{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nNeuroserpin, the protein encoded by SERPINI1, is a neuronal serine protease inhibitor that plays a crucial role in the central nervous system by regulating tissue‐type plasminogen activator (tPA) activity. By rapidly interacting with tPA, neuroserpin helps modulate processes such as synaptic development, plasticity, and protection against excitotoxicity. Its expression is enriched in various brain regions and is dynamically regulated during development, ensuring proper neuronal migration and circuit formation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "5"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMutations in SERPINI1 underlie a group of neurodegenerative disorders collectively exemplified by familial encephalopathy with neuroserpin inclusion bodies (FENIB). In these conditions, missense mutations (e.g., S49P and the Portland variant) compromise protein folding, leading to retention of mutant neuroserpin in the endoplasmic reticulum. Misfolded neuroserpin molecules polymerize or become trapped in a latent conformation, eliciting cellular stress responses—including non‐canonical activation of NF‑κB—and ultimately contributing to neurodegeneration and dementia, sometimes accompanied by myoclonic epilepsy."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "6", "end_ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nNeuroserpin is also intimately linked to Alzheimer’s disease pathophysiology. In the Alzheimer brain, increased neuroserpin levels and the formation of tPA–neuroserpin complexes are thought to curtail plasmin activity, thereby reducing amyloid‑β clearance. Moreover, neuroserpin can bind directly to amyloid‑β peptides, altering their aggregation and mitigating cytotoxicity. These interactions highlight a dual role for neuroserpin in both proteolytic regulation and the modulation of amyloid pathology."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "17"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its neuroprotective actions, circulating neuroserpin levels have been investigated in the context of cerebral ischemia and stroke. Elevated serum neuroserpin correlates with favorable outcomes in patients with acute ischemic events, and experimental models indicate that exogenous neuroserpin administration can reduce infarct size and neuronal apoptosis even in tissues independent of tPA activity. Moreover, specific SERPINI1 gene polymorphisms have been associated with altered stroke risk among young individuals."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "18", "end_ref": "21"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its roles in mature neurons, neuroserpin is crucial during brain development and may influence neuropsychiatric conditions. SERPINI1 lies in a genomic context with genes such as PDCD10 under common regulatory control, and its expression in the hippocampus is critical for timely neurogenesis and synaptic maturation. Altered neuroserpin expression or activity might also contribute to disorders like bipolar disease, suggesting that proper regulation of SERPINI1 is essential for both developmental and adult brain function."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "22", "end_ref": "24"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRecent studies have further revealed non‐neuronal roles for neuroserpin. In colorectal cancer cell lines, SERPINI1 has been implicated in mediating epithelial–mesenchymal transition, while in the immune system neuroserpin participates in the orchestration of immune synapse formation and T cell activation. These findings expand the functional repertoire of SERPINI1 beyond the confines of classical neurobiology."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "25"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBiophysical investigations have provided key insights into the conformational dynamics of neuroserpin, elucidating the mechanisms that govern its folding, polymerization, and latent state formation. Detailed studies using refolding assays, glycosylation mapping, thermal denaturation, hydrogen–deuterium exchange, and molecular dynamics simulations have characterized both the native inhibitory form and the aberrant polymeric species. These analyses underscore the delicate balance between neuroserpin’s functional conformation and its propensity to misfold, a balance that is perturbed in pathogenic variants."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "27", "end_ref": "34"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdditionally, oxidative modifications of neuroserpin can alter its local conformation and inhibitory activity, further impacting its neuroprotective potential. Such post‐translational modifications may represent another level of regulation that influences both its normal function and its contribution to serpinopathies."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "35"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Karen Barker-Carlson, Daniel A Lawrence, Bradford S Schwartz "}, {"type": "b", "children": [{"type": "t", "text": "Acyl-enzyme complexes between tissue-type plasminogen activator and neuroserpin are short-lived in vitro."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M207740200"}], "href": "https://doi.org/10.1074/jbc.M207740200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12228252"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12228252"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Manuel Yepes, Daniel A Lawrence "}, {"type": "b", "children": [{"type": "t", "text": "Neuroserpin: a selective inhibitor of tissue-type plasminogen activator in the central nervous system."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Thromb Haemost (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1160/TH03-12-0766"}], "href": "https://doi.org/10.1160/TH03-12-0766"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "14983220"}], "href": "https://pubmed.ncbi.nlm.nih.gov/14983220"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Tambet Teesalu, Andres Kulla, Aadu Simisker, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Tissue plasminogen activator and neuroserpin are widely expressed in the human central nervous system."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Thromb Haemost (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1160/TH02-12-0310"}], "href": "https://doi.org/10.1160/TH02-12-0310"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15269833"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15269833"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Stefano Ricagno, Sonia Caccia, Graziella Sorrentino, et al. 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