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BCL2-related protein A1 (BFL-1) is a member of the anti-apoptotic BCL-2 protein family. It shares four BH domains that allow interaction with multiple pro-apoptotic partners and is primarily regulated by NF-κB and various inflammatory cytokines. BFL-1 is upregulated in several cancers and contributes to tumor cell survival and resistance to chemotherapy. Its function includes blocking mitochondrial cytochrome c release and caspase activation, enabling cell survival during immune activation and inflammation. BFL-1's rapid turnover and non-essential status for normal system homeostasis make it a promising therapeutic target for cancer, though no approved drugs directly target it yet. Its activity, expression, and splice variants are considered for biomarker development, especially within hematologic malignancies.
Anti-apoptotic effect: binds and neutralizes pro-apoptotic proteins (e.g., BIM, PUMA, NOXA, BIK, BID, HRK, BAK, BAX) via BH3-domain interactions. Reduces release of cytochrome c from mitochondria, inhibiting caspase activation. Acts downstream of NF-κB signaling, upregulated in response to inflammatory stimuli.
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