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J Biol Chem, Vol. 273, Issue 22, 13399-13402, May 29, 1998
2-Macroglobulin to the 2-Macroglobulin
Signaling Receptor Activates Phosphatidylinositol 3-Kinase
From the Department of Pathology, Duke University Medical Center,
Durham, North Carolina 27710
Ligation of the
2-macroglobulin (2M) signaling
receptor by receptor-recognized forms of 2M
(2M*) initiates mitogenesis secondary to increased
intracellular Ca2+. We report here that ligation of the
2M signaling receptor also causes a 1.5-2.5-fold
increase in wortmannin-sensitive phosphatidylinositol 3-kinase (PI3K)
activity as measured by the quantitation of phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 formation was
2M* concentration-dependent with a maximal
response at ~50 pM ligand concentration. The peak formation of PIP3 occurred at 10 min of incubation. The
2M receptor binding fragment mutant K1370R which binds
to the 2M signaling receptor activating the signaling
cascade, increased PIP3 formation by 2-fold. The mutant
K1374A, which binds very poorly to the 2M signaling
receptor, did not cause any increase in PIP3 formation. 2M*-induced DNA synthesis was inhibited by
wortmannin.
1,2Bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acetoxymethylester a chelator of intracellular
Ca2+, drastically reduced 2M*-induced
increases in PIP3 formation. We conclude that PI3K is
involved in 2M*-induced mitogenesis in macrophages and
intracellular Ca2+ plays a role in PI3K activation.
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