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J Biol Chem, Vol. 274, Issue 37, 26105-26112, September 10, 1999
From the Division of Biochemistry and Molecular Biology, School of
Biological Sciences, Southampton, SO16 7PX, United Kingdom
The protein-tyrosine phosphatase PTP
has been
proposed to play an important role in controlling the dephosphorylation
of a number of key signaling proteins and in regulating insulin
signaling. To examine the potential cellular functions and
physiological substrates of PTP, a potent phosphorothioate
oligonucleotide-based antisense strategy was developed that
specifically depleted endogenous PTP from 3T3-L1 adipocytes. The
antisense probe, AS1, achieved PTP depletion levels
normally of 
85% and which varied up to levels where PTP was not
detected at all. Elimination of PTP by 85% inhibited c-Src activity
by 80%. Abolishing PTP to levels undetected did not alter the
tyrosine dephosphorylation of the insulin receptor or insulin receptor
substrate proteins. Moreover, the ability of insulin to activate ERK2
or to stimulate DNA synthesis was not altered by AS1. It
is concluded that endogenous PTP is a key regulator of c-Src
activity in 3T3-L1 adipocytes and that PTP is not required for the
dephosphorylation of the insulin receptor or the insulin receptor
substrate proteins or for the regulation of several downstream insulin
signaling events in 3T3-L1 adipocytes. Finally, the development of the
antisense probe, AS1, provides an important molecular
tool of general applicability for further dissecting the roles and
precise targets of endogenous PTP.
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