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(Received for publication, October 28,
1994; and in revised form, December 12, 1994) The regulation of sodium-dependent L-alanine transport
is described for the first time in intestinal cells. Substrate analogue
inhibition patterns and Dixon analyses indicated that uptake occurred
via transport system B, an epithelial cell variant of systems
B
Volume 270,
Number 8,
Issue of February 24, 1995 pp. 3582-3587
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
and ASC. System B served >95% of the
Na
-dependent alanine uptake in both undifferentiated
(2 days postpassaging) and differentiated (>9 days postpassaging)
states of the human Caco-2 cultured intestinal cell line.
(Methylamino)isobutyric acid-inhibitable system A transport accounted
for <5% of total alanine uptake. System B activity was greater in
undifferentiated cells compared with the differentiated state, and
activity at any differentiation state was stimulated by
12-O-tetradecanoylphorbol-13-acetate (TPA). The maximal
stimulation, determined by TPA dose-response/exposure time data, was
attributable to a change in cell transport capacity (V
), with K
unaffected. The V
of system B was
greater in 2-day-old cells (2.79 ± 0.21 nmol min
mg of protein
; K
= 164 ± 26 µM alanine),
decreasing to V
= 0.51 ± 0.03 nmol min
mg of protein
(K
= 159 ± 14
µM) in 9-day-old cells. Regardless of differentiation
status, the sodium-activation Hill coefficient was 1.06 ± 0.10,
and the alanine passive diffusion permeability coefficient was 0.53
± 0.08 µl min
mg of
protein
. Phorbol ester up-regulated the V
of system B in 2-day-old cells to V
= 6.32 ± 0.37 nmol
min
mg of protein
(K
= 169 ± 18
µM), and in 9-day-old cells to V
= 1.42 ± 0.05 nmole min
mg of protein
(K
= 180 ± 10 µM). Phorbol ester
stimulation of transport occurred after at least 6 h of continual
exposure, and was blocked by the protein kinase C inhibitors
chelerythrine or photoactivated calphostin C. Protein synthesis
inhibitors cycloheximide and actinomycin D each blocked the phorbol
ester up-regulation of system B activity. It is concluded that Caco-2
cells regulate carrier-mediated sodium-dependent transport of L-alanine by changing the membrane capacity to transport
alanine via system B and that this regulation involves de novo protein synthesis under the control of protein kinase C.
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