Linked Life Data

17574202

Source:http://linkedlifedata.com/resource/pubmed/id/17574202

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2007-8-27
pubmed:abstractText
A member of the aldo-keto reductase superfamily, AKR1C15, was isolated via cDNA cloning, but its physiological function remains unknown. Here, we show that recombinant AKR1C15 is an NADPH-dependent reductase with broad substrate specificity for aromatic, alicyclic and aliphatic carbonyl compounds, including acetoin, 2,5-hexanedione, methylglyoxal, farnesal, retinals, 17-ketosteroids and monosaccharides. Especially, all-trans-retinal, alpha-diketones and lipid-derived aldehydes including 4-hydroxynonenal were excellent substrates showing low K(m) values (0.3-5.5 microM). Immunohistochemical and reverse transcription-PCR analyses revealed that AKR1C15 is highly expressed in rat bronchiolar Clara cells, type II alveolar cells, gastric parietal cells, the epithelial cells of the stomach and colon, and the brown adipocytes. The enzyme was not detected in cells of other rat tissues, but is consistently expressed in the vascular endothelial cells. These results suggest that AKR1C15 plays a role in retinoid, steroid, isoprenoid and carbohydrate metabolism, as well as a defense system, protecting against reactive carbonyl compounds.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
465
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
136-47
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Enzymatic characteristics of an aldo-keto reductase family protein (AKR1C15) and its localization in rat tissues.
pubmed:affiliation
Laboratory of Biochemistry, Gifu Pharmaceutical University, Mitahora-higashi, Gifu 502-8585, Japan. sendo@gifu-pu.ac.jp
pubmed:publicationType
Journal Article