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Dual Mechanisms Regulating AMPK Kinase Action in the Ischemic Heart

Dual Mechanisms Regulating AMPK Kinase Action in the Ischemic Heart Integrative Physiology Dual Mechanisms Regulating AMPK Kinase Action in the Ischemic Heart Suzanne J. Baron,* Ji Li,* Raymond R. Russell III, Dietbert Neumann, Edward J. Miller, Roland Tuerk, Theo Wallimann, Rebecca L. Hurley, Lee A. Witters, Lawrence H. Young Abstract—AMP-activated protein kinase (AMPK) is emerging as an important signaling protein during myocardial ischemia. AMPK is a heterotrimeric complex containing an  catalytic subunit and  and  regulatory subunits. Phosphorylation of Thr in the activation loop of the  subunit by upstream AMPK kinase(s) (AMPKK) is a critical determinant of AMPK activity. However, the mechanisms regulating AMPK phosphorylation in the ischemic heart remain uncertain and were therefore investigated. In the isolated working rat heart, low-flow ischemia rapidly activated AMPKK activity when measured using recombinant AMPK (rAMPK) as substrate. The addition of AMP (10 to 200 mol/L) augmented the ability of heterotrimeric    or    rAMPK to be phosphorylated by heart AMPKK 1 1 1 2 1 1 in vitro, whereas physiologic concentrations of ATP inhibited rAMPK phosphorylation. However, neither AMP nor ATP directly influenced AMPKK activity: they had no effect on AMPKK-mediated phosphorylation of rAMPK 1-312 substrates lacking normal AMP-binding  subunits (isolated truncated  http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Circulation Research Wolters Kluwer Health

Dual Mechanisms Regulating AMPK Kinase Action in the Ischemic Heart

Young, Lawrence H.
Circulation Research , Volume 96 (3) – Feb 1, 2005
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References (42)

ISSN
0009-7330
eISSN
1524-4571
DOI
10.1161/01.RES.0000155723.53868.d2
pmid
15653571
Publisher site
See Article on Publisher Site

Abstract

Integrative Physiology Dual Mechanisms Regulating AMPK Kinase Action in the Ischemic Heart Suzanne J. Baron,* Ji Li,* Raymond R. Russell III, Dietbert Neumann, Edward J. Miller, Roland Tuerk, Theo Wallimann, Rebecca L. Hurley, Lee A. Witters, Lawrence H. Young Abstract—AMP-activated protein kinase (AMPK) is emerging as an important signaling protein during myocardial ischemia. AMPK is a heterotrimeric complex containing an  catalytic subunit and  and  regulatory subunits. Phosphorylation of Thr in the activation loop of the  subunit by upstream AMPK kinase(s) (AMPKK) is a critical determinant of AMPK activity. However, the mechanisms regulating AMPK phosphorylation in the ischemic heart remain uncertain and were therefore investigated. In the isolated working rat heart, low-flow ischemia rapidly activated AMPKK activity when measured using recombinant AMPK (rAMPK) as substrate. The addition of AMP (10 to 200 mol/L) augmented the ability of heterotrimeric    or    rAMPK to be phosphorylated by heart AMPKK 1 1 1 2 1 1 in vitro, whereas physiologic concentrations of ATP inhibited rAMPK phosphorylation. However, neither AMP nor ATP directly influenced AMPKK activity: they had no effect on AMPKK-mediated phosphorylation of rAMPK 1-312 substrates lacking normal AMP-binding  subunits (isolated truncated 

Journal

Circulation Research – Wolters Kluwer Health

Published: Feb 1, 2005

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