aldehyde dehydrogenase 1A1 (ALDH1A1) is a member of the aldehyde dehydrogenase superfamily that oxidizes aldehydes to their corresponding acids, reactions that are coupled to the reduction of NAD+ to NADH
ablation of retinoic acid signaling in host dencritic cells by deletion of isoform RALDH2 protects mice from acute graft-versus-host disease. Isoform RALDH1 deletion fails to reduce acute graft-versus-host disease
changes in ALDH1A1 expression appear to be part of the early acute-phase inflammatory response, which alters the expression of other retinoid homeostatic genes
retinoic acid-producing dendritic cells play critical roles in gut immunity. Retinal dehydrogenase 2 (RALDH2) encoded by Aldh1a2 is a key enzyme for generating retinoic acid in dendritic cells
aldehyde dehydrogenase 1A1 increases NADH levels and promotes tumor growth via glutathione/dihydrolipoic acid-dependent NAD+ reduction. ALDH1A1 can also use glutathione (GSH) and dihydrolipoic acid (DHLA) as electron donors to reduce NAD+ to NADH. The GSH/DHLA-dependent NAD+-reduction activity of ALDH1A1 is not affected by the aldehyde dehydrogenase inhibitor or by mutation of the residues in its aldehyde-binding pocket. It is thus a distinct biochemical reaction from the classic aldehyde-dehydrogenase activity catalyzed by ALDH1A1. The GSH/DHLA-dependent NAD+-reduction activity of ALDH1A1 can decrease cellular NAD(P)+/NAD(P)H ratio and promote tumor growth. The tumor-promoting effect of ALDH1A1 is achieved, at least partially, through decreasing the cellular NAD+/ NADH ratio
ALDH1A1 contributes to protection of A-549 cells against retinaldehyde toxicity. ALDH1 confers protection against retinaldehyde toxicity in cancer cells
ALDH1A1 is a NAD+-dependent aldehyde dehydrogenase that participates in multiple metabolic pathways and has been indicated to play an important role in obesity and diabetes
retinal dehydrogenase 5 is an important enzyme in the visual cycle and plays a crucial role in suppressing proliferation and metastasis in hepatocellular carcinoma
the cytosolic isozymes ALDH1A1, ALDH1A2, and ALDH1A3 play important roles in cell signaling via oxidation of retinaldehyde to retinoic acid. In the cell, retinoic acid produced in the cytoplasm binds to cellular retinoic acid binding protein type II, and is transferred to the nucleus where it binds to heterodimers of retinoic acid receptor (RAR) and retinoid X receptor (RXR). Once activated, these receptor complexes bind to retinoic acid response elements (RAREs), which are regulatory sequences that induce gene transcription and modulate a wide range of biological processes, including cell proliferation, differentiation, cell cycle arrest and apoptosis
retinoic acid-producing dendritic cells play critical roles in gut immunity. Retinal dehydrogenase 2 (RALDH2) encoded by Aldh1a2 is a key enzyme for generating retinoic acid in dendritic cells
high-fat diet significantly decreases basal retinal levels in liver to 44% of control rats. Enhanced activity and expression of RALDHs in liver of high-fat diet rats
MAPK activation is required for GM-CSF-induced Aldh1a2 expression and Sp1 nuclear translocation. Sp1 participates in the Aldh1a2 expression. CpG methylation in the Aldh1a2 promoter region inhibits Sp1-dependent Aldh1a2 promoter activation. Aldh1a2 transcription silencing by CpG methylation of the promoter region is not due to direct interference with Sp1 binding to the promoter region
MAPK activation is required for GM-CSF-induced Aldh1a2 expression and Sp1 nuclear translocation. Sp1 participates in the Aldh1a2 expression. CpG methylation in the Aldh1a2 promoter region inhibits Sp1-dependent Aldh1a2 promoter activation. Aldh1a2 transcription silencing by CpG methylation of the promoter region is not due to direct interference with Sp1 binding to the promoter region
high-fat diet significantly decreases basal retinal levels in liver to 44% of control rats. Enhanced activity and expression of RALDHs in liver of high-fat diet rats
MAPK activation is required for GM-CSF-induced Aldh1a2 expression and Sp1 nuclear translocation. Sp1 participates in the Aldh1a2 expression. CpG methylation in the Aldh1a2 promoter region inhibits Sp1-dependent Aldh1a2 promoter activation. Aldh1a2 transcription silencing by CpG methylation of the promoter region is not due to direct interference with Sp1 binding to the promoter region