Aldehyde dehydrogenase 3 family member A1 (ALDH3A1)

Aldehyde dehydrogenase 3 family member A1 (ALDH3A1) is a cytoplasmic, homodimeric enzyme that catalyzes the NAD(P)+-dependent oxidation of medium-chain aliphatic and aromatic aldehydes to their corresponding carboxylic acids[1][2][6]. It is highly expressed in tissues requiring strong antioxidant protection, especially the cornea (where it can comprise up to 50% of water-soluble proteins), as well as in the stomach, bladder, skin, liver (inducibly), and lung[1][2][3]. In the cornea, ALDH3A1 detoxifies reactive aldehyde byproducts of UV-induced lipid peroxidation, protecting against oxidative stress, apoptosis, and DNA damage[1][2][4][5]. The enzyme has been linked with cytoprotective effects in airway epithelia (notably against cigarette smoke toxicity) and in regulation of DNA damage response pathways[3][2]. In cancer, ALDH3A1 expression has been associated with cancer stem cell phenotypes, roles in tumor resistance to certain chemotherapies, and is modulated by pathways such as Wnt/beta-catenin[6][7]. Drugs that interact with ALDH3A1 include the chemotherapeutic prodrug cyclophosphamide (which it metabolizes) and experimental peptide inhibitors[6]. ALDH3A1 is a clinically and biologically important target for detoxification and cellular stress defense, though pharmacological manipulation must consider the risk of impairing vital protective functions in healthy tissues[1][2][3][6][7].

Other names

Aldehyde dehydrogenase, dimeric NADP-preferringALDH3A1Aldehyde dehydrogenase 3A1

Oxidation of medium-chain aldehydes to carboxylic acids; Detoxification of lipid peroxidation products; Prevention of aldehyde-induced cytotoxicity; Chemoresistance through metabolizing cytotoxic aldehyde byproducts