Prepubertal Regulation of the Rat Dioxin-Inducible Aldehyde Dehydrogenase (ALDH3)

Stephanou, Panayiotis; Pappas, Periklis; Vasiliou, Vasilis; Marselos, Marios

doi:10.1007/978-1-4615-4735-8_17

Cited by 2 publications

(2 citation statements)

References 13 publications

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“…Interestingly, while ALDH3A1 is poorly expressed in normal liver, its expression in hepatoma cells increases in direct correlation with the degree of tumor growth [182]. ALDH3A1 is induced in other neoplastic tissues and cell lines [183] and its expression is differentially affected by hormones such as progesterone (downregulates) and cortisone (upregulates), suggesting a potential role in hormone-dependent tumors [184]. ALDH3A1 expression is also induced by various xenobiotics, including polycyclic hydrocarbons (PAHs) and 3-methylcholanthrene, through multiple ALDH3A1 xenobiotic response elements (XREs) [185,186].…”

Section: Aldh3a1mentioning

confidence: 99%

Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase superfamily

Marchitti

Brocker

Stagos

et al. 2008

Expert Opinion on Drug Metabolism & Toxicology

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Background-Aldehydes are highly reactive molecules. While several non-P450 enzyme systems participate in their metabolism, one of the most important is the aldehyde dehydrogenase (ALDH) superfamily, composed of NAD(P) +-dependent enzymes that catalyze aldehyde oxidation. Objective-This article presents a review of what is currently known about each member of the human ALDH superfamily including the pathophysiological significance of these enzymes. Methods-Relevant literature involving all members of the human ALDH family was extensively reviewed, with the primary focus on recent and novel findings. Conclusion-To date, 19 ALDH genes have been identified in the human genome and mutations in these genes and subsequent inborn errors in aldehyde metabolism are the molecular basis of several diseases, including Sjögren-Larsson syndrome, type II hyperprolinemia, γ-hydroxybutyric aciduria and pyridoxine-dependent seizures. ALDH enzymes also play important roles in embryogenesis and development, neurotransmission, oxidative stress and cancer. Finally, ALDH enzymes display multiple catalytic and non-catalytic functions including ester hydrolysis, antioxidant properties, xenobiotic bioactivation and UV light absorption.

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Section: Aldh3a1mentioning

confidence: 99%

Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase superfamily

Marchitti

Brocker

Stagos

et al. 2008

Expert Opinion on Drug Metabolism & Toxicology

Self Cite

682

470

View full text Add to dashboard Cite

show abstract

“…ALDH3A1 expression is differentially affected by hormones such as progesterone and cortisone, suggesting a potential hormones-dependent role in some tumors. 128 In addition, ALDH3A1 expression is also induced by several xenobiotics, including polycyclic hydrocarbons (PAHs) and 3-metylcolantrene, through multiple response elements to xenobiotics (XREs). 129,130 These data suggest that ALDH3A1 is an important regulatory element in cell stress defense.…”

Section: ■ Antioxidant Cellular Responsementioning

confidence: 99%

Role of Aldehyde Dehydrogenases in Physiopathological Processes

Rodríguez‐Zavala

Calleja

Moreno‐Sánchez

et al. 2019

Chem. Res. Toxicol.

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Many different diseases are associated with oxidative stress. One of the main consequences of oxidative stress at the cellular level is lipid peroxidation, from which toxic aldehydes may be generated. Below their toxicity thresholds, some aldehydes are involved in signaling processes, while others are intermediaries in the metabolism of lipids, amino acids, neurotransmitters, and carbohydrates. Some aldehydes ubiquitously distributed in the environment, such as acrolein or formaldehyde, are extremely toxic to the cell. On the other hand, aldehyde dehydrogenases (ALDHs) are able to detoxify a wide variety of aldehydes to their corresponding carboxylic acids, thus helping to protect from oxidative stress. ALDHs are located in different subcellular compartments such as cytosol, mitochondria, nucleus, and endoplasmic reticulum. The aim of this review is to analyze, and highlight, the role of different ALDH isoforms in the detoxification of aldehydes generated in processes that involve high levels of oxidative stress. The ALDH physiological relevance becomes evident by the observation that their expression and activity are enhanced in different pathologies that involve oxidative stress such as neurodegenerative disorders, cardiopathies, atherosclerosis, and cancer as well as inflammatory processes. Furthermore, ALDH mutations bring about several disorders in the cell. Thus, understanding the mechanisms by which these enzymes participate in diverse cellular processes may lead to better contend with the damage caused by toxic aldehydes in different pathologies by designing modulators and/or protocols to modify their activity or expression.

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Prepubertal Regulation of the Rat Dioxin-Inducible Aldehyde Dehydrogenase (ALDH3)

Cited by 2 publications

References 13 publications

Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase superfamily

Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase superfamily

Role of Aldehyde Dehydrogenases in Physiopathological Processes

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