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Inhibition of SH2‐domain containing inositol phosphatase 2 (SHIP2) in insulin producing INS1E cells improves insulin signal transduction and induces proliferation
Author(s) -
Grempler Rolf,
Leicht Stefanie,
Kischel Ivonne,
Eickelmann Peter,
Redemann Norbert
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.11.066
Subject(s) - insulin receptor , signal transduction , insulin , phosphatase , protein kinase b , glycogen synthase , endocrinology , phosphorylation , medicine , inositol , microbiology and biotechnology , chemistry , biology , biochemistry , receptor , insulin resistance
Inhibition of the lipid phosphatase SH2‐domain containing inositol phosphatase 2 (SHIP2) in L6‐C10 muscle cells, in 3T3‐L1 adipocytes and in the liver of db/db mice has been shown to ameliorate insulin signal transduction and established SHIP2 as a negative regulator of insulin action. Here we show that SHIP2 inhibition in INS1E insulinoma cells increased Akt, glycogen synthase kinase 3 and extracellular signal‐regulated kinases 1 and 2 phosphorylation. SHIP2 inhibition did not prevent palmitate‐induced apoptosis, but increased cell proliferation. Our data raise the interesting possibility that SHIP2 inhibition exerts proliferative effects in β‐cells and further support the attractiveness of a specific inhibition of SHIP2 for the treatment of type 2 diabetes.