{"id":"29d28efc-adbc-5464-9d13-08de5938e7ac","stable_key":"475ea55a-65e9-51c3-a539-738a6a8f683f:mangiferin-rpe-sod2","predicate":"preserves_expression_and_activity","statement":"Mangiferin opposed H2O2-associated loss of manganese superoxide dismutase expression and activity.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"a4397c2b-6e84-52c1-bf2f-760e5f13bed6","mechanism_event_label":"An enzyme that depends on manganese was part of the measured response.","subject":{"id":"2cfc0bd9-b5cc-58ab-852a-7705f3d8d47f","slug":"mangiferin","display_name":"Mangiferin","entity_type_key":"small_molecule"},"object":{"id":"eda566c2-d338-54b2-a872-0dd39daffcdf","slug":"sod2","display_name":"Human mitochondrial manganese superoxide dismutase / SOD2","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"a4397c2b-6e84-52c1-bf2f-760e5f13bed6","stable_key":"475ea55a-65e9-51c3-a539-738a6a8f683f:mangiferin-rpe-sod2-event","event_type":"biochemical_relationship","label":"An enzyme that depends on manganese was part of the measured response.","description":"Mangiferin opposed H2O2-associated loss of manganese superoxide dismutase expression and activity.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"2cfc0bd9-b5cc-58ab-852a-7705f3d8d47f","slug":"mangiferin","display_name":"Mangiferin","entity_type_key":"small_molecule"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"eda566c2-d338-54b2-a872-0dd39daffcdf","slug":"sod2","display_name":"Human mitochondrial manganese superoxide dismutase / SOD2","entity_type_key":"protein"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/mangiferin-research/38586992.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"3568135f9e3471d748a1f42c7ed136800b1cb9d017ebd9aa1522de71b71a72be\", \"start_char\": 0, \"end_char\": 1792, \"text_sha256\": \"3568135f9e3471d748a1f42c7ed136800b1cb9d017ebd9aa1522de71b71a72be\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Hydrogen-peroxide challenge with pharmacological HO-1 inhibition","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Mangiferin before H2O2 exposure","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Cell protection is not demonstrated retinal clinical efficacy; GPx isoforms unresolved and expression is not cofactor sufficiency.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Mangiferin research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"mangiferin","display_name":"Mangiferin","entity_type_key":"small_molecule"}},{"dimension":"organism","value_text":"Homo sapiens","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"An enzyme that depends on manganese was part of the measured response.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[mangiferin-p38586992] Activation of Heme Oxygenase-1 by Mangiferin in Human Retinal Pigment Epithelial Cells Contributes to Blocking Oxidative Damage. (2024). https://pubmed.ncbi.nlm.nih.gov/38586992/ DOI: 10.4062/biomolther.2023.175","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"ARPE-19 retinal pigment epithelial cells","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"04d68f26-6898-5043-ba32-868fec7bd4d4","evidence_kind":"source_excerpt","locator":"Lines 614-625","start_line":614,"end_line":625,"excerpt":"### mangiferin-rpe-sod2\nMangiferin opposed H2O2-associated loss of manganese superoxide dismutase expression and activity.\nCondition category: normal\nnutrient_topic: Mangiferin research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: An enzyme that depends on manganese was part of the measured response.\norganism: Homo sapiens\ntissue_or_cell_type: ARPE-19 retinal pigment epithelial cells\nexperimental_model: Hydrogen-peroxide challenge with pharmacological HO-1 inhibition\nlimitations: Cell protection is not demonstrated retinal clinical efficacy; GPx isoforms unresolved and expression is not cofactor sufficiency.\nexposure: Mangiferin before H2O2 exposure\nevidence_span: {\"source_cache\": \"artifacts/mangiferin-research/38586992.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"3568135f9e3471d748a1f42c7ed136800b1cb9d017ebd9aa1522de71b71a72be\", \"start_char\": 0, \"end_char\": 1792, \"text_sha256\": \"3568135f9e3471d748a1f42c7ed136800b1cb9d017ebd9aa1522de71b71a72be\"}\n[mangiferin-p38586992] Activation of Heme Oxygenase-1 by Mangiferin in Human Retinal Pigment Epithelial Cells Contributes to Blocking Oxidative Damage. 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