{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSERPINB9, also known as proteinase inhibitor 9 (PI‐9), is an intracellular serpin that selectively blocks granzyme B activity, thereby preventing granzyme B–mediated apoptosis. In cytotoxic lymphocytes—including CD8⁺ T cells and natural killer (NK) cells—as well as in antigen‐presenting cells such as dendritic cells and mesenchymal stem cells, SERPINB9 is expressed to protect these cells against self‐inflicted cell death during degranulation. Moreover, nonimmune cells (for example, those in the placenta or transplanted tissues) upregulate SERPINB9 as an intrinsic mechanism to avoid collateral damage from granzyme B released from attacking lymphocytes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "9"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the setting of infection and inflammation, SERPINB9 expression is dynamically regulated. During viral infections (for example, cytomegalovirus) and bacterial challenges such as Mycobacterium tuberculosis, SERPINB9 is induced—and can even be detected in complexes with granzyme B—in ways that modulate effector cell activity. In addition, variants that compromise SERPINB9’s ability to inhibit caspase 1 have been linked to autoinflammatory disease, underscoring its role in fine‐tuning immune responses and preventing excessive inflammation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nA prominent role for SERPINB9 has emerged in tumor immune evasion and resistance to therapy. Numerous studies have shown that malignant cells—including those from lung, breast, prostate, testicular, and hematological cancers—upregulate SERPINB9 to neutralize granzyme B, thereby preventing apoptosis induced by cytotoxic lymphocytes as well as by engineered immunotherapies (e.g., CAR T cells). Modulatory factors such as estrogen and dietary components (for example, genistein) can further enhance SERPINB9 expression in tumor cells, a feature that correlates with more aggressive disease, treatment resistance, and poor prognosis. In addition, elevated SERPINB9 has been identified in cancer stem cell populations and metastatic lesions, reinforcing its potential as both a prognostic biomarker and a therapeutic target in oncology."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "14", "end_ref": "31"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its roles in immune protection and tumor resistance, SERPINB9 is subject to multifaceted regulatory mechanisms that include epigenetic modifications and redox‐dependent modulation. Altered DNA methylation at SERPINB9 loci has been observed in diverse contexts—from circulating T cells associated with post‐transplant squamous cell carcinoma risk to long‐term meditators with markers of healthy aging. Moreover, cellular stress signals such as reactive oxygen species can inactivate SERPINB9, thereby lowering the threshold for granzyme B–mediated cell death and influencing immune cell function in chronic inflammatory or autoimmune disorders."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "32", "end_ref": "35"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Claire E Hirst, Marguerite S Buzza, Catherina H Bird, et al. 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