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J Biol Chem, Vol. 273, Issue 43, 28178-28184, October 23, 1998
From the Amino acids have been identified as important
signaling molecules involved in pancreatic
Branched-chain Amino Acids Are Essential in the Regulation of
PHAS-I and p70 S6 Kinase by Pancreatic
-Cells
A POSSIBLE ROLE IN PROTEIN TRANSLATION AND MITOGENIC
SIGNALING
,,,,
Department of Pathology, Washington
University School of Medicine, St. Louis, Missouri 63110 and the
§ Department of Pharmacology, University of Virginia School
of Medicine, Charlottesville, Virginia 22908
-cell proliferation,
although the cellular mechanism responsible for this effect is not well
defined. We previously reported that amino acids are required for
glucose or exogenous insulin to stimulate phosphorylation of PHAS-I
(phosphorylated heat- and acid-stable protein regulated by insulin), a
recently discovered regulator of translation initiation during cell
mitogenesis. Here we demonstrate that essential amino acids, in
particular branched-chain amino acids (leucine, valine, and
isoleucine), are largely responsible for mediating this effect. The
transamination product of leucine, 
-ketoisocaproic acid, also
stimulates PHAS-I phosphorylation although the transamination products
of isoleucine and valine are ineffective. Since amino acids are
secretagogues for insulin secretion by -cells, we investigated
whether endogenous insulin secreted by -cells is involved.
Interestingly, branched-chain amino acids stimulate phosphorylation of
PHAS-I independent of endogenous insulin secretion since genistein (10 µM) and herbimycin A (1 µM), two
tyrosine kinase inhibitors in the insulin signaling pathway, exert no
effect on amino acid-induced phosphorylation of PHAS-I. Furthermore,
branched-chain amino acids retain their ability to induce
phosphorylation of PHAS-I under conditions that block insulin secretion
from -cells. In exploring the signaling pathway responsible for
these effects, we find that rapamycin (25 nM) inhibits the
ability of branched-chain amino acids to stimulate the phosphorylation
of PHAS-I and p70s6 kinase, suggesting that the mammalian
target of rapamycin signaling pathway is involved. The branched-chain
amino acid, leucine, also exerts similar effects on PHAS-I
phosphorylation in isolated pancreatic islets. In addition, we find
that amino acids are necessary for insulin-like growth factor (IGF-I)
to stimulate the phosphorylation of PHAS-I indicating that a
requirement for amino acids may be essential for other -cell growth
factors in addition to insulin and IGF-I to activate this signaling
pathway. We propose that amino acids, in particular branched-chain
amino acids, may promote -cell proliferation either by stimulating
phosphorylation of PHAS-I and p70s6k via the mammalian
target of rapamycin pathway and/or by facilitating the proliferative
effect mediated by growth factors such as insulin and IGF-I.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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