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Volume 272, Number 36, Issue of September 5, 1997 pp. 22751-22757
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Retinoblastoma Protein-dependent Growth Signal Conflict and Caspase Activity Are Required for Protein Kinase C-signaled Apoptosis of Prostate Epithelial Cells

(Received for publication, March 6, 1997, and in revised form, July 3, 1997)

Xin Zhao Dagger , Jürgen E. Gschwend § , C. Thomas Powell § , Rosalinda G. Foster , Kathleen C. Day Dagger and Mark L. Day Dagger

From the Dagger  Department of Surgery, Section of Urology and The University of Michigan Comprehensive Cancer Center, Ann Arbor, Michigan 48109, § Memorial Sloan-Kettering Cancer Center, New York, New York 10021, and the  Department of Medicine and Cell Biology, Washington University School of Medicine, St. Louis, Missouri 63110

Both protein kinase C and the retinoblastoma tumor suppressor protein have been linked to the regulation of cell growth and cell death, suggesting the differential roles these factors play in mediating cell fate. In some cells, protein kinase C-induced activation of the retinoblastoma protein results in G1 arrest. However, inducible overexpression and activation of the protein kinase Calpha isozyme or the addition of 12-O-tetradecanoylphorbol-13-acetate in the prostate epithelial cell line, LNCaP, resulted in apoptosis preceded by induction of p21 and dephosphorylation of the retinoblastoma protein. Consistent with a role for the retinoblastoma growth suppressor protein in protein kinase C-induced apoptosis, DU145 cells, which do not express functional retinoblastoma protein or LNCaP cells, which have been transfected with the retinoblastoma inhibitor, E1a, were resistant to apoptosis. LNCaP apoptosis was initiated by a unique conflict between the growth-suppressive activity of the retinoblastoma protein and growth-promoting mitogenic signals. Thus, when this conflict was prevented by serum depletion, apoptosis was suppressed. The caspase family of cysteine proteases is believed to encompass the execution machinery of mammalian apoptosis, and addition of the cell-permeable caspase inhibitor, Z-Val-Ala-Asp-fluoromethylketone, afforded nearly total protection from protein kinase C-signaled apoptosis. This protection correlated with the total loss of caspase activity as measured by the proteolytic cleavage of nuclear poly(ADP-ribose) polymerase. On the basis of these results, we propose that protein kinase C regulates a novel cell death pathway that is initiated by a cellular conflict between retinoblastoma growth-suppressive signals and serum mitogenic signals in proliferating prostate epithelial cells and that is executed by the caspase family of cysteine proteases.


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