Aldehyde dehydrogenase 1B1 (ALDH1B1)

Aldehyde dehydrogenase 1B1 (ALDH1B1) is a mitochondrial enzyme belonging to the aldehyde dehydrogenase superfamily, primarily responsible for oxidation of a broad range of endogenous and exogenous aldehyde substrates, including acetaldehyde and lipid peroxidation products[1][2][3]. It is highly expressed in the liver, small intestine, pancreas, and at lower levels in tissues such as lung and colon, where it is particularly enriched in stem cell compartments[1]. ALDH1B1 is catalytically similar to ALDH2, with a high affinity for acetaldehyde, supporting a role in ethanol metabolism[2][3]. Elevated ALDH1B1 expression is observed in several cancers, notably colon and pancreatic adenocarcinomas, where it contributes to cell proliferation, chemoresistance, and may serve as a diagnostic or prognostic biomarker[1][4][6]. Additionally, ALDH1B1 has been implicated in antiviral defense mechanisms by promoting antiviral signaling pathways in infected cells[8]. Disulfiram and other aldehyde dehydrogenase inhibitors can target ALDH1B1, which has therapeutic implications but may present safety challenges, given its physiological roles in tissue homeostasis and detoxification[2][3][4].

Other names

ALDH1B1Aldehyde dehydrogenase family 1 member B1

Enzymatic oxidation of toxic aldehydes to carboxylic acids Modulation of chemoresistance in cancer cells Regulation of antiviral signaling via MAVS aggregation and RIG-I pathway activation[8]