Document Detail


Cloning of monkey RALDH1 and characterization of retinoid metabolism in monkey kidney proximal tubule cells.
MedLine Citation:
PMID:  12576512     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Helene Brodeur; Isabelle Gagnon; Sylvie Mader; Pangala V Bhat
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2002-11-04
Journal Detail:
Title:  Journal of lipid research     Volume:  44     ISSN:  0022-2275     ISO Abbreviation:  J. Lipid Res.     Publication Date:  2003 Feb 
Date Detail:
Created Date:  2003-02-10     Completed Date:  2004-02-24     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0376606     Medline TA:  J Lipid Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  303-13     Citation Subset:  IM    
Affiliation:
Laboratory of Nutrition and Cancer, Universite de Montreal, Montreal, Quebec, Canada.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/AF542418
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MeSH Terms
Descriptor/Qualifier:
Aldehyde Oxidoreductases / 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:
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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