Contractions induce phosphorylation of the AMPK site Ser565 in hormone-sensitive lipase in muscle.
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
Standard
Contractions induce phosphorylation of the AMPK site Ser565 in hormone-sensitive lipase in muscle. / Donsmark, Morten; Langfort, Jozef; Holm, Cecilia; Ploug, Thorkil; Galbo, Henrik.
I: Biochemical and Biophysical Research Communications, Bind 316, Nr. 3, 2004, s. 867-71.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - Contractions induce phosphorylation of the AMPK site Ser565 in hormone-sensitive lipase in muscle.
AU - Donsmark, Morten
AU - Langfort, Jozef
AU - Holm, Cecilia
AU - Ploug, Thorkil
AU - Galbo, Henrik
N1 - Keywords: Animals; Binding Sites; Blotting, Western; Cyclic AMP-Dependent Protein Kinases; Epinephrine; Male; Mitogen-Activated Protein Kinases; Multienzyme Complexes; Muscle Contraction; Muscle, Skeletal; Naphthalenes; Phosphorylation; Protein Kinase C; Protein-Serine-Threonine Kinases; Rats; Rats, Wistar; Serine; Sterol Esterase; Time Factors; Triglycerides
PY - 2004
Y1 - 2004
N2 - 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 5min 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.
AB - 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 5min 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.
U2 - 10.1016/j.bbrc.2004.02.140
DO - 10.1016/j.bbrc.2004.02.140
M3 - Journal article
C2 - 15033481
VL - 316
SP - 867
EP - 871
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -
ID: 8462367