{"id":"2743d6f3-2fc0-55b4-8a71-534751d3c8cb","stable_key":"5d8e27d8-6a74-5560-827f-3f90908bbc34:ala-lipt1-lactate-partial-response","predicate":"reduces_in_patient_cells","statement":"Lipoic-acid exposure lowered lactate release from the studied LIPT1-deficient fibroblasts, while control-cell lactate increased.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"098f8725-0368-5381-8e53-f444f1722d38","mechanism_event_label":"The same exposure changed this marker in opposite directions depending on the cells.","subject":{"id":"ab091982-3acb-5a87-80fb-85dfe292c1e0","slug":"lipoic-acid","display_name":"Lipoic acid","entity_type_key":"small_molecule"},"object":{"id":"69c08597-ba20-54d0-9bd1-b557f719217f","slug":"fibroblast-lactate-release","display_name":"Fibroblast lactate release","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"098f8725-0368-5381-8e53-f444f1722d38","stable_key":"5d8e27d8-6a74-5560-827f-3f90908bbc34:ala-lipt1-lactate-partial-response-event","event_type":"biochemical_relationship","label":"The same exposure changed this marker in opposite directions depending on the cells.","description":"Lipoic-acid exposure lowered lactate release from the studied LIPT1-deficient fibroblasts, while control-cell lactate increased.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"a044660b-d63d-5adb-9b1f-ac9c2b8901bd","slug":"lipt1","display_name":"Human lipoyl amidotransferase / LIPT1","entity_type_key":"protein"},"role":"impaired_machinery","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"ab091982-3acb-5a87-80fb-85dfe292c1e0","slug":"lipoic-acid","display_name":"Lipoic acid","entity_type_key":"small_molecule"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"69c08597-ba20-54d0-9bd1-b557f719217f","slug":"fibroblast-lactate-release","display_name":"Fibroblast lactate release","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"availability_state","value_text":"machinery_impairment","comparator":null,"unit":null,"notes":"Imported condition classification; unverified.","entity":null},{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/ala-research/24341803.fulltext.txt\", \"locator\": \"Exact primary full-text span; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"44f3fc89f065e58c1deb82f02c93a3654504f002fbc051d00a7703d3fbe6764b\", \"start_char\": 19977, \"end_char\": 20689, \"text_sha256\": \"3a495a2251965512793b341794c86b5caedc8525754344b8bba51281e7802a79\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"LIPT1 patient fibroblasts with supplementation and genetic complementation","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Lipoic acid 10 or 100 micromolar for three weeks","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Partial biochemical changes do not establish restored lipoylation or clinical efficacy. Historical pathway speculation is not imported as current enzymology.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"lipoic-acid","display_name":"Lipoic acid","entity_type_key":"small_molecule"}},{"dimension":"organism","value_text":"Human","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"The same exposure changed this marker in opposite directions depending on the cells.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[ala-p24341803] Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase. (2013). https://pubmed.ncbi.nlm.nih.gov/24341803/ DOI: 10.1186/1750-1172-8-192","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Patient and control fibroblasts","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"trigger_kind","value_text":"machinery_impairment","comparator":null,"unit":null,"notes":"Imported condition classification; unverified.","entity":null}],"evidence":[{"id":"36a3bb0f-e1e1-5e6a-a6f6-fac0e390d150","evidence_kind":"source_excerpt","locator":"Lines 481-492","start_line":481,"end_line":492,"excerpt":"### ala-lipt1-lactate-partial-response\nLipoic-acid exposure lowered lactate release from the studied LIPT1-deficient fibroblasts, while control-cell lactate increased.\nCondition category: machinery_impairment\nnutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: The same exposure changed this marker in opposite directions depending on the cells.\norganism: Human\ntissue_or_cell_type: Patient and control fibroblasts\nexperimental_model: LIPT1 patient fibroblasts with supplementation and genetic complementation\nlimitations: Partial biochemical changes do not establish restored lipoylation or clinical efficacy. Historical pathway speculation is not imported as current enzymology.\nexposure: Lipoic acid 10 or 100 micromolar for three weeks\nevidence_span: {\"source_cache\": \"artifacts/ala-research/24341803.fulltext.txt\", \"locator\": \"Exact primary full-text span; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"44f3fc89f065e58c1deb82f02c93a3654504f002fbc051d00a7703d3fbe6764b\", \"start_char\": 19977, \"end_char\": 20689, \"text_sha256\": \"3a495a2251965512793b341794c86b5caedc8525754344b8bba51281e7802a79\"}\n[ala-p24341803] Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase. (2013). https://pubmed.ncbi.nlm.nih.gov/24341803/ DOI: 10.1186/1750-1172-8-192","model_system":"LIPT1 patient fibroblasts with supplementation and genetic complementation","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [ala-p24341803] Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase. 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