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J Biol Chem, Vol. 273, Issue 12, 7099-7106, March 20, 1998
From INSERM U151, Institut Louis Bugnard, IFR 31, CHU Rangueil,
31403 Toulouse Cedex 04, France and § Institut Cochin de
Génétique Moléculaire, 75014 Paris, France
We have previously reported in Chinese hamster
ovary (CHO) cells expressing sst2 that activation of the sst2
somatostatin receptor inhibits insulin-induced cell proliferation by a
mechanism involving stimulation of a tyrosine phosphatase activity.
Here we show that the tyrosine phosphatase SHP-1 was associated with the insulin receptor (IR) at the basal level. Activation of IR by
insulin resulted in a rapid and transient increase of tyrosine phosphorylation of IR, its substrates IRS-1 and Shc, and also of SHP-1.
This was then followed by a rapid dephosphorylation of these molecules,
which was related to the insulin-induced increase of SHP-1 association
to IR and of SHP-1 activity. On the other hand, addition to insulin of
the somatostatin analogue, RC160, resulted in a higher and faster
increase of SHP-1 association to IR directly correlated with an
inhibition of phosphorylation of IR and its substrates, IRS-1 and Shc.
RC160 also induced a higher and more sustained increase in SHP-1
activity. Furthermore, RC160 completely suppressed the effect of
insulin on SHP-1 phosphorylation. Finally, in CHO cells coexpressing
sst2 and a catalytically inactive mutant SHP-1, insulin as well as
RC160 could no longer stimulate SHP-1 activity. Overexpression of the
SHP-1 mutant prevented the insulin-induced signaling to be terminated
by dephosphorylation of IR, suppressed the inhibitory effect of RC160
on insulin-induced IR phosphorylation, and abolished the cell
proliferation modulation by insulin and RC160. Our results suggest that
SHP-1 plays a role in negatively modulating insulin signaling by
association with IR. Furthermore, somatostatin inhibits the
insulin-induced mitogenic signal by accelerating and amplifying the
effect of SHP-1 on the termination of the insulin signaling
pathway.
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