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(2010). https://pubmed.ncbi.nlm.nih.gov/20207735/ DOI: 10.1074/jbc.m109.077925","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified enzyme and osmotic-stress cell assays","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"eb89b4f6-46b2-5fe4-842c-6b439013db99","evidence_kind":"source_excerpt","locator":"Lines 646-657","start_line":646,"end_line":657,"excerpt":"### choline-aldh7-osmotic\nHuman ALDH7A1 expression attenuated apoptosis caused by high extracellular sucrose or sodium chloride in CHO cells.\nCondition category: normal\nnutrient_topic: Choline research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: The enzyme protected these cells during osmotic stress.\norganism: Human ALDH7A1; Chinese hamster ovary expression host\ntissue_or_cell_type: Purified enzyme and osmotic-stress cell assays\nexperimental_model: Purified recombinant human enzyme and CHO-cell expression\nlimitations: The enzyme also detoxifies other aldehydes; betaine is a proposed contributor, not an isolated mediator in this endpoint.\nexposure: Betaine aldehyde substrate; increased extracellular sucrose or NaCl\nevidence_span: {\"source_cache\": \"artifacts/choline-research/20207735.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"510558afae2825079b269c8a4ee3f16114ab8d7f6c357c1a085ec14f1924e5e5\", \"start_char\": 0, \"end_char\": 1582, \"text_sha256\": \"510558afae2825079b269c8a4ee3f16114ab8d7f6c357c1a085ec14f1924e5e5\"}\n[choline-p20207735] Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in cellular defense against hyperosmotic stress. 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