Acetaldehyde

availability_state

nutrient_deficiency Imported condition classification; unverified.

evidence_span

{"source_cache": "artifacts/alcohol-research/27531.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e30f315b327e70a22ed855a935921234fad553d9ed765578c0292446c7bace98", "start_char": 0, "end_char": 2014, "text_sha256": "e30f315b327e70a22ed855a935921234fad553d9ed765578c0292446c7bace98"}

experimental_model

Erythrocyte and hepatic experiments isolating acetaldehyde from ethanol

exposure

Acetaldehyde exposure with PLP measurement

limitations

A confirmatory mechanism study attributing the effect specifically to acetaldehyde.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Human and rat material

plain_language

The vitamin damage is done by the metabolite, which is why it tracks with how fast alcohol is oxidised.

primary_references

[alcohol-p27531] The role of acetaldehyde in mediating the deleterious effect of ethanol on pyridoxal 5'-phosphate metabolism. (1978). https://pubmed.ncbi.nlm.nih.gov/27531/ DOI: 10.1172/jci109128

tissue_or_cell_type

Erythrocytes and liver

trigger_kind

nutrient_deficiency Imported condition classification; unverified.

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 657–668

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Erythrocyte and hepatic experiments isolating acetaldehyde from ethanol · source_derived_draft · unverified_draft

### alcohol-acetaldehyde-mediates-b6 Acetaldehyde was shown to mediate the deleterious effect of ethanol on pyridoxal 5-phosphate metabolism. Condition category: nutrient_deficiency nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: The vitamin damage is done by the metabolite, which is why it tracks with how fast alcohol is oxidised. organism: Human and rat material tissue_or_cell_type: Erythrocytes and liver experimental_model: Erythrocyte and hepatic experiments isolating acetaldehyde from ethanol limitations: A confirmatory mechanism study attributing the effect specifically to acetaldehyde. exposure: Acetaldehyde exposure with PLP measurement evidence_span: {"source_cache": "artifacts/alcohol-research/27531.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e30f315b327e70a22ed855a935921234fad553d9ed765578c0292446c7bace98", "start_char": 0, "end_char": 2014, "text_sha256": "e30f315b327e70a22ed855a935921234fad553d9ed765578c0292446c7bace98"} [alcohol-p27531] The role of acetaldehyde in mediating the deleterious effect of ethanol on pyridoxal 5'-phosphate metabolism. (1978). https://pubmed.ncbi.nlm.nih.gov/27531/ DOI: 10.1172/jci109128

availability_state

nutrient_deficiency Imported condition classification; unverified.

evidence_span

{"source_cache": "artifacts/alcohol-research/4359937.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1df4485150b1be55f3e5214c424f960ff627cfc317e643c86a0f6747efed8b08", "start_char": 0, "end_char": 1650, "text_sha256": "1df4485150b1be55f3e5214c424f960ff627cfc317e643c86a0f6747efed8b08"}

experimental_model

Plasma PLP in 66 alcoholic subjects without liver abnormality, plus erythrocyte enzyme assays

exposure

Chronic alcohol abuse; acetaldehyde and ethanol applied to erythrocytes

limitations

Selecting subjects without abnormal liver function isolates the vitamin effect from liver disease. The phosphatase mechanism is shown in erythrocytes, not liver.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Human

plain_language

It is the breakdown product that destroys the vitamin, and it works by exposing it to a phosphatase rather than by blocking its synthesis.

primary_references

[alcohol-p4359937] Vitamin B6 metabolism in chronic alcohol abuse. Pyridoxal phosphate levels in plasma and the effects of acetaldehyde on pyridoxal phosphate synthesis and degradation in human erythrocytes. (1974). https://pubmed.ncbi.nlm.nih.gov/4359937/ DOI: 10.1172/jci107607

tissue_or_cell_type

Plasma and erythrocytes

trigger_kind

nutrient_deficiency Imported condition classification; unverified.

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 644–655

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Plasma PLP in 66 alcoholic subjects without liver abnormality, plus erythrocyte enzyme assays · source_derived_draft · unverified_draft

