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(Received for publication, April 9, 1997, and in revised form, May 28, 1997)
From the The regulation of the high affinity cationic
amino acid transporter Cat-1 in Fao rat hepatoma cells by amino acid
availability has been studied. Cat-1 mRNA level
increased (3-fold) in 4 h in response to amino acid starvation and
remained high for at least 24 h. This induction was independent of
the presence of serum in the media and transcription and protein
synthesis were required for induction to occur. When Fao cells were
shifted from amino acid-depleted media to amino acid-fed media, the
levels of the induced cat-1 mRNA returned to the basal
level. In amino acid-fed cells, accumulation of cat-1
mRNA was dependent on protein synthesis, indicating that a
labile protein is required to sustain cat-1 mRNA level.
No change in the transcription rate of the cat-1 gene during amino acid starvation was observed, indicating that
cat-1 is regulated at a post-transcriptional step. System
y+ mediated transport of arginine was reduced by 50% in 1 h and
by 70% in 24 h after amino acid starvation. However, when 24-h
amino acid-starved Fao cells were preloaded with 2 mM
lysine or arginine for 1 h prior to the transport assays, arginine
uptake was trans-stimulated by 5-fold. This stimulation was
specific for cationic amino acids, since alanine, proline, or leucine
had no effect. These data lead to the hypothesis that amino acid
starvation results in an increased cat-1 mRNA level to
support synthesis of additional Cat-1 protein. The following lines of
evidence support the hypothesis: (i) the use of inhibitors of protein
synthesis in starved cells inhibits the trans-zero
transport of arginine; (ii) cells starved for 1-24 h exhibited an
increase of trans-stimulated arginine transport activity
for the first 6 h and had no loss of activity at 24 h, suggesting that constant replenishment of the transporter protein occurs; (iii) immunofluorescent staining of 24-h fed and starved cells
for cat-1 showed similar cell surface distribution; (iv) new protein
synthesis is not required for trans-stimulation of arginine
transport upon refeeding of 24-h starved cells. We conclude that the
increased level of cat-1 mRNA in response to amino acid starvation support the synthesis of Cat-1 protein during starvation and
increased amino acid transport upon substrate presentation. Therefore,
the cat-1 mRNA content is regulated by a
derepression/repression mechanism in response to amino acid
availability. We propose that the amino acid-signal transduction
pathway consists of a series of steps which include the
post-transcriptional regulation of amino acid transporter genes.
Volume 272, Number 32,
Issue of August 8, 1997
pp. 19951-19957
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
Department of Nutrition, Case Western
Reserve University School of Medicine, Cleveland, Ohio 44106 and
the § Department of Biochemistry and Molecular Biology, The
University of Florida College of Medicine,
Gainesville, Florida 32610-0245
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