Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2011 Aug;4(4):577-85.
doi: 10.1161/CIRCEP.110.957662.

Advances in cardiac ATP-sensitive K+ channelopathies from molecules to populations

Andre Terzic  1 , Alexey E Alekseev, Satsuki Yamada, Santiago Reyes, Timothy M Olson
Affiliations

Advances in cardiac ATP-sensitive K+ channelopathies from molecules to populations

Andre Terzic et al. Circ Arrhythm Electrophysiol. 2011 Aug.
No abstract available

PubMed Disclaimer

Figures

Figure 1
Figure 1. Structure and function of ventricular sarcolemmal KATP channel complexes
The pore-forming KCNJ11-encoded Kir6.2 subunit assembles with the regulatory ABCC9-encoded SUR2A protein to form heteromultimeric KATP channels abundantly expressed in the ventricular sarcolemma. The defining feature of KATP channel operation is adenine nucleotide-dependent gating, ensuring high-fidelity coupling between the cellular energetic state and membrane electrical activity. Intracellular ATP keeps KATP channels closed under normal conditions, while ADP promotes channel opening in response to metabolic challenge. KATP channel opening under stress translates into shortening of the cardiac action potential (↓APD) and accelerated repolarization (↓QT).
Figure 2
Figure 2. Pathogenic mutations and risk-conferring polymorphisms in KATP channel genes associated with human cardiac disorders
Topology of Kir6.2/Kir6.1 and SUR2A (with nucleotide binding domain NBD1/NBD2 and transmembrane domains TMD0-TMD1-TMD2) subunits, with mapped locations of variant sites underlying KATP channelopathies.
Figure 3
Figure 3. Advances in KATP channelopathies
Over the last three decades, science has increasingly defined KATP channel structure and function at molecular, cellular, organ and organism levels. Today, new knowledge in KATP channelopathies informs the practice of cardiovascular medicine expanding the understanding of cardioprotection in health and disease.
See this image and copyright information in PMC

References

    1. Alekseev AE, Hodgson DM, Karger AB, Park S, Zingman LV, Terzic A. ATP-sensitive K+ channel channel/enzyme multimer: Metabolic gating in the heart. J Mol Cell Cardiol. 2005;38:895–905. - PMC - PubMed
    1. Miki T, Seino S. Roles of KATP channels as metabolic sensors in acute metabolic changes. J Mol Cell Cardiol. 2005;38:917–925. - PubMed
    1. Nichols CG. KATP channels as molecular sensors of cellular metabolism. Nature. 2006;440:470–476. - PubMed
    1. Ashcroft FM. ATP-sensitive K+ channels and disease: from molecule to malady. Am J Physiol Endocrinol Metab. 2007;293:E880–E889. - PubMed
    1. Reyes S, Park S, Terzic A, Alekseev AE. KATP channels process nucleotide signals in muscle thermogenic response. Crit Rev Biochem Mol Biol. 2010;45:506–519. - PMC - PubMed

Publication types

MeSH terms