Molecular Mechanisms of Protein Kinase C-induced Apoptosis in Prostate Cancer Cells

• Published in: BMB reports Vol. 38; no. 6; pp. 639 - 645
• Main Authors: Gonzalez-Guerrico, Anatilde M. (University of Pennsylvania School of Medicine, Philadelphia, PA, USA), Benavides, Fernando; Conti, Claudio J. (The University of Texas M.D. Anderson Cancer Center, Smithville, Texas, USA), Meshki, John (niversity of Pennsylvania School of Medicine, Philadelphia, PA, USA), Xiao, Liqing (niversity of Pennsylvania School of Medicine, Philadelphia, PA, USA), Kazanietz, Marcelo G. (niversity of Pennsylvania School of Medicine, Philadelphia, PA, USA), E-mail: marcelo@spirit.gcrc.upenn.edu
• Format: Journal Article
• Language: English
• Published: Korea (South) 30.11.2005
• Subjects: Androgens - metabolism; APOPTOSE; APOPTOSIS; Caspase 8 - metabolism; Cell Line, Tumor; Cell Survival; Gene Expression Regulation, Neoplastic; Humans; Isoenzymes - chemistry; Male; Models, Genetic; Phorbol esters; PKC; Prostate cancer cells; Prostatic Neoplasms - enzymology; Prostatic Neoplasms - pathology; Protein Kinase C - metabolism; Protein Kinase C-alpha - chemistry; Protein Kinase C-delta - chemistry; Protein Kinase C-epsilon - chemistry; Signal Transduction; TNFα
• ISSN: 1225-8687; 1976-6696; 0219-1024
• DOI: 10.5483/bmbrep.2005.38.6.639

Protein kinase C (PKC) isozymes, a family of serinethreonine kinases, are important regulators of cell proliferation and malignant transformation. Phorbol esters, the prototype PKC activators, cause PKC translocation to the plasma membrane in prostate cancer cells, and trigger an apoptotic response. Studies in recent years have determined that each member of the PKC family exerts different effects on apoptotic or survival pathways. PKCδ, one of the novel PKCs, is a key player of the apoptotic response via the activation of the p38 MAPK pathway. Studies using RNAi revealed that depletion of PKCδ totally abolishes the apoptotic effect of the phorbol ester PMA. Activation of the classical PKCα promotes the dephosphorylation and inactivation of the survival kinase Akt.