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When the researchers investigated mice without ALDH, they found that alcohol caused four times as much damage to DNA when compared with mice that could produce ALDH.
Beyond ALDH, the body has a range of other secondary mechanisms that can repair various types of DNA damage.
In addition to ADH and ALDH enzymes, cytochrome P450 2Ei (CYP2E1) is also a pathway of ethanol oxidation.
ALDH genotyping was performed with multiplex PCR, using the method of Tamakoshi et al.
Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) were measured using commercially available diagnostic kits (Wuhan Boster Bio-Engineering Limited Company, Wuhan, China) according to the manufacturer's recommended instructions.
The data showed that the levels of the metabolic enzymes ADH and ALDH in the model control group were significantly reduced compared with those in the normal control group (p < 0.01, n= 15).
Other alleles of the ADH and ALDH genes also have been reported to affect risk; however, these effects are much smaller and are not detected in all studies.
The acetaldehyde then is converted rapidly to acetate by the enzyme aldehyde dehydrogenase (ALDH).
In humans, most of the knowledge about acetaldehyde's properties has been gathered indirectly by studying people carrying a deficient variant (i.e., allele) of the gene encoding the ALDH enzyme known as ALDH2*2.
KEY WORDS: Ethanol metabolism; ethanol-to-acetaldehyde metabolism; acetaldehyde; acetate; aldehyde dehydrogenase (ALDH); central nervous system; brain; catalase; cytochrome P450; alcohol dehydrogenase (ADH); ethanol oxidation; behavior; ethanol preference
The metabolism of acetaldehyde in the brain is much less controversial than the metabolism of ethanol because ALDH enzymes have long been known to be present in brain cells (Deitrich 1966; Erwin and Deitrich 1966).
The acetaldehyde produced in all these reactions is, in turn, metabolized to acetate in a reaction catalyzed by the aldehyde dehydrogenase (ALDH) enzymes.