### alcohol-acetaldehyde-not-ethanol Acetaldehyde, but not ethanol, impaired net formation of PLP from pyridoxal, pyridoxine and pyridoxine phosphate by erythrocytes, and the effect was abolished when the B6-phosphate phosphatase was inhibited by 80 mM phosphate, while pyridoxal kinase and pyridoxine phosphate oxidase activities were not decreased. Condition category: nutrient_deficiency nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: It is the breakdown product that destroys the vitamin, and it works by exposing it to a phosphatase rather than by blocking its synthesis. organism: Human tissue_or_cell_type: Plasma and erythrocytes experimental_model: Plasma PLP in 66 alcoholic subjects without liver abnormality, plus erythrocyte enzyme assays limitations: Selecting subjects without abnormal liver function isolates the vitamin effect from liver disease. The phosphatase mechanism is shown in erythrocytes, not liver. exposure: Chronic alcohol abuse; acetaldehyde and ethanol applied to erythrocytes evidence_span: {"source_cache": "artifacts/alcohol-research/4359937.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1df4485150b1be55f3e5214c424f960ff627cfc317e643c86a0f6747efed8b08", "start_char": 0, "end_char": 1650, "text_sha256": "1df4485150b1be55f3e5214c424f960ff627cfc317e643c86a0f6747efed8b08"} [alcohol-p4359937] Vitamin B6 metabolism in chronic alcohol abuse. Pyridoxal phosphate levels in plasma and the effects of acetaldehyde on pyridoxal phosphate synthesis and degradation in human erythrocytes. (1974). https://pubmed.ncbi.nlm.nih.gov/4359937/ DOI: 10.1172/jci107607

evidence_span

{"source_cache": "artifacts/alcohol-research/27056945.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c01bbdf333ac3266271f33f59dc90b58fb733575ade7193b1e9c1664983ac4f5", "start_char": 0, "end_char": 2034, "text_sha256": "c01bbdf333ac3266271f33f59dc90b58fb733575ade7193b1e9c1664983ac4f5"}

experimental_model

Rhesus monkeys exposed to alcohol with oral mucosa DNA adduct measurement

exposure

Alcohol exposure with mass-spectrometric adduct quantification

limitations

A primate measurement of the specific adduct. It establishes exposure of the tissue DNA, not that a tumour follows.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Rhesus monkey

plain_language

The first breakdown product sticks to DNA in the tissue that alcohol touches first.

primary_references

[alcohol-p27056945] Increased levels of the acetaldehyde-derived DNA adduct N 2-ethyldeoxyguanosine in oral mucosa DNA from Rhesus monkeys exposed to alcohol. (2016). https://pubmed.ncbi.nlm.nih.gov/27056945/ DOI: 10.1093/mutage/gew016

tissue_or_cell_type

Oral mucosa

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 527–538

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Rhesus monkeys exposed to alcohol with oral mucosa DNA adduct measurement · source_derived_draft · unverified_draft

### alcohol-dna-adducts Levels of the acetaldehyde-derived DNA adduct N2-ethyl-deoxyguanosine were increased in oral mucosa DNA from rhesus monkeys exposed to alcohol. Condition category: normal nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: The first breakdown product sticks to DNA in the tissue that alcohol touches first. organism: Rhesus monkey tissue_or_cell_type: Oral mucosa experimental_model: Rhesus monkeys exposed to alcohol with oral mucosa DNA adduct measurement limitations: A primate measurement of the specific adduct. It establishes exposure of the tissue DNA, not that a tumour follows. exposure: Alcohol exposure with mass-spectrometric adduct quantification evidence_span: {"source_cache": "artifacts/alcohol-research/27056945.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c01bbdf333ac3266271f33f59dc90b58fb733575ade7193b1e9c1664983ac4f5", "start_char": 0, "end_char": 2034, "text_sha256": "c01bbdf333ac3266271f33f59dc90b58fb733575ade7193b1e9c1664983ac4f5"} [alcohol-p27056945] Increased levels of the acetaldehyde-derived DNA adduct N 2-ethyldeoxyguanosine in oral mucosa DNA from Rhesus monkeys exposed to alcohol. (2016). https://pubmed.ncbi.nlm.nih.gov/27056945/ DOI: 10.1093/mutage/gew016

availability_state

machinery_impairment Imported condition classification; unverified.

evidence_span

{"source_cache": "artifacts/alcohol-research/2562960.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0f0722fad2747c7b723bce352582f07519b1b9b964edadb8674740458475efe1", "start_char": 0, "end_char": 800, "text_sha256": "0f0722fad2747c7b723bce352582f07519b1b9b964edadb8674740458475efe1"}

experimental_model

Polymerase chain reaction genotyping of 24 Japanese livers against enzyme phenotype

exposure

ALDH2 genotype compared with measured enzyme activity

limitations

Establishes dominance of the inactive allele, so heterozygotes are affected. The sample is 24 livers.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Human

plain_language

The flush is the body reacting to the first breakdown product, not to alcohol itself.

primary_references

[alcohol-p2562960] Genotypes for aldehyde dehydrogenase deficiency and alcohol sensitivity. The inactive ALDH2(2) allele is dominant. (1989). https://pubmed.ncbi.nlm.nih.gov/2562960/ DOI: 10.1172/jci113875

tissue_or_cell_type

Liver

trigger_kind

machinery_impairment Imported condition classification; unverified.

