Evidence map›Paper›PMID 20616185›Full record

ArticleDrug metabolism and disposition: the biological fate of chemicals2010

Aldehyde dehydrogenase 1B1: molecular cloning and characterization of a novel mitochondrial acetaldehyde-metabolizing enzyme.

Dimitrios Stagos, Ying Chen, Chad Brocker, Elizabeth Donald, Brian C Jackson, David J Orlicky, David C Thompson, Vasilis Vasiliou

Open access · bronzeAbstract read
In one paragraph

Article in Drug metabolism and disposition: the biological fate of chemicals, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
4.1field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

87 citing papers in PubMed, 137 citations in OpenAlex.

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  13. A crucial active site network of titratable residues guides catalysis and NADProtein science : a publication of the Protein Society · 2025
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  14. The Significance of Aldehyde Dehydrogenase 1 in Cancers.International journal of molecular sciences · 2024
    Review
  15. Article
  16. Article
  17. Article
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  20. Article

27 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 2 countries.

Dimitrios StagosDepartment of Pharmaceutical Sciences,University of Colorado-Denver, Aurora, CO, USA.
Ying Chen
Chad Brocker
Elizabeth Donald
Brian C Jackson
David J Orlicky
David C Thompson
Vasilis Vasiliou
University of Thessaly · GRUniversity of Colorado Denver · US

Funding

Novel Role of Corneal Crystallins as Modulators of Cell Growth and TransparencyR01EY017963 · NEI · YALE UNIVERSITY · PI VASILIOU, VASILIS · 2007 to 2019
$3.7M
Role of Mitochondrial Aldehyde Dehydrogenases in Ethanol Metabolism and ToxicityR21AA017754 · NIAAA · UNIVERSITY OF COLORADO DENVER · PI VASILIOU, VASILIS · 2009 to 2010
$411k
NEI NIH HHS EY17963NEI NIH HHS R01 EY017963NIAAA NIH HHS AA017754NIAAA NIH HHS R21 AA017754
6 · The paper itself

Abstract

Ethanol-induced damage is largely attributed to its toxic metabolite, acetaldehyde. Clearance of acetaldehyde is achieved by its oxidation, primarily catalyzed by the mitochondrial class II aldehyde dehydrogenase (ALDH2). ALDH1B1 is another mitochondrial aldehyde dehydrogenase (ALDH) that shares 75% peptide sequence homology with ALDH2. Recent population studies in whites suggest a role for ALDH1B1 in ethanol metabolism. However, to date, no formal documentation of the biochemical properties of ALDH1B1 has been forthcoming. In this current study, we cloned and expressed human recombinant ALDH1B1 in Sf9 insect cells. The resultant enzyme was purified by affinity chromatography to homogeneity. The kinetic properties of purified human ALDH1B1 were assessed using a wide range of aldehyde substrates. Human ALDH1B1 had an exclusive preference for NAD(+) as the cofactor and was catalytically active toward short- and medium-chain aliphatic aldehydes, aromatic aldehydes, and the products of lipid peroxidation, 4-hydroxynonenal and malondialdehyde. Most importantly, human ALDH1B1 exhibited an apparent K(m) of 55 μM for acetaldehyde, making it the second low K(m) ALDH for metabolism of this substrate. The dehydrogenase activity of ALDH1B1 was sensitive to disulfiram inhibition, a feature also shared with ALDH2. The tissue distribution of ALDH1B1 in C57BL/6J mice and humans was examined by quantitative polymerase chain reaction, Western blotting, and immunohistochemical analysis. The highest expression occurred in the liver, followed by the intestinal tract, implying a potential physiological role for ALDH1B1 in these tissues. The current study is the first report on the expression, purification, and biochemical characterization of human ALDH1B1 protein.

Indexed as

Aldehyde DehydrogenaseRecombinant ProteinsAcetaldehydeAldehyde Dehydrogenase 1 FamilyAldehyde Dehydrogenase, MitochondrialAmino Acid SequenceAnimalsBaculoviridaeBlotting, WesternCell LineCloning, MolecularEthanolGenetic VectorsHumansImmunohistochemistryInsectaAcetaldehydeAldehyde DehydrogenaseAldehyde Dehydrogenase 1 FamilyAldehyde Dehydrogenase, MitochondrialALDH1B1 protein, humanEthanolNADRecombinant Proteins

Identifiers

PMID20616185
PMCPMC2957164
OpenAlexW2137075933

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.