PMID- 21851339
OWN - NLM
STAT- MEDLINE
DCOM- 20120313
LR  - 20211020
IS  - 1573-4935 (Electronic)
IS  - 0144-8463 (Linking)
VI  - 32
IP  - 2
DP  - 2012 Apr 1
TI  - 5'-AMP-activated protein kinase is inactivated by adrenergic signalling in adult 
      cardiac myocytes.
PG  - 197-213
LID - 10.1042/BSR20110076 [doi]
AB  - In adult rat cardiac myocytes adrenaline decreased AMPK (AMP-activated protein 
      kinase) activity with a half-time of approximately 4 min, decreased 
      phosphorylation of AMPK (alpha-Thr172) and decreased phosphorylation of ACC 
      (acetyl-CoA carboxylase). Inactivation of AMPK by adrenaline was through both alpha1- 
      and beta-ARs (adrenergic receptors), but did not involve cAMP or calcium signalling, 
      was not blocked by the PKC (protein kinase C) inhibitor BIM I (bisindoylmaleimide 
      I), by the ERK (extracellular-signal-regulated kinase) cascade inhibitor U0126 or 
      by PTX (pertussis toxin). Adrenaline caused no measurable change in LKB1 
      activity. Adrenaline decreased AMPK activity through a process that was distinct 
      from AMPK inactivation in response to insulin or PMA. Neither adrenaline nor PMA 
      altered the myocyte AMP:ATP ratio although the adrenaline effect was attenuated 
      by oligomycin and by AICAR (5-amino-4-imidazolecarboxamide-1-beta-D-ribofuranoside), 
      agents that mimic 'metabolic stress'. Inactivation of AMPK by adrenaline was 
      abolished by 1 muM okadaic acid suggesting that activation of PP2A (phosphoprotein 
      phosphatase 2A) might mediate the adrenaline effect. However, no change in PP2A 
      activity was detected in myocyte extracts. Adrenaline increased phosphorylation 
      of the AMPK beta-subunit in vitro but there was no detectable change in vivo in 
      phosphorylation of previously identified AMPK sites (beta-Ser24, beta-Ser108 or 
      beta-Ser182) suggesting that another site(s) is targeted.
FAU - Tsuchiya, Yugo
AU  - Tsuchiya Y
AD  - *Institute of Structural and Molecular Biology, Division of Biosciences, 
      University College London, Gower Street, London, WC1E 6BT, U.K.
FAU - Denison, Fiona C
AU  - Denison FC
FAU - Heath, Richard B
AU  - Heath RB
FAU - Carling, David
AU  - Carling D
FAU - Saggerson, David
AU  - Saggerson D
LA  - eng
GR  - MC_U120027537/MRC_/Medical Research Council/United Kingdom
GR  - PG/07/038/22871/BHF_/British Heart Foundation/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Biosci Rep
JT  - Bioscience reports
JID - 8102797
RN  - 0 (Insulin)
RN  - 0 (Receptors, Adrenergic, beta)
RN  - EC 2.7.11.31 (AMP-Activated Protein Kinases)
RN  - EC 3.1.3.16 (Protein Phosphatase 2)
RN  - EC 6.4.1.2 (Acetyl-CoA Carboxylase)
RN  - JAC85A2161 (Adenine)
RN  - YKH834O4BH (Epinephrine)
SB  - IM
MH  - AMP-Activated Protein Kinases/*metabolism
MH  - Acetyl-CoA Carboxylase/metabolism
MH  - Adenine/metabolism
MH  - Animals
MH  - Cell Survival
MH  - Cells, Cultured
MH  - Enzyme Activation
MH  - Epinephrine/*metabolism
MH  - Insulin/metabolism
MH  - Myocytes, Cardiac/cytology/*enzymology/metabolism
MH  - Protein Phosphatase 2/metabolism
MH  - Rats
MH  - Receptors, Adrenergic, beta/metabolism
EDAT- 2011/08/20 06:00
MHDA- 2012/03/14 06:00
CRDT- 2011/08/20 06:00
PHST- 2011/08/20 06:00 [entrez]
PHST- 2011/08/20 06:00 [pubmed]
PHST- 2012/03/14 06:00 [medline]
AID - BSR20110076 [pii]
AID - 10.1042/BSR20110076 [doi]
PST - ppublish
SO  - Biosci Rep. 2012 Apr 1;32(2):197-213. doi: 10.1042/BSR20110076.