Document Detail

The mouse liver content of carbonic anhydrase III and glutathione S-tranferases A3 and P1 depend on dietary supply of methionine and cysteine.
MedLine Citation:
PMID:  15203113     Owner:  NLM     Status:  MEDLINE    
The contents of glutathione S-transferase (GST) subunits, carbonic anhydrase III (CAIII), glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and a 230 kDa protein are affected by protein deprivation in mouse liver. In order to know if particular amino acids control these contents, the effects of feeding for 5 days with diets containing different amino acids were examined. After an exploration using SDS-PAGE analysis, the action of selected diets was further examined by distinct techniques. The 230 kDa protein was identified as fatty acid synthase (FAS) by both mass spectrometry and amino acid sequence analyses. Dietary tests showed that: (1) a protein-free diet (PFD) increased the content of glutathione S-transferases P1 and M1, and glyceraldehyde-3-phosphate dehydrogenase, while the content of glutathione S-transferase A3, fatty acid synthase and carbonic anhydrase III decreased; (2) a protein-free diet having either methionine or cysteine preserved the normal contents of glutathione S-transferases P1, A3, M1 and carbonic anydrase III; (3) a protein-free diet having threonine preserved partially the normal contents of glutathione S-transferases P1, A3, M1 and carbonic anhydrase III; (4) a protein-free diet having methionine, threonine and cysteine prevented in part the loss of fatty acid synthase; and (5) the glyceraldehyde-3-phosphate dehydrogenase content was controlled by increased carbohydrate level and/or by lower amino acid content of diets, but not by any specific amino acid. These data indicate that methionine and cysteine exert a main role on the control of liver glutathione S-transferases A3 and P1, and carbonic anhydrase III. Thus, they emerge necessary to prevent unsafe alterations of liver metabolism caused by protein deprivation.
Virginia Paola Ronchi; Rubén Danilo Conde; Jean Claude Guillemot; Pedro Mariano Sanllorenti
Related Documents :
15596483 - Anabolic signaling deficits underlie amino acid resistance of wasting, aging muscle.
14340053 - The stimulation by treatment in vivo with tri-iodothyronine of amino acid incorporation...
21886103 - Comparative analysis of s-fatty acylation of gel-separated proteins by stable isotope-c...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The international journal of biochemistry & cell biology     Volume:  36     ISSN:  1357-2725     ISO Abbreviation:  Int. J. Biochem. Cell Biol.     Publication Date:  2004 Oct 
Date Detail:
Created Date:  2004-06-18     Completed Date:  2005-03-21     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9508482     Medline TA:  Int J Biochem Cell Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  1993-2004     Citation Subset:  IM    
Facultad de Ciencias Exactas y Naturales, Instituto de Investigaciones Biológicas, Universidad Nacional de Mar del Plata, C.C. 1245, B7600GTQ Mar del Plata, Argentina.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Carbonic Anhydrase III / analysis*,  biosynthesis
Cysteine / administration & dosage,  metabolism,  pharmacology*
Glutathione Transferase / analysis*,  biosynthesis
Liver / drug effects*,  enzymology*,  metabolism
Methionine / administration & dosage,  metabolism,  pharmacology*
Mice, Inbred BALB C
Reg. No./Substance:
52-90-4/Cysteine; 63-68-3/Methionine; EC Transferase; EC 4.2.1.-/Carbonic Anhydrase III

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  In vitro modification of betaine-homocysteine S-methyltransferase by tissue-type transglutaminase.
Next Document:  Investigating filopodia sensing using arrays of defined nano-pits down to 35 nm diameter in size.