Document Detail

Binding of all-trans-retinoic acid to MLTC-1 proteins.
MedLine Citation:
PMID:  16132685     Owner:  NLM     Status:  MEDLINE    
The covalent incorporation of [(3)H]all-trans-retinoic acid into proteins has been studied in tumoural Leydig (MLTC-1) cells. The maximum retinoylation activity of MLTC-1 cell proteins was 710+/-29 mean+/-SD) fmoles/8 x 10(4) cells at 37 degrees C. About 90% of [(3)H]retinoic acid was trichloroacetic acid-soluble after proteinase-K digestion and about 65--75% after hydrolysis with hydroxylamine. Thus, retinoic acid is most probably linked to proteins as a thiol ester. The retinoylation reaction was inhibited by 13-cis-retinoic acid and 9-cis-retinoic acid with IC(50) values of 0.9 microM and 0.65 microM, respectively. Retinoylation was not inhibited by high concentrations of palmitic or myristic acids (250 microM); but there was an increase of the binding activity of about 25% and 130%, respectively. On the other hand, the retinoylation reaction was inhibited (about 40%) by 250 microM lauric acid. After pre-incubation of the cells with different concentrations of unlabeled RA, the retinoylation reaction with 100 nM [(3)H]RA involved first an increase at 100 nM RA and then a decrease of retinoylation activity between 200 and 600 nM RA. After cycloheximide treatment of the tumoural Leydig cells the binding activity of [(3)H]RA was about the same as that in the control, suggesting that the bond occurred on proteins in pre-existing cells.
Erika Cione; Paola Tucci; Valentina Senatore; Giuseppina Ioele; Giuseppe Genchi
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Molecular and cellular biochemistry     Volume:  276     ISSN:  0300-8177     ISO Abbreviation:  Mol. Cell. Biochem.     Publication Date:  2005 Aug 
Date Detail:
Created Date:  2005-08-31     Completed Date:  2006-01-10     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0364456     Medline TA:  Mol Cell Biochem     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  55-60     Citation Subset:  IM    
Copyright Information:
(Mol Cell Biochem 276: 55-60, 2005).
Dipartimento Farmaco-Biologico, Università della Calabria, Cosenza 87100, Italia.
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MeSH Terms
Cell Line, Tumor
Leydig Cells / chemistry,  metabolism*
Mice, Inbred C57BL
Neoplasm Proteins / metabolism*
Protein Binding
Tretinoin / metabolism*
Reg. No./Substance:
0/Neoplasm Proteins; 302-79-4/Tretinoin

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