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
Review
. 2005 Jul;39(1):7-16.
doi: 10.1016/j.yjmcc.2004.12.003. Epub 2005 Feb 19.

Mitochondrial K(ATP) channels in cell survival and death

Affiliations
Review

Mitochondrial K(ATP) channels in cell survival and death

Hossein Ardehali et al. J Mol Cell Cardiol. 2005 Jul.

Abstract

Since the discovery of the mitochondrial ATP-sensitive potassium channel (mitoK(ATP)) more than 13 years ago, it has been implicated in the processes of ischemic preconditioning (IPC), apoptosis and mitochondrial matrix swelling. Different approaches have been employed to characterize the pharmacological profile of the channel, and these studies strongly suggest that cellular protection well correlates with the opening of mitoK(ATP). However, there are many questions regarding mitoK(ATP) that remain to be answered. These include the very existence of mitoK(ATP) itself, its degree of importance in the process of IPC, its response to different pharmacological agents, and how its activation leads to the process of IPC and protection against cell death. Recent findings suggest that mitoK(ATP) may be a complex of multiple mitochondrial proteins, including some which have been suggested to be components of the mitochondrial permeability transition pore. However, the identity of the pore-forming unit of the channel and the details of the interactions between these proteins remain unclear. In this review, we attempt to highlight the recent advances in the physiological role of mitoK(ATP) and discuss the controversies and unanswered questions.

PubMed Disclaimer

Figures

Fig. 1
Fig. 1
Evidence for physical and functional interaction between SDH and mitoKATP. (A) Co-immunoprecipitation studies revealed that the 30- and 70-kDa components of SDH interact with four mitochondrial proteins: mABC1, ANT, ATPase and PIC. (B) Unitary K+ currents were recorded in lipid planar bilayers after fusion of native microsomes from a partially purified mitochondrial fraction containing the mABC1-SDH-PIC-ANT-ATPase protein complex. (C) The channel activity was increased by diazoxide, and the diazoxide activated channel activity was inhibited by 5-HD, glibenclamide and ATP. (D) Schematic presentation of the proteins associated with mitoKATP activity. The complex containing SDH-PIC-mABC1-ATPase-ANT is capable of transporting K+ with characteristics similar to those of mitoKATP. The pore-forming unit of the channel has not been characterized yet. Gli, glibenclamide; IMS, intermembrane space; Mito IM, mitochondrial inner membrane.

References

    1. Kloner RA, Bolli R, Marban E, Reinlib L, Braunwald E. Medical and cellular implications of stunning, hibernation, and preconditioning: an NHLBI workshop. Circulation. 1998;97:1848–67. - PubMed
    1. Murry CE, Jennings RB, Reimer KA. Preconditioning with ischemia: a delay of lethal cell injury in ischemic myocardium. Circulation. 1986;74:1124–36. - PubMed
    1. Cohen MV, Baines CP, Downey JM. Ischemic preconditioning: from adenosine receptor of KATP channel. Annu Rev Physiol. 2000;62:79–109. In Process Citation. - PubMed
    1. Zhang DX, Chen YF, Campbell WB, Zou AP, Gross GJ, Li PL. Characteristics and superoxide-induced activation of reconstituted myocardial mitochondrial ATP-sensitive potassium channels. Circ Res. 2001;89:1177–83. - PubMed
    1. Sato T, O'Rourke B, Marban E. Modulation of mitochondrial ATP-dependent K+ channels by protein kinase C. Circ Res. 1998;83:110–4. - PubMed

MeSH terms

LinkOut - more resources