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Perforin-1 (PRF1) is a calcium-dependent pore-forming immune protein encoded by the PRF1 gene and found predominantly in cytotoxic T lymphocytes (CTLs) and natural killer (NK) cells. Upon immune cell activation, perforin is released from cytolytic granules and inserts into the target cell membrane, oligomerizing to form transmembrane pores. These pores allow the rapid entry of pro-apoptotic granzymes, leading to programmed cell death (apoptosis) of infected, malignant, or otherwise abnormal cells. The protein is structurally homologous to complement component C9 and contains a MACPF domain critical for pore formation. Mutations in PRF1 underlie familial hemophagocytic lymphohistiocytosis type 2 and contribute to impaired immune surveillance, with increased risk of immune dysregulation and cancer.
Not applicable for approved drugs; experimental agents or research inhibitors may act by blocking PRF1 expression, polymerization, or pore-forming function.
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