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J Biol Chem, Vol. 273, Issue 6, 3173-3179, February 6, 1998
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From the Departments of The insulin-stimulated uptake of
2-(methylamino)isobutyric acid (MeAIB), a nonmetabolizable
substrate for system A, in 3T3-L1 adipocytes was investigated. As cells
took on a more adipogenic phenotype, the insulin-stimulated
versus the saturable basal MeAIB uptake increased by
5-fold. The induced transport activity showed properties characteristic
of system A, with a Km value of 190 µM. The half-life of the induced system A activity was independent of de novo mRNA and protein synthesis and
was not accelerated by ambient amino acids, therefore, it was
mechanistically distinct from the previously described adaptive and
hormonal regulation of system A. Inhibition of mitogen-activated
protein kinase kinase by PD98059, Ras farnesylation by PD152440 and
B581, p70S6K by rapamycin, and phosphatidylinositol
3-kinase (PI 3 Molecular Biology and
¶ Cell Biology, Parke-Davis Pharmaceutical Research Division
of Warner Lambert Co., Ann Arbor, Michigan 48105
-K) by wortmannin and LY294002 revealed that only
wortmannin and LY294002 inhibited the insulin-induced MeAIB uptake with
IC50 values close to that previously reported for
inhibition of PI 3-K. These results suggest that the
Ras/mitogen-activated protein kinase and pp70S6K insulin
signaling pathways are neither required nor sufficient for insulin
stimulation of MeAIB uptake, and activation of PI 3-K or a
wortmannin/LY294002-sensitive pathway may play an important role in
regulation of system A transport by insulin in 3T3-L1 cells.
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