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J Biol Chem, Vol. 273, Issue 24, 14663-14666, June 12, 1998
,
From the Arginine transport is important for a number of
biological processes in vertebrates, and its transport may be
rate-limiting for the production of nitric oxide. The majority of
L-Arg transport is mediated by System y+,
although several other carriers have been kinetically defined. System
y+ cationic amino acid transport is mediated by proteins
encoded by a family of genes, Cat1, Cat2, and
Cat3. High affinity L-arginine transport was
investigated in embryonic fibroblast cells derived from
Cat1 knockout mice that lack functional Cat1. Both wild
type and knockout cells transport arginine with comparable
Km and Vmax. However, the
apparent affinity for lysine transport was 2.4 times lower in
Cat1 San Diego Cancer Center and Department of
Medicine, University of California, La Jolla, California 92093-0684 and
¶ Department of Pharmacology, Faculty of Medicine, Kyoto
University, Kyoto 606, Japan
/ cells when compared with wild type
cells, a property characteristic of Cat3-mediated transport. Northern
analysis-documented Cat2 mRNA increased 2-fold, whereas
Cat3 mRNA levels increased 11-fold in
Cat1/ relative to
Cat1+/+ cells. The low affinity
Cat2a mRNA was not detectably expressed in these cells.
Even though Cat3 expression is normally limited to adult
brain, there was a large increase in the amount of Cat3 protein present
at the plasma membrane of Cat1/ embryonic
fibroblast cells. These results suggest that Cat3 compensates for the
loss of functional Cat1 in cells derived from Cat1 knockout mice and mediates the majority of high affinity arginine transport.
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