Document Detail


Hepatic lipid composition and stearoyl-coenzyme A desaturase 1 mRNA expression can be estimated from plasma VLDL fatty acid ratios.
MedLine Citation:
PMID:  19850634     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
BACKGROUND: Stearoyl-coenzyme A desaturase 1 (SCD1) catalyzes the limiting step of monounsaturated fatty acid synthesis in humans and is an important player in triglyceride generation. SCD1 has been repeatedly implicated in the pathogenesis of metabolic and inflammatory diseases. Therefore it is of great importance to determine SCD1 activity in human samples. In this study we aimed to evaluate a hepatic SCD1 activity index derived from plasma VLDL triglyceride composition as a tool to estimate hepatic SCD1 expression in humans. Additionally, we further evaluated commonly used fatty acid ratios [elongase, de novo lipogenesis, and Delta5 and Delta6 desaturase] in plasma VLDL and hepatic lipid fractions.
DESIGN AND METHODS: Liver biopsies and plasma samples were simultaneously collected from 15 individuals. Plasma VLDL was obtained by ultracentrifugation. Hepatic and plasma VLDL lipids were fractionated by thin-layer chromatography, and the fatty acid composition of each fraction was analyzed by gas chromatography. Hepatic SCD1 expression was determined by real-time PCR.
RESULTS: Hepatic SCD1 mRNA expression was associated with the product/precursor ratios (16:1/16:0 and 18:1/18:0) of hepatic lipid fractions. The 16:1/16:0 ratio in hepatic and VLDL triglycerides as well as the 18:1/18:0 ratio in plasma VLDL were closely associated with hepatic SCD1 expression. The hepatic de novo lipogenesis index from triglycerides was associated with expression of lipogenic genes [fatty acid synthase (FASN), acetyl-Coenzyme A carboxylase alpha (ACACA), and sterol regulatory element binding transcription factor 1 (SREBP-1)] and is closely reflected by the de novo lipogenesis index in VLDL triglycerides.
CONCLUSION: We demonstrated for the first time that hepatic SCD1 expression can be estimated noninvasively from routine blood samples by measuring the SCD1 activity index in fasting plasma VLDL.
Authors:
Andreas Peter; Alexander Cegan; Silvia Wagner; Rainer Lehmann; Norbert Stefan; Alfred Königsrainer; Ingmar Königsrainer; Hans-Ulrich Häring; Erwin Schleicher
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-10-22
Journal Detail:
Title:  Clinical chemistry     Volume:  55     ISSN:  1530-8561     ISO Abbreviation:  Clin. Chem.     Publication Date:  2009 Dec 
Date Detail:
Created Date:  2009-11-30     Completed Date:  2009-12-28     Revised Date:  2012-05-24    
Medline Journal Info:
Nlm Unique ID:  9421549     Medline TA:  Clin Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2113-20     Citation Subset:  IM    
Affiliation:
Department of Internal Medicine, Division of Endocrinology, Diabetology, Vascular Medicine, Nephrology and Clinical Chemistry, University of Tübingen, Tübingen Germany. Andreas.Peter@med.uni-tuebingen.de
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MeSH Terms
Descriptor/Qualifier:
Acetyl-CoA Carboxylase / biosynthesis
Acetyltransferases / biosynthesis,  genetics
Aged
Chromatography, Thin Layer
Fatty Acid Desaturases / biosynthesis,  genetics
Fatty Acid Synthetase Complex / biosynthesis
Fatty Acids, Nonesterified / blood,  chemistry*
Female
Humans
Linoleoyl-CoA Desaturase / biosynthesis,  genetics
Lipids / chemistry*
Lipogenesis
Lipoproteins, VLDL / blood,  chemistry*
Liver / enzymology,  metabolism*
Male
RNA, Messenger / biosynthesis*
Stearoyl-CoA Desaturase / biosynthesis*,  genetics
Sterol Regulatory Element Binding Protein 1 / biosynthesis
Triglycerides / blood,  chemistry*
Chemical
Reg. No./Substance:
0/Fatty Acids, Nonesterified; 0/Lipids; 0/Lipoproteins, VLDL; 0/RNA, Messenger; 0/SREBF1 protein, human; 0/Sterol Regulatory Element Binding Protein 1; 0/Triglycerides; EC 1.14.19.-/Fatty Acid Desaturases; EC 1.14.19.1/SCD1 protein, human; EC 1.14.19.1/Stearoyl-CoA Desaturase; EC 1.14.19.3/Linoleoyl-CoA Desaturase; EC 1.14.99.-/delta-5 fatty acid desaturase; EC 2.3.1.-/Acetyltransferases; EC 2.3.1.-/fatty acid elongases; EC 6.-/Fatty Acid Synthetase Complex; EC 6.4.1.2/Acetyl-CoA Carboxylase
Comments/Corrections
Comment In:
Clin Chem. 2009 Dec;55(12):2071-3   [PMID:  19850628 ]

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


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