Document Detail


Low expression of long-chain acyl-CoA dehydrogenase in human skeletal muscle.
MedLine Citation:
PMID:  20363655     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
PURPOSE: Long-chain acyl-CoA dehydrogenase (LCAD) is a mitochondrial flavoenzyme thought to be one of the major enzymes responsible for the first step of long-chain fatty acid (LCFA) beta-oxidation. Surprisingly, recent studies have shown LCAD is hardly detectable in human tissues such as liver and heart. Skeletal muscle is the largest organ in the body in terms of mass, and accounts for the majority of LCFA oxidation, especially during exercise. The purpose of this study was to investigate the expression levels of LCAD in human skeletal muscle.
METHODS: Muscle biopsies were obtained from the vastus lateralis of healthy athletic men and women, and examined for mRNA abundance, protein content, and enzyme activity of LCAD. We compared LCAD content with that of very-long chain acyl-CoA dehydrogenase (VLCAD) and medium chain acyl-CoA dehydrogenase (MCAD); two mitochondrial beta-oxidation enzymes that have overlapping chain-length specificity to that of LCAD. LCAD protein content and enzyme activity were also examined in enriched mitochondrial protein fractions. As controls, LCAD presence in skeletal muscle was compared to human heart, liver, and mouse skeletal muscle.
RESULTS: The mRNA presence of LCAD in human skeletal muscle is significantly less than VLCAD and MCAD (0.08+/-0.01 vs 7.3+/-0.5 vs 2.4+/-0.2 respectively, P<or=0.0001). LCAD protein was undetectable in human muscle homogenates, and coordinately LCAD enzyme activity was undetectable in enriched mitochondrial samples.
CONCLUSION: LCAD is minimally expressed in human skeletal muscle and likely does not play a significant role in LCFA oxidation.
Authors:
Amy C Maher; Al-Walid Mohsen; Jerry Vockley; Mark A Tarnopolsky
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2010-03-19
Journal Detail:
Title:  Molecular genetics and metabolism     Volume:  100     ISSN:  1096-7206     ISO Abbreviation:  Mol. Genet. Metab.     Publication Date:  2010 Jun 
Date Detail:
Created Date:  2010-05-17     Completed Date:  2010-08-09     Revised Date:  2011-01-26    
Medline Journal Info:
Nlm Unique ID:  9805456     Medline TA:  Mol Genet Metab     Country:  United States    
Other Details:
Languages:  eng     Pagination:  163-7     Citation Subset:  IM    
Affiliation:
Department of Medical Science, McMaster University, Ontario, Canada. maherac@mcmaster.ca
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MeSH Terms
Descriptor/Qualifier:
Acyl-CoA Dehydrogenase / genetics
Acyl-CoA Dehydrogenase, Long-Chain / genetics*
Animals
Female
Humans
Male
Mice
Mitochondria, Heart / enzymology
Mitochondria, Liver / enzymology
Mitochondria, Muscle / enzymology
Muscle, Skeletal / enzymology*
RNA, Messenger / metabolism
Young Adult
Grant Support
ID/Acronym/Agency:
R01 DK078775-04/DK/NIDDK NIH HHS; R01DK78775/DK/NIDDK NIH HHS
Chemical
Reg. No./Substance:
0/RNA, Messenger; EC 1.3.99.13/Acyl-CoA Dehydrogenase, Long-Chain; EC 1.3.99.3/Acyl-CoA Dehydrogenase

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


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