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Caspase-9 is an initiator caspase that triggers the intrinsic pathway of apoptosis, while protein phosphatase 2A (PP2A) is a major cellular serine/threonine phosphatase regulating several cell processes, including cell growth, DNA repair, and survival. Their direct interaction modulates caspase-9 activation and, consequently, the induction of programmed cell death. In cancer, dysregulation of this interaction allows tumor cells to evade apoptosis. Therapeutic peptides, such as C9h and PEP-010, specifically target and disrupt the caspase-9/PP2A interaction to restore apoptosis selectively in tumor cells, representing a novel approach in oncological drug development[1][5][7]. This entry refers to a protein-protein interaction and not a single molecule or receptor; structured databases often require such details to be split into their respective protein components for standard annotation.
Cell-penetrating peptides (e.g., C9h, DPT-C9h, PEP-010) block or modulate the caspase-9/PP2A interaction, restore caspase-9 activation, and induce apoptosis in tumor cells without affecting healthy primary cells
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