Aldehyde dehydrogenases: from eye crystallins to metabolic disease and cancer stem cells.
Chemico-biological interactions
confidence
Key findings
Comprehensive review of ALDH superfamily roles in aldehyde metabolism, disease, embryogenesis, oxidative stress, cancer; no clinical/biological endpoints reported.
View source on PubMed (PMID 23159885) ↗
- Sample size
- Not applicable (review)
- Population
- Review of human and eukaryotic ALDH superfamily; diseases including gout, osteoporosis, cancer, metabolic disease
- Dosing
- Not applicable
- Duration
- Not applicable
- Route
- Not applicable
- Blinding
- not_reported
- Controls
- not_reported
- Drug class
- coenzyme
Full abstract
The aldehyde dehydrogenase (ALDH) superfamily is composed of nicotinamide adenine dinucleotide (phosphate) (NAD(P)(+))-dependent enzymes that catalyze the oxidation of aldehydes to their corresponding carboxylic acids. To date, 24 ALDH gene families have been identified in the eukaryotic genome. In addition to aldehyde metabolizing capacity, ALDHs have additional catalytic (e.g. esterase and reductase) and non-catalytic activities. The latter include functioning as structural elements in the eye (crystallins) and as binding molecules to endobiotics and xenobiotics. Mutations in human ALDH genes and subsequent inborn errors in aldehyde metabolism are the molecular basis of several diseases. Most recently ALDH polymorphisms have been associated with gout and osteoporosis. Aldehyde dehydrogenase enzymes also play important roles in embryogenesis and development, neurotransmission, oxidative stress and cancer. This article serves as a comprehensive review of the current state of knowledge regarding the ALDH superfamily and the contribution of ALDHs to various physiological and pathophysiological processes.