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Bisperoxovanadium compounds are potent PTEN inhibitors
Author(s) -
Schmid Annette C.,
Byrne Richard D.,
Vilar Ramón,
Woscholski Rüdiger
Publication year - 2004
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.2004.03.102
Subject(s) - pten , tensin , phosphatase , phosphorylation , protein tyrosine phosphatase , protein kinase b , ly294002 , cancer research , kinase , tyrosine phosphorylation , pi3k/akt/mtor pathway , chemistry , tyrosine , biochemistry , biology , microbiology and biotechnology , signal transduction
The tumour suppressor phosphatase and tensin homologue deleted on chromosome 10 (PTEN) shares homology with protein tyrosine phosphatases (PTPases). Similarly, bisperoxovanadium (bpV) molecules that are well‐established PTPase inhibitors were shown to inhibit PTEN, but at up to 100‐fold lower concentrations. The preference and potency of the bpVs towards PTEN was validated in vivo as demonstrated by: (i) an increase of Ser473 phosphorylation of protein kinase B (PKB) at similar low nanomolar doses, (ii) the lack of any effect on the PKB phosphorylation in the PTEN negative cell line UM‐UC‐3, (iii) the ability to rescue Ly294002‐induced phosphoinositide 3‐kinase inhibition and (iv) a lack of tyrosine phosphorylation at low nanomolar doses.