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 163–174

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Polymerase chain reaction genotyping of 24 Japanese livers against enzyme phenotype · source_derived_draft · unverified_draft

### alcohol-flush-from-acetaldehyde The alcohol flush reaction is the result of excessive acetaldehyde accumulation, and the unpleasant symptoms tend to reduce alcohol consumption. Condition category: machinery_impairment nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: The flush is the body reacting to the first breakdown product, not to alcohol itself. organism: Human tissue_or_cell_type: Liver experimental_model: Polymerase chain reaction genotyping of 24 Japanese livers against enzyme phenotype limitations: Establishes dominance of the inactive allele, so heterozygotes are affected. The sample is 24 livers. exposure: ALDH2 genotype compared with measured enzyme activity evidence_span: {"source_cache": "artifacts/alcohol-research/2562960.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0f0722fad2747c7b723bce352582f07519b1b9b964edadb8674740458475efe1", "start_char": 0, "end_char": 800, "text_sha256": "0f0722fad2747c7b723bce352582f07519b1b9b964edadb8674740458475efe1"} [alcohol-p2562960] Genotypes for aldehyde dehydrogenase deficiency and alcohol sensitivity. The inactive ALDH2(2) allele is dominant. (1989). https://pubmed.ncbi.nlm.nih.gov/2562960/ DOI: 10.1172/jci113875

availability_state

machinery_impairment Imported condition classification; unverified.

evidence_span

{"source_cache": "artifacts/alcohol-research/19710201.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "22b9547745b08adaa8a9a722228e9c5987ac67442b20f2737d8c54f6988ec7c5", "start_char": 0, "end_char": 1426, "text_sha256": "22b9547745b08adaa8a9a722228e9c5987ac67442b20f2737d8c54f6988ec7c5"}

experimental_model

An animal model built to reproduce the human alcohol dehydrogenase polymorphism

exposure

Higher-activity alcohol dehydrogenase against voluntary intake

limitations

A constructed animal model of a human protective genotype. It supports the acetaldehyde-burst explanation; it is not a human trial.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Rat model of the human variant

plain_language

A faster first enzyme makes the unpleasant metabolite arrive sooner.

primary_references

[alcohol-p19710201] Mechanism of protection against alcoholism by an alcohol dehydrogenase polymorphism: development of an animal model. (2010). https://pubmed.ncbi.nlm.nih.gov/19710201/ DOI: 10.1096/fj.09-132563

tissue_or_cell_type

Liver and behaviour

trigger_kind

machinery_impairment Imported condition classification; unverified.

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 189–200

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · An animal model built to reproduce the human alcohol dehydrogenase polymorphism · source_derived_draft · unverified_draft

### alcohol-adh1b-fast-oxidation An animal model developed to test the mechanism of protection against alcoholism by an alcohol dehydrogenase polymorphism supports faster ethanol oxidation producing higher acetaldehyde as the protective step. Condition category: machinery_impairment nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: A faster first enzyme makes the unpleasant metabolite arrive sooner. organism: Rat model of the human variant tissue_or_cell_type: Liver and behaviour experimental_model: An animal model built to reproduce the human alcohol dehydrogenase polymorphism limitations: A constructed animal model of a human protective genotype. It supports the acetaldehyde-burst explanation; it is not a human trial. exposure: Higher-activity alcohol dehydrogenase against voluntary intake evidence_span: {"source_cache": "artifacts/alcohol-research/19710201.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "22b9547745b08adaa8a9a722228e9c5987ac67442b20f2737d8c54f6988ec7c5", "start_char": 0, "end_char": 1426, "text_sha256": "22b9547745b08adaa8a9a722228e9c5987ac67442b20f2737d8c54f6988ec7c5"} [alcohol-p19710201] Mechanism of protection against alcoholism by an alcohol dehydrogenase polymorphism: development of an animal model. (2010). https://pubmed.ncbi.nlm.nih.gov/19710201/ DOI: 10.1096/fj.09-132563

availability_state

machinery_impairment Imported condition classification; unverified.

evidence_span

{"source_cache": "artifacts/alcohol-research/2562960.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0f0722fad2747c7b723bce352582f07519b1b9b964edadb8674740458475efe1", "start_char": 0, "end_char": 800, "text_sha256": "0f0722fad2747c7b723bce352582f07519b1b9b964edadb8674740458475efe1"}

experimental_model

Polymerase chain reaction genotyping of 24 Japanese livers against enzyme phenotype

exposure

ALDH2 genotype compared with measured enzyme activity

limitations

Establishes dominance of the inactive allele, so heterozygotes are affected. The sample is 24 livers.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Human

plain_language

One bad copy is enough, because the faulty subunit poisons the four-part enzyme.

primary_references

[alcohol-p2562960] Genotypes for aldehyde dehydrogenase deficiency and alcohol sensitivity. The inactive ALDH2(2) allele is dominant. (1989). https://pubmed.ncbi.nlm.nih.gov/2562960/ DOI: 10.1172/jci113875

tissue_or_cell_type

Liver

trigger_kind

machinery_impairment Imported condition classification; unverified.

