Contractions induce phosphorylation of the AMPK site Ser(565) in hormone-sensitive lipase in muscle
(2004) In Biochemical and Biophysical Research Communications 316(3). p.867-871- Abstract
- Intramyocellular triglyceride is an important energy store which is related to insulin resistance. Mobilization of fatty acids from this pool is probably regulated by hormone-sensitive lipase (HSL), which has recently been shown to exist in muscle and to be activated by epinephrine via PKA and by contractions via PKC and ERK. 5' AMP-activated protein kinase (AMPK) is an intracellular fuel gauge which regulates metabolism. In this Study we incubated rat soleus Muscle to investigate if AMPK influences HSL during 5 min of repeated tetanic contractions. An eightfold increase in AMPK activity was accompanied by a 2.5-fold increase in phosphorylation of the AMPK-site Ser(565) in HSL (p < 0.05). Inhibition of PKC by Calphostin C abolished the... (More)
- Intramyocellular triglyceride is an important energy store which is related to insulin resistance. Mobilization of fatty acids from this pool is probably regulated by hormone-sensitive lipase (HSL), which has recently been shown to exist in muscle and to be activated by epinephrine via PKA and by contractions via PKC and ERK. 5' AMP-activated protein kinase (AMPK) is an intracellular fuel gauge which regulates metabolism. In this Study we incubated rat soleus Muscle to investigate if AMPK influences HSL during 5 min of repeated tetanic contractions. An eightfold increase in AMPK activity was accompanied by a 2.5-fold increase in phosphorylation of the AMPK-site Ser(565) in HSL (p < 0.05). Inhibition of PKC by Calphostin C abolished the contraction-mediated HSL activation while HSL-Ser(565) phosphorylation was not reduced. The study indicates that during contractions AMPK phosphorylates HSL in Ser(565), but this phosphorylation is not directly responsible for the contraction-induced activation of HSL. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/283055
- author
- Donsmark, M ; Langfort, J ; Holm, Cecilia LU ; Ploug, T and Galbo, H
- organization
- publishing date
- 2004
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- exercise, muscle, metabolims, triacylglyceol, lipolysis, enzyme
- in
- Biochemical and Biophysical Research Communications
- volume
- 316
- issue
- 3
- pages
- 867 - 871
- publisher
- Elsevier
- external identifiers
-
- pmid:15033481
- wos:000220579200041
- scopus:1642356600
- ISSN
- 1090-2104
- DOI
- 10.1016/j.bbrc.2004.02.140
- language
- English
- LU publication?
- yes
- id
- 7eae0c71-4677-4091-99a4-7c805915de70 (old id 283055)
- date added to LUP
- 2016-04-01 15:51:05
- date last changed
- 2022-04-07 01:12:18
@article{7eae0c71-4677-4091-99a4-7c805915de70, abstract = {{Intramyocellular triglyceride is an important energy store which is related to insulin resistance. Mobilization of fatty acids from this pool is probably regulated by hormone-sensitive lipase (HSL), which has recently been shown to exist in muscle and to be activated by epinephrine via PKA and by contractions via PKC and ERK. 5' AMP-activated protein kinase (AMPK) is an intracellular fuel gauge which regulates metabolism. In this Study we incubated rat soleus Muscle to investigate if AMPK influences HSL during 5 min of repeated tetanic contractions. An eightfold increase in AMPK activity was accompanied by a 2.5-fold increase in phosphorylation of the AMPK-site Ser(565) in HSL (p < 0.05). Inhibition of PKC by Calphostin C abolished the contraction-mediated HSL activation while HSL-Ser(565) phosphorylation was not reduced. The study indicates that during contractions AMPK phosphorylates HSL in Ser(565), but this phosphorylation is not directly responsible for the contraction-induced activation of HSL.}}, author = {{Donsmark, M and Langfort, J and Holm, Cecilia and Ploug, T and Galbo, H}}, issn = {{1090-2104}}, keywords = {{exercise; muscle; metabolims; triacylglyceol; lipolysis; enzyme}}, language = {{eng}}, number = {{3}}, pages = {{867--871}}, publisher = {{Elsevier}}, series = {{Biochemical and Biophysical Research Communications}}, title = {{Contractions induce phosphorylation of the AMPK site Ser(565) in hormone-sensitive lipase in muscle}}, url = {{http://dx.doi.org/10.1016/j.bbrc.2004.02.140}}, doi = {{10.1016/j.bbrc.2004.02.140}}, volume = {{316}}, year = {{2004}}, }