Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Contractions induce phosphorylation of the AMPK site Ser(565) in hormone-sensitive lipase in muscle

Donsmark, M ; Langfort, J ; Holm, Cecilia LU ; Ploug, T and Galbo, H (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:
author
; ; ; and
organization
publishing date
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 &lt; 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}},
}