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J Biol Chem, Vol. 275, Issue 19, 14331-14335, May 12, 2000
From the Departments of We provide evidence here that
b0,+ amino acid transporter (b0,+AT)
interacts with 4F2 heavy chain (4F2hc) as well as with the protein related to b0,+ amino acid transporter (rBAT) to constitute
functionally competent b0,+-like amino acid transport
systems. This evidence has been obtained by co-expression of
b0,+AT and 4F2hc or b0,+AT and rBAT in human
retinal pigment epithelial cells and in COS-1 cells. The ability to
interact with 4F2hc and rBAT is demonstrable with mouse
b0,+AT as well as with human b0,+AT. Even
though both the 4F2hc·b0,+AT complex and the
rBAT·b0,+AT complex exhibit substrate specificity that is
characteristic of system b0,+, these two complexes differ
significantly in substrate affinity. The 4F2hc·b0,+AT
complex has higher substrate affinity than the
rBAT·b0,+AT complex. In situ hybridization
studies demonstrate that the regional distribution pattern of mRNA
in the kidney is identical for b0,+AT and 4F2hc. The
pattern of rBAT mRNA expression is different from that of
b0,+AT mRNA and 4F2hc mRNA, but there are regions
in the kidney where b0,+AT mRNA expression overlaps
with rBAT mRNA expression as well as with 4F2hc mRNA expression.
Differential Influence of the 4F2 Heavy Chain and the Protein
Related to b0,+ Amino Acid Transport on Substrate
Affinity of the Heteromeric b0,+ Amino Acid
Transporter*
,,,
,,, and**
Biochemistry and Molecular
Biology, § Physiology and Endocrinology, and
¶ Obstetrics and Gynecology and the Institute of Molecular
Medicine and Genetics, Medical College of Georgia,
Augusta, Georgia 30912
*
This work was supported by National Institutes of Health
Grants DA 10045 and HD 33347.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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