Evidence for the existence of an inner membrane anion channel in mitochondria

Garlid, Keith D.; Beavis, Andrew D.

doi:10.1016/0304-4173(87)90001-2

Cited by 122 publications

(54 citation statements)

References 135 publications

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“…At that time, Azzone et al [39] considered two possible efflux mechanisms : an electroncutral phosphate pump directly coupled to electron flow and Brierley's model [32, 401 in which phosphate efflux was passive and electrophoretic. In the light of the present results, Azzone's data are fully consistent with the involvement of the anion uniporter in the process of respiration driven mitochondria1 contraction (see [2]). …”

Section: Discussionsupporting

confidence: 90%

“…However, as Garlid and Bcavis [2] have discussed previously, it has potential roles in mitochondria1 volume homeostasis and in the regulation of the efficiency of oxidative phosphorylation. In view of the fact that the anion uniporter is normally almost inactive at pH values less than 7.2, it could be argued than this uniportcr may have no physiological role.…”

Section: Discussionmentioning

confidence: 97%

“…This inner membrane anion uniporter or channel, which has been given the acronym lMAC [2,31, has negligible activity in normal freshly isolated mitochondria [I]; however, rapid transport