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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/213049
- author
- Hansson, Ola
LU
; Donsmark, M
; Ling, Charlotte
LU
; Nevsten, Pernilla
LU
; Danfelter, Mikael
LU
; Andersen, Jesper N
; Galbo, H
and Holm, Cecilia
LU
- organization
- publishing date
- 2005
- 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
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Electron Microscopy Unit (013100002), Department of Clinical Sciences, Malmö (013240000), Department of Experimental Medical Science (013210000), Polymer and Materials Chemistry (LTH) (011001041), Molecular Endocrinology (013212018), Department of Clinical Sciences, Lund (013230000), Diabetes and Endocrinology (013241530), Epigenetics and Diabetes (013241505)
- id
- 5f73078f-1e06-4802-ad45-8250c56334e7 (old id 213049)
- date added to LUP
- 2016-04-01 12:23:19
- date last changed
- 2024-01-08 18:46:36
@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}},
keywords = {{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}},
doi = {{10.1194/jlr.M500028-JLR200}},
volume = {{46}},
year = {{2005}},
}