Document Detail


The mitogen-induced lysophospholipid:acyl-CoA acyltransferase (LAT) expression in human T-lymphocytes is diminished by hydrocortisone.
MedLine Citation:
PMID:  9299417     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
One of the earliest changes observed in activated lymphocytes is the enhanced incorporation of unsaturated fatty acids into membrane phospholipids catalyzed by phospholipases and acyltransferases. This early membrane phospholipid remodeling has been shown to be independent from protein synthesis. We have investigated the oleic acid incorporation into phospholipids of activated T-lymphocytes within hours and present data that the sustained membrane phospholipid remodeling in activated T-lymphocytes was largely decreased by cycloheximide and actinomycin D treatment while neither protein synthesis inhibitor had an effect on the fatty acid incorporation into phospholipids in resting T-lymphocytes. Lisofylline, an inhibitor of lysophosphatidic acid:acyl-CoA acyltransferase, had no inhibitory activity, indicating that the membrane lipid remodeling was not due to fatty acid incorporation into de novo-synthesized phospholipids. The membrane phospholipid alteration induced by mitogens was also diminished by hydrocortisone (HC) in a concentration-dependent manner. The steroid hormone antagonist RU486 failed to reverse but potentiated this inhibitory activity of HC. HC did not affect the fatty acid uptake, and the decrease of fatty acid incorporation into phospholipids induced by HC was accompanied by an increase of fatty acid incorporation into triglycerides, indicating that the inhibitory activity of HC was specific for fatty acid incorporation into phospholipids catalyzed by lysophospholipidacyl-CoA acyltransferase (LAT). HC did not directly inhibit the LAT enzyme activity. From these data we conclude that LAT gene transcription is induced as an early event following T-cell activation. The inhibitory action of hydrocortisone may give new insights into the regulatory mechanisms involved in LAT expression.
Authors:
C Kerkhoff; L Gehring; K Habben; K Resch; V Kaever
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  237     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  1997 Aug 
Date Detail:
Created Date:  1997-10-15     Completed Date:  1997-10-15     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  632-8     Citation Subset:  IM    
Affiliation:
Institut für Molekularpharmakologie, Medizinische Hochschule Hannover, Germany.
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MeSH Terms
Descriptor/Qualifier:
1-Acylglycerophosphocholine O-Acyltransferase / biosynthesis*,  metabolism
Antigens, CD / biosynthesis
Antigens, Differentiation, T-Lymphocyte / biosynthesis
Cells, Cultured
Cycloheximide / pharmacology
Fatty Acids / analysis
Gene Expression Regulation, Enzymologic / drug effects*
Humans
Hydrocortisone / pharmacology*
Lymphocyte Activation
Mifepristone / pharmacology
Mitogens / pharmacology*
Muromonab-CD3 / pharmacology
Oleic Acid / metabolism
Phospholipids / chemistry,  metabolism
T-Lymphocytes / drug effects,  enzymology*,  immunology
Chemical
Reg. No./Substance:
0/Antigens, CD; 0/Antigens, Differentiation, T-Lymphocyte; 0/CD69 antigen; 0/Fatty Acids; 0/Mitogens; 0/Muromonab-CD3; 0/Phospholipids; 112-80-1/Oleic Acid; 50-23-7/Hydrocortisone; 66-81-9/Cycloheximide; 84371-65-3/Mifepristone; EC 2.3.1.23/1-Acylglycerophosphocholine O-Acyltransferase

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


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