Aldehyde Dehydrogenase
Aldehyde Dehydrogenase - Related Videos
09:59
Application of AlDeSense to Stratify Ovarian Cancer Cells Based on Aldehyde Dehydrogenase 1A1 Activity
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Cited by 3 •
2023
Methods to measure ALDH1A1 activity in live cells are critical in cancer research due to its status as a biomarker of stemness. In this study, we employed an isoform-selective fluorogenic probe to determine the relative levels of ALDH1A1 activity in a panel of five ovarian cancer cell lines.
03:09
Identification of Unknown Aldehydes and Ketones - Concepts
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2020
Aldehydes and Ketones Aldehydes and ketones have a carbonyl group (C=O) as a functional group. A ketone has two alkyl or aryl groups attached to the carbonyl carbon (RCOR’). The simplest ketone is acetone, which has two methyl groups attached to the carbonyl carbon (CH3COCH3). An aldehyde is similar to a ketone, except that instead of two side groups connected to the carbonyl carbon, they have at least one hydrogen (RCOH). The simplest aldehyde is formaldehyde (HCOH), as it has two hydrogens...
15:03
Identification of Unknown Aldehydes and Ketones - Student Protocol
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2020
Source: Lara Al Hariri and Ahmed Basabrain at the University of Massachusetts Amherst, MA, USA DNPH Test for Aromatic Aldehydes and KetonesExpand In this lab, you'll use the DNPH test, the Tollens' test, and the iodoform test to identify two unknown aldehydes or ketones. You'll use butanone and benzaldehyde as known compounds to confirm that the tests are working as expected. You'll start the lab with the DNPH test, which relies on the reaction between 2,4-dinitrophenylhydrazine, or DNPH,...
03:02
A Lactate Dehydrogenase Release Assay To Detect Macrophage Death Following Nigericin Exposure
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2025
This video demonstrates the lactate dehydrogenase assay to detect inflammasome-mediated macrophage death. The macrophages are exposed to lipopolysaccharide for priming, followed by exposure to nigericin to cause inflammasome-induced cell death, which is determined by the lactate dehydrogenase assay.
03:25
A Lactate Dehydrogenase Release Assay to Detect Cryptococcus neoformans Infection in Macrophages
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2025
In this video, we demonstrate a cytotoxicity assay to assess Cryptococcus neoformans, a pathogenic fungus, infection in macrophages. The cytotoxicity is determined by the release of cytoplasmic lactate dehydrogenase enzyme due to macrophage lysis caused by Cryptococcus neoformans infection.
FAQs
The active-site cysteine first reacts with an aldehyde to form a temporary thiohemiacetal intermediate. During this reaction, a hydride is transferred from the substrate to NAD+ or NADP+, producing an oxidized intermediate. Water then helps release the carboxylic acid and restore the catalytic cysteine, completing the reaction cycle.
NAD+ and NADP+ function as hydride acceptors during aldehyde oxidation. Their participation allows electrons removed from the aldehyde to be captured in a defined cofactor-dependent step, while the substrate becomes a carboxylic acid. This cofactor use connects aldehyde dehydrogenase activity with the cell’s broader metabolic redox processes.
Aldehydes can be chemically reactive, so their accumulation can increase cellular stress. Aldehyde dehydrogenase activity limits this burden by converting reactive intermediates into less reactive acids. This protective role is relevant when aldehydes arise from alcohol metabolism, lipid-related processes, or drug-derived compounds, linking enzyme activity with cellular stress responses.
The term family reflects the presence of related enzymes that carry out the same broad type of aldehyde oxidation in different biological settings. Together, these enzymes can contribute to alcohol processing, detoxification of lipid- and drug-derived aldehydes, and retinal metabolism. Studying the family therefore helps connect enzyme chemistry with diverse cellular pathways.
During alcohol metabolism, aldehydes occur as reactive intermediates that must be processed further. Aldehyde dehydrogenase converts these compounds into carboxylic acids, reducing their chemical reactivity and supporting continued metabolic handling. Its activity therefore contributes both to the progression of the pathway and to protection against aldehyde accumulation during alcohol processing.
Aldehyde dehydrogenase participates in converting retinal into retinoic acid, placing the enzyme within a biologically important differentiation-related pathway. This connection extends its significance beyond detoxification: changes in aldehyde processing can influence pathways associated with cellular differentiation, making retinal metabolism an important context for studying enzyme function in biology.
Aldehyde dehydrogenase activity is associated with cellular stress responses, drug resistance, and cancer stem-cell biology. These links make the enzyme a useful research target for examining how cells handle reactive aldehydes and respond to treatment-related challenges. Investigators can therefore study its activity as part of broader questions about tumor-cell behavior and persistence.