Figure 2: Prostate-selective therapeutics designed to induce rapid apoptosis by dephosphorylating BAD and downregulating Mcl-1. Inhibition of PI3-kinase with latent inhibitor activated by prostate-specific antigen protease leads to dephosphorylation of BAD. This allows BAD to bind and neutralize antiapoptotic proteins Bcl_XL and Bcl2, but not Mcl-1. Mcl-1 protein is characterized by rapid turnover. Chimera of antigen binding domain of J591PE antibodies against prostate-specific membrane antigen and translocation and catalytic domains of Pseudomonas aeruginosa exotoxin selectively inhibits protein synthesis in prostate cells and downregulate Mcl-1 expression. Combined loss of BAD phosphorylation and Mcl-1 expression induces rapid apoptosis in PTEN-deficient prostate cancer cells.^27,43