (NaPi-2) in Rat Kidney*
Identification of Three Isoforms for the Na+-dependent Phosphate Cotransporter (NaPi-2) in Rat Kidney*
复制标题
大鼠肾脏中 Na 依赖性磷酸盐协同转运蛋白 (NaPi-2) 的三种亚型的鉴定*
DOI:
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复制
发表时间:
1998
影响因子:
4.8
通讯作者:
E. Takeda
中科院分区:
文献类型:
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作者:
S. Tatsumi;K. Miyamoto;T. Kouda;Keiko Motonaga;K. Katai;I. Ohkido;K. Morita;H. Segawa;Yoshiko Tani;Hironori Yamamoto;Y. Taketani;E. Takeda
We have isolated three unique NaPi-2-related protein cDNAs (NaPi-2α, NaPi-2β, and NaPi-2γ) from a rat kidney library. NaPi-2α cDNA encodes 337 amino acids which have high homology to the N-terminal half of NaPi-2 containing 3 transmembrane domains. NaPi-2β 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-2γ 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 α, β, and γ were found to be 36, 36, and 29 kDa amino acid polypeptides, respectively. NaPi-2α and NaPi-2γ 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-2γ and -2α 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.
DOI:
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发表时间:
1994
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Werner,A;Kempson,SA;Biber,J;Murer,H
通讯作者:
Murer,H
影响因子:
19.6
作者:
Kavanaugh, MP;Kabat, D
通讯作者:
Kabat, D