Retinaldehyde dehydrogenase (RALDH)

Retinaldehyde dehydrogenase refers to a group of **aldehyde dehydrogenase enzymes (RALDH1/ALDH1A1, RALDH2/ALDH1A2, RALDH3/ALDH1A3)** that catalyze the oxidation of **retinaldehyde to retinoic acid**, a crucial step in vitamin A metabolism and retinoic acid signaling[2][4][8]. These enzymes are essential for embryonic development, tissue differentiation, and immune regulation by supplying ligand for retinoic acid receptors, thus controlling numerous gene expression events[3][4][6]. RALDH enzymes are widely studied as therapeutic targets in oncology (e.g., cancer stem cell biology and chemoresistance), regenerative medicine, and developmental biology[8]. Dysfunction or dysregulation of these enzymes can result in developmental malformations, immune disorders, and altered response to cancer therapies[3][8]. Expression and activity are tissue-specific, with key functions in liver, gastrointestinal tract, nervous system, and reproductive organs[2][3][4].[6][8]

Other names

Aldehyde dehydrogenase 1 family member A1 (ALDH1A1)Aldehyde dehydrogenase 1 family member A2 (ALDH1A2)Aldehyde dehydrogenase 1 family member A3 (ALDH1A3)ALDH1A1, ALDH1A2, ALDH1A3RALDH1, RALDH2, RALDH3

Aldehyde dehydrogenase inhibitors (block conversion of retinaldehyde to retinoic acid, affecting RA signaling and cell differentiation); Retinoic acid analogues (modulate downstream signaling after RA production); Chemotherapy metabolic modulation (inactivation or activation of prodrugs)