| Cloning of monkey RALDH1 and characterization of retinoid metabolism in monkey kidney proximal tubule cells. | |
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MedLine Citation:
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PMID: 12576512 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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All-trans and 9-cis retinoic acids function as ligands for retinoic acid receptors (RARs and RXRs), which are ligand-dependent transcription factors and play important roles in development and cellular differentiation. Several retinal dehydrogenases are likely to contribute to the production of all-trans and 9-cis RAs in vivo, but their respective roles in different tissues are still poorly characterized. We have previously characterized and cloned from kidney tissues the rat retinal dehydrogenase type 1 (RALDH1), which oxidizes all-trans and 9-cis retinal with high efficiency but is inactive with 13-cis retinal. Here we have characterized the retinal-oxidizing activity in monkey JTC12 cells, which are derived from kidney proximal tubules. In vitro assay of cell lysates revealed the presence of a NAD+-dependent dehydrogenase that catalyzed the oxidation of all-trans, 9-cis, and 13-cis retinal. Northern blot analysis of JTC12 RNAs and cloning by reverse transcription-polymerase chain reaction demonstrated expression of a monkey homolog of RALDH1. Bacterially expressed JTC12 RALDH1 catalyzed conversion of all three retinal isomers, with a higher catalytic efficiency for 9-cis retinal than for all-trans and 13-cis retinal. Accordingly, live JTC12 produced 9-cis retinoic acid more efficiently than all-trans retinoic acid from their respective retinal precursors. Only metabolites corresponding to the same steric conformation were formed from 9-cis or all-trans retinal, indicating a lack of detectable isomerizing activity in JTC12 cells. |
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Authors:
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Helene Brodeur; Isabelle Gagnon; Sylvie Mader; Pangala V Bhat |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2002-11-04 |
Journal Detail:
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Title: Journal of lipid research Volume: 44 ISSN: 0022-2275 ISO Abbreviation: J. Lipid Res. Publication Date: 2003 Feb |
Date Detail:
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Created Date: 2003-02-10 Completed Date: 2004-02-24 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0376606 Medline TA: J Lipid Res Country: United States |
Other Details:
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Languages: eng Pagination: 303-13 Citation Subset: IM |
Affiliation:
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Laboratory of Nutrition and Cancer, Universite de Montreal, Montreal, Quebec, Canada. |
| Data Bank Information | |
Bank Name/Acc. No.:
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GENBANK/AF542418 |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Aldehyde Oxidoreductases
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genetics,
metabolism* Amino Acid Sequence Animals Base Sequence Cell Line Cloning, Molecular Haplorhini* Humans Hydrogen-Ion Concentration Isomerism Isotretinoin / metabolism* Kidney Tubules, Proximal / cytology, metabolism* Molecular Sequence Data Rats Retinal Dehydrogenase Retinaldehyde / metabolism* Sequence Alignment Substrate Specificity Tretinoin / metabolism* |
| Chemical | |
Reg. No./Substance:
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116-31-4/Retinaldehyde; 302-79-4/Tretinoin; 4759-48-2/Isotretinoin; 514-85-2/9-cis-retinal; EC 1.2.-/Aldehyde Oxidoreductases; EC 1.2.1.36/Retinal Dehydrogenase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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