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 150–161

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Polymerase chain reaction genotyping of 24 Japanese livers against enzyme phenotype · source_derived_draft · unverified_draft

### alcohol-aldh2-allele-dominant The inactive ALDH2 subunit carries a substitution of lysine for glutamate at position 487, and correlating genotype with phenotype in 24 Japanese livers shows the allele encoding the abnormal subunit is dominant. Condition category: machinery_impairment nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: One bad copy is enough, because the faulty subunit poisons the four-part enzyme. organism: Human tissue_or_cell_type: Liver experimental_model: Polymerase chain reaction genotyping of 24 Japanese livers against enzyme phenotype limitations: Establishes dominance of the inactive allele, so heterozygotes are affected. The sample is 24 livers. exposure: ALDH2 genotype compared with measured enzyme activity evidence_span: {"source_cache": "artifacts/alcohol-research/2562960.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0f0722fad2747c7b723bce352582f07519b1b9b964edadb8674740458475efe1", "start_char": 0, "end_char": 800, "text_sha256": "0f0722fad2747c7b723bce352582f07519b1b9b964edadb8674740458475efe1"} [alcohol-p2562960] Genotypes for aldehyde dehydrogenase deficiency and alcohol sensitivity. The inactive ALDH2(2) allele is dominant. (1989). https://pubmed.ncbi.nlm.nih.gov/2562960/ DOI: 10.1172/jci113875

availability_state

machinery_impairment Imported condition classification; unverified.

evidence_span

{"source_cache": "artifacts/alcohol-research/19698717.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4262a0549d8e78b4e7719f62bfa61849f3cf6eb3403bf45fe28d32b7d7662c58", "start_char": 0, "end_char": 1706, "text_sha256": "4262a0549d8e78b4e7719f62bfa61849f3cf6eb3403bf45fe28d32b7d7662c58"}

experimental_model

Case-control study of oesophageal cancer with ADH1B and ALDH2 genotypes and smoking

exposure

Alcohol consumption and smoking across functional genotypes

limitations

A gene-environment interaction study. Synergy is reported on a statistical interaction scale, and the design is case-control.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Human

plain_language

The variant that makes drinking unpleasant also makes each drink more carcinogenic.

primary_references

[alcohol-p19698717] Functional variants in ADH1B and ALDH2 coupled with alcohol and smoking synergistically enhance esophageal cancer risk. (2009). https://pubmed.ncbi.nlm.nih.gov/19698717/ DOI: 10.1053/j.gastro.2009.07.070

tissue_or_cell_type

Oesophagus

trigger_kind

machinery_impairment Imported condition classification; unverified.

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 540–551

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Case-control study of oesophageal cancer with ADH1B and ALDH2 genotypes and smoking · source_derived_draft · unverified_draft

### alcohol-genotype-cancer-synergy Functional variants in ADH1B and ALDH2 coupled with alcohol and smoking synergistically enhanced oesophageal cancer risk. Condition category: machinery_impairment nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: The variant that makes drinking unpleasant also makes each drink more carcinogenic. organism: Human tissue_or_cell_type: Oesophagus experimental_model: Case-control study of oesophageal cancer with ADH1B and ALDH2 genotypes and smoking limitations: A gene-environment interaction study. Synergy is reported on a statistical interaction scale, and the design is case-control. exposure: Alcohol consumption and smoking across functional genotypes evidence_span: {"source_cache": "artifacts/alcohol-research/19698717.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4262a0549d8e78b4e7719f62bfa61849f3cf6eb3403bf45fe28d32b7d7662c58", "start_char": 0, "end_char": 1706, "text_sha256": "4262a0549d8e78b4e7719f62bfa61849f3cf6eb3403bf45fe28d32b7d7662c58"} [alcohol-p19698717] Functional variants in ADH1B and ALDH2 coupled with alcohol and smoking synergistically enhance esophageal cancer risk. (2009). https://pubmed.ncbi.nlm.nih.gov/19698717/ DOI: 10.1053/j.gastro.2009.07.070