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J Biol Chem, Vol. 273, Issue 51, 33893-33896, December 18, 1998
From the Department of Cancer Biology, The Lerner Research
Institute, Cleveland Clinic Foundation, Cleveland, Ohio 44195
Binding of interleukin (IL)-4 to its
transmembrane receptor results in the Jak-mediated tyrosine
phosphorylation of a number of protein components of the IL-4 signaling
cascade, including Jak1, Jak2, Jak3, Tyk2, IL-4R
, IRS-1, IRS-2, and
Stat6 in appropriate cell types. However, the protein-tyrosine
phosphatases (PTPs) that dephosphorylate these proteins and terminate
signaling remained unidentified. We have noted that
IL-4-dependent activation of Stat6 is sustained longer in
fibroblasts than in lymphoid cells. Because Shp-1, an SH2
domain-containing PTP, is expressed primarily in hematopoietic cells,
we examined whether Shp-1 activity could regulate
IL-4-dependent cell signaling. Expression of an Shp-1 transgene in NIH 3T3 cells markedly reduces both
IL-4-dependent Stat6 activation and Stat6-mediated
transcription of IL-4-responsive genes. In accord with this, IL-4
treatment of bone marrow-derived macrophages from viable
motheaten mice that express substantially reduced levels of Shp-1
activity show remarkably enhanced activation of Stat6. In addition,
Stat6 activation by IL-4 is significantly enhanced in pre-B cells
derived from motheaten (Shp-1 null mutant) mice compared
with normal pre-B cells derived from control animals. These data
clearly implicate Shp-1 in the negative regulation of the
IL-4/IL-13-activated Jak-Stat pathway.
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