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J Biol Chem, Vol. 274, Issue 21, 14875-14883, May 21, 1999
From the Departments of ¶ Obstetrics & Gynecology and
We have cloned the human
Na+-dependent multivitamin transporter
(SMVT), which transports the water-soluble vitamins pantothenate, biotin, and lipoate, from a placental choriocarcinoma cell line (JAR).
The cDNA codes for a protein of 635 amino acids with 12 transmembrane domains and 4 putative sites for N-linked
glycosylation. The human SMVT exhibits a high degree of homology
(84% identity and 89% similarity) to the rat counterpart. When
expressed in HRPE cells, the cDNA-induced transport process is
obligatorily dependent on Na+ and accepts pantothenate,
biotin, and lipoate as substrates. The relationship between the
cDNA-specific uptake rate of pantothenate or biotin and
Na+ concentration is sigmoidal with a
Na+:vitamin stoichiometry of 2:1. The human SMVT, when
expressed in Xenopus laevis oocytes, induces inward
currents in the presence of pantothenate, biotin, and lipoate in a
Na+-, concentration-, and potential-dependent
manner. We also report here on the structural organization and
chromosomal localization of the human SMVT gene. The
SMVT gene is ~14 kilobase pairs in length and consists of
17 exons. The SMVT gene is located on chromosome 2p23 as
evidenced by somatic cell hybrid analysis and fluorescence in
situ hybridization.
Human Placental Na+-dependent
Multivitamin Transporter
CLONING, FUNCTIONAL EXPRESSION, GENE STRUCTURE, AND CHROMOSOMAL
LOCALIZATION
,,,,¶, and¶
Biochemistry & Molecular Biology, Medical College of
Georgia, Augusta, Georgia 30912 and the § Department of
Genetics, Yale University School of Medicine,
New Haven, Connecticut 06510
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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