Document Detail


Glutamine stimulates mTORC1 independent of the cell content of essential amino acids.
MedLine Citation:
PMID:  22566039     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Glutamine and leucine are important mTORC1 modulators, although their roles are not precisely defined. In HepG2 and HeLa cells glutamine-free incubation lowers mTORC1 activity, although cell leucine is not decreased. mTORC1 activity, suppressed by amino acid-free incubation, is completely rescued only if essential amino acids (EAA) and glutamine are simultaneously restored, although cell leucine is higher in the absence than in the presence of glutamine. Thus, glutamine stimulates mTORC1 independent of cell leucine, suggesting the existence of two distinct stimulatory signals from either glutamine or EAA.
Authors:
Martina Chiu; Saverio Tardito; Amelia Barilli; Massimiliano G Bianchi; Valeria Dall'Asta; Ovidio Bussolati
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-05-08
Journal Detail:
Title:  Amino acids     Volume:  43     ISSN:  1438-2199     ISO Abbreviation:  Amino Acids     Publication Date:  2012 Dec 
Date Detail:
Created Date:  2012-11-09     Completed Date:  2013-05-16     Revised Date:  2013-09-30    
Medline Journal Info:
Nlm Unique ID:  9200312     Medline TA:  Amino Acids     Country:  Austria    
Other Details:
Languages:  eng     Pagination:  2561-7     Citation Subset:  IM    
Affiliation:
Unit of General and Clinical Pathology, Department of Experimental Medicine, University of Parma, Via Volturno 39, 43125, Parma, Italy.
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MeSH Terms
Descriptor/Qualifier:
Amino Acids, Essential / analysis,  pharmacology*
Dose-Response Relationship, Drug
Glutamine / pharmacology*
HeLa Cells
Hep G2 Cells
Humans
Multiprotein Complexes / metabolism*
Structure-Activity Relationship
TOR Serine-Threonine Kinases / metabolism*
Chemical
Reg. No./Substance:
0/Amino Acids, Essential; 0/Multiprotein Complexes; 0/mechanistic target of rapamycin complex 1; 56-85-9/Glutamine; EC 2.7.1.1/TOR Serine-Threonine Kinases

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


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