{"id":"f4d5ae3e-e272-5674-9975-25e24b1884fb","stable_key":"be889add-cec8-500b-be89-676431432a70:mn-clin-zip8-glycosylation","predicate":"impaired","statement":"The genetic investigation linked SLC39A8 variants, very low blood manganese and type II glycosylation abnormalities.","claim_class":"observational","status":"source_derived_draft","evidence_grade":"ungraded","direction":"negative","is_public":true,"mechanism_event_id":"aed43482-54fd-5075-bfdd-c3c629331100","mechanism_event_label":"A transport defect can deprive sugar-building enzymes of manganese.","subject":{"id":"fa612614-e2e4-5c16-b6a3-690c2d78effe","slug":"human-slc39a8-deficiency","display_name":"Human SLC39A8 transport deficiency","entity_type_key":"cellular_process"},"object":{"id":"7781d1ed-44c5-5dc4-9a18-d6ff7d08cb98","slug":"transferrin-glycosylation","display_name":"Transferrin glycosylation","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"aed43482-54fd-5075-bfdd-c3c629331100","stable_key":"be889add-cec8-500b-be89-676431432a70:mn-clin-zip8-glycosylation-event","event_type":"observed_intervention","label":"A transport defect can deprive sugar-building enzymes of manganese.","description":"The genetic investigation linked SLC39A8 variants, very low blood manganese and type II glycosylation abnormalities.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"059eea33-6e24-58ca-970f-014e2e65df77","slug":"slc39a8","display_name":"Human ZIP8 (SLC39A8)","entity_type_key":"protein"},"role":"affected_protein","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"c9dd1749-dbc5-5e9a-9b18-a005c345b261","slug":"blood-manganese-concentration","display_name":"Blood manganese concentration (specimen not further specified)","entity_type_key":"cellular_process"},"role":"low_marker","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"a76bbd5b-08c9-5d74-8b6f-d69502ffa655","slug":"udp-galactose","display_name":"UDP-galactose","entity_type_key":"small_molecule"},"role":"related_substrate","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"fa612614-e2e4-5c16-b6a3-690c2d78effe","slug":"human-slc39a8-deficiency","display_name":"Human SLC39A8 transport deficiency","entity_type_key":"cellular_process"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"7781d1ed-44c5-5dc4-9a18-d6ff7d08cb98","slug":"transferrin-glycosylation","display_name":"Transferrin glycosylation","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"availability_state","value_text":"machinery_impairment","comparator":null,"unit":null,"notes":"Imported condition classification; unverified.","entity":null},{"dimension":"cross_nutrient","value_text":"Human ZIP8 (SLC39A8) (affected_protein); Blood manganese concentration (specimen not further specified) (low_marker); UDP-galactose (related_substrate)","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/manganese-clinical-sources/park2015.abstract.txt\", \"locator\": \"Indexed primary abstract\", \"file_sha256\": \"c4e7009c947d1854370f8c9f62c206a8c2190b2e23099a5b991b01465321023d\", \"start_char\": 0, \"end_char\": 1348, \"text_sha256\": \"c4e7009c947d1854370f8c9f62c206a8c2190b2e23099a5b991b01465321023d\", \"text_characters\": 1348}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Genetic investigation of two individuals with SLC39A8-CDG","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Affected individuals with compound heterozygous SLC39A8 variants.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Inherited transport failure is distinct from dietary shortage. The study supports hypogalactosylation but does not directly measure activity of every manganese enzyme in every tissue.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Manganese research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"manganese","display_name":"Manganese","entity_type_key":"nutrient_element"}},{"dimension":"organism","value_text":"Homo sapiens","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"A transport defect can deprive sugar-building enzymes of manganese.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[mn-clin-park2015] SLC39A8 Deficiency: A Disorder of Manganese Transport and Glycosylation. 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The study supports hypogalactosylation but does not directly measure activity of every manganese enzyme in every tissue.\nexposure: Affected individuals with compound heterozygous SLC39A8 variants.\ncross_nutrient: Human ZIP8 (SLC39A8) (affected_protein); Blood manganese concentration (specimen not further specified) (low_marker); UDP-galactose (related_substrate)\nevidence_span: {\"source_cache\": \"artifacts/manganese-clinical-sources/park2015.abstract.txt\", \"locator\": \"Indexed primary abstract\", \"file_sha256\": \"c4e7009c947d1854370f8c9f62c206a8c2190b2e23099a5b991b01465321023d\", \"start_char\": 0, \"end_char\": 1348, \"text_sha256\": \"c4e7009c947d1854370f8c9f62c206a8c2190b2e23099a5b991b01465321023d\", \"text_characters\": 1348}\n[mn-clin-park2015] SLC39A8 Deficiency: A Disorder of Manganese Transport and Glycosylation. 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