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Phosphatidylinositol-3-kinase activity is required for the anti-ig-
mediated growth inhibition of a human B-lymphoma cell line
M Beckwith, RG Fenton, IM Katona and DL Longo
Biological Carcinogenesis and Development Program, Science Applications
International Corporation/Frederick, MD, USA.
Stimulation of B lymphocytes through the Ig receptor initiates a cascade of
biochemical changes, which can ultimately lead to either activation and
growth, or cell-cycle arrest and cell death. One of the critical events
that occurs in both cases is the activation of tyrosine kinases, and the
resulting phosphorylation of a variety of proteins on tyrosine residues. In
this report we identify one of the substrates of phosphorylation as the
85-kD subunit of the enzyme phosphatidylinositol- 3 kinase (PI3K), and show
that both anti-IgM and anti-IgD stimulation results in an increase in the
anti-phosphotyrosine-precipitable PI3K activity. Furthermore, we show that
the potent and specific inhibitor of PI3K, Wortmannin, can completely
abrogate anti-Ig-mediated growth inhibition without affecting tyrosine
kinase induction or protein kinase C (PKC) activation. Treatment of intact
cells with Wortmannin results in an irreversible decrease in
anti-Ig-induced PI3K activity, suggesting that the effect of Wortmannin on
anti-Ig-mediated growth inhibition is caused by its inactivation of PI3K
activity. Taken together, these data show that activation of PI3K is a
critical component of the anti-Ig-initiated signaling cascade that leads to
growth inhibition of human B lymphoma cells.
Volume 87,
Issue 1,
pp. 202-210,
01/01/1996
Copyright © 1996 by The American Society of Hematology
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