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Am J Physiol Cell Physiol 284: C119-C126, 2003. First published September 11, 2002; doi:10.1152/ajpcell.00247.2002
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Vol. 284, Issue 1, C119-C126, January 2003

Elevated L-PGDS activity contributes to PMA-induced apoptosis concomitant with downregulation of PI3-K

Louis Ragolia1,2, Thomas Palaia1, Enesa Paric1, and John K. Maesaka1,2

1 Cellular Biology Laboratory, Winthrop-University Hospital, Mineola 11501; and 2 School of Medicine, State University of New York, Stony Brook, New York 11794

Recently we demonstrated the induction of apoptosis by the addition of recombinant lipocalin-type prostaglandin D2 synthase (L-PGDS) to the culture medium of LLC-PK1 cells. Because protein kinase C (PKC) has been shown to be involved in the apoptotic process of various cell types, we examined the potential role of L-PGDS in phorbol 12-myristate 13-acetate (PMA)-induced apoptosis. We report here the enzymatic activation and phosphorylation of L-PGDS in response to phorbol ester in cell culture and the direct phosphorylation of recombinant L-PGDS by PKC in vitro. Treatment of cells with PMA or L-PGDS decreased phosphatidylinositol 3-kinase (PI3-K) activity and concomitantly inhibited protein kinase B (PKB/Akt) phosphorylation, which led to the hypophosphorylation and activation of Bad. In addition, hypophosphorylation of retinoblastoma protein was also observed in response to L-PGDS-induced apoptosis. Cellular depletion of L-PGDS levels by using an antisense RNA strategy prevented PI3-K inactivation by phorbol ester and inhibited caspase-3 activation and apoptosis. We conclude that phorbol ester-induced apoptosis is mediated by L-PGDS phosphorylation and activation by PKC and is accompanied by inhibition of the PI3-K/PKB anti-apoptotic signaling pathways.

lipocalin-type prostaglandin D2 synthase; phorbol 12-myristate 13-acetate; phosphatidylinositol 3-kinase; apoptosis; LLC-PK1; protein kinase C; beta -trace protein


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