Evidence map›Paper›PMID 20207735›Full record

ArticleThe Journal of biological chemistry2010

Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in cellular defense against hyperosmotic stress.

Chad Brocker, Natalie Lassen, Tia Estey, Aglaia Pappa, Miriam Cantore, Valeria V Orlova, Triantafyllos Chavakis, Kathryn L Kavanagh, Udo Oppermann, Vasilis Vasiliou

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed
6.8field-weighted citation impact, top 2% 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

101 citing papers in PubMed, 194 citations in OpenAlex.

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41 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

10 authors at 4 institutions in 2 countries.

Chad BrockerDepartment of Pharmaceutical Sciences, University of Colorado Denver, Aurora, Colorado 80045, USA.
Natalie Lassen
Tia Estey
Aglaia Pappa
Miriam Cantore
Valeria V Orlova
Triantafyllos Chavakis
Kathryn L Kavanagh
Udo Oppermann
Vasilis Vasiliou
University of Colorado Denver · USGenomics England · GBCenter for Cancer Research · USNational Institutes of Health · US

Funding

Role and Molecular Mechanisms of Corneal Aldehyde DehydrogenaseR01EY011490 · NEI · YALE UNIVERSITY · PI VASILIOU, VASILIS · 2004 to 2013
$4.0M
Novel Role of Corneal Crystallins as Modulators of Cell Growth and TransparencyR01EY017963 · NEI · YALE UNIVERSITY · PI VASILIOU, VASILIS · 2007 to 2019
$3.7M
MOLECULAR MECHANISMS AND CORNEAL ALDEHYDE DEHYDROGENASER29EY011490 · NEI · UNIVERSITY OF COLORADO DENVER · PI VASILIOU, VASILIS · 1998 to 2002
$308k
CIHRNEI NIH HHS EY11490NEI NIH HHS EY17963NEI NIH HHS R01 EY011490NEI NIH HHS R01 EY017963NEI NIH HHS R29 EY011490Wellcome Trust
6 · The paper itself

Abstract

Mammalian ALDH7A1 is homologous to plant ALDH7B1, an enzyme that protects against various forms of stress, such as salinity, dehydration, and osmotic stress. It is known that mutations in the human ALDH7A1 gene cause pyridoxine-dependent and folic acid-responsive seizures. Herein, we show for the first time that human ALDH7A1 protects against hyperosmotic stress by generating osmolytes and metabolizing toxic aldehydes. Human ALDH7A1 expression in Chinese hamster ovary cells attenuated osmotic stress-induced apoptosis caused by increased extracellular concentrations of sucrose or sodium chloride. Purified recombinant ALDH7A1 efficiently metabolized a number of aldehyde substrates, including the osmolyte precursor, betaine aldehyde, lipid peroxidation-derived aldehydes, and the intermediate lysine degradation product, alpha-aminoadipic semialdehyde. The crystal structure for ALDH7A1 supports the enzyme's substrate specificities. Tissue distribution studies in mice showed the highest expression of ALDH7A1 protein in liver, kidney, and brain, followed by pancreas and testes. ALDH7A1 protein was found in the cytosol, nucleus, and mitochondria, making it unique among the aldehyde dehydrogenase enzymes. Analysis of human and mouse cDNA sequences revealed mitochondrial and cytosolic transcripts that are differentially expressed in a tissue-specific manner in mice. In conclusion, ALDH7A1 is a novel aldehyde dehydrogenase expressed in multiple subcellular compartments that protects against hyperosmotic stress by generating osmolytes and metabolizing toxic aldehydes.

Indexed as

OsmosisAldehyde DehydrogenaseAldehydesAnimalsCHO CellsCricetinaeCricetulusCrystallography, X-RayFemaleGene Expression Regulation, EnzymologicHumansMaleMiceProteinsTissue DistributionAldehyde DehydrogenaseAldehydesALDH7A1 protein, humanAldh7a1 protein, mouseProteins

Identifiers

PMID20207735
PMCPMC2881771
OpenAlexW2145908472

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.