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Transcriptome and proteome analysis of soleus muscle of hormone-sensitive lipase-null mice

Hansson, Ola LU ; Donsmark, M; Ling, Charlotte LU ; Nevsten, Pernilla LU ; Danfelter, Mikael LU ; Andersen, Jesper N; Galbo, H and Holm, Cecilia LU (2005) In Journal of Lipid Research 46(12). p.2614-2623
Abstract
Hormone-sensitive lipase (HSL), a key enzyme in fatty acid mobilization in adipocytes, has been demonstrated also in skeletal muscle. To gain further insight into the role and importance of HSL in skeletal muscle, a transcriptome analysis of soleus muscle of HSL-null mice was performed. A total of 161 transcripts were found to be differentially expressed. Increased mRNA levels of fructose-1,6-bisphosphatase, fructose-2,6-bisphosphatase, and phosphorylase kinase gamma 1A suggest a higher glycogen flux in soleus muscle of HSL-null mice. An observed increase in the utilization of glycogen stores supports this finding. Moreover, an increased amount of intramyocellular lipid droplets, observed by transmission electron microscopy, suggests... (More)
Hormone-sensitive lipase (HSL), a key enzyme in fatty acid mobilization in adipocytes, has been demonstrated also in skeletal muscle. To gain further insight into the role and importance of HSL in skeletal muscle, a transcriptome analysis of soleus muscle of HSL-null mice was performed. A total of 161 transcripts were found to be differentially expressed. Increased mRNA levels of fructose-1,6-bisphosphatase, fructose-2,6-bisphosphatase, and phosphorylase kinase gamma 1A suggest a higher glycogen flux in soleus muscle of HSL-null mice. An observed increase in the utilization of glycogen stores supports this finding. Moreover, an increased amount of intramyocellular lipid droplets, observed by transmission electron microscopy, suggests decreased mobilization of lipid stores in HSL-null mice. To complement the transcriptome data, protein expression analysis was performed. Five spots were found to be differentially expressed: pyruvate dehydrogenase E1 alpha, creatine kinase (CK), ankyrin-repeat domain 2, glyceraldehyde-3-phosphate dehydrogenase, and one protein yet to be identified. The increased protein level of CK indicates creatine phosphate degradation to be of increased importance in HSL-null mice. The results of this study suggest that in the absence of HSL, a metabolic switch from reliance on lipid to carbohydrate energy substrates takes place, supporting an important role of HSL in soleus muscle lipid metabolism. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
glycogen, proteomics, metabolic switch, skeletal muscle
in
Journal of Lipid Research
volume
46
issue
12
pages
2614 - 2623
publisher
American Society for Biochemistry and Molecular Biology
external identifiers
  • pmid:16199803
  • wos:000233301100009
  • scopus:30844451999
ISSN
1539-7262
DOI
10.1194/jlr.M500028-JLR200
language
English
LU publication?
yes
id
5f73078f-1e06-4802-ad45-8250c56334e7 (old id 213049)
date added to LUP
2007-09-28 08:25:01
date last changed
2017-02-26 03:38:25
@article{5f73078f-1e06-4802-ad45-8250c56334e7,
  abstract     = {Hormone-sensitive lipase (HSL), a key enzyme in fatty acid mobilization in adipocytes, has been demonstrated also in skeletal muscle. To gain further insight into the role and importance of HSL in skeletal muscle, a transcriptome analysis of soleus muscle of HSL-null mice was performed. A total of 161 transcripts were found to be differentially expressed. Increased mRNA levels of fructose-1,6-bisphosphatase, fructose-2,6-bisphosphatase, and phosphorylase kinase gamma 1A suggest a higher glycogen flux in soleus muscle of HSL-null mice. An observed increase in the utilization of glycogen stores supports this finding. Moreover, an increased amount of intramyocellular lipid droplets, observed by transmission electron microscopy, suggests decreased mobilization of lipid stores in HSL-null mice. To complement the transcriptome data, protein expression analysis was performed. Five spots were found to be differentially expressed: pyruvate dehydrogenase E1 alpha, creatine kinase (CK), ankyrin-repeat domain 2, glyceraldehyde-3-phosphate dehydrogenase, and one protein yet to be identified. The increased protein level of CK indicates creatine phosphate degradation to be of increased importance in HSL-null mice. The results of this study suggest that in the absence of HSL, a metabolic switch from reliance on lipid to carbohydrate energy substrates takes place, supporting an important role of HSL in soleus muscle lipid metabolism.},
  author       = {Hansson, Ola and Donsmark, M and Ling, Charlotte and Nevsten, Pernilla and Danfelter, Mikael and Andersen, Jesper N and Galbo, H and Holm, Cecilia},
  issn         = {1539-7262},
  keyword      = {glycogen,proteomics,metabolic switch,skeletal muscle},
  language     = {eng},
  number       = {12},
  pages        = {2614--2623},
  publisher    = {American Society for Biochemistry and Molecular Biology},
  series       = {Journal of Lipid Research},
  title        = {Transcriptome and proteome analysis of soleus muscle of hormone-sensitive lipase-null mice},
  url          = {http://dx.doi.org/10.1194/jlr.M500028-JLR200},
  volume       = {46},
  year         = {2005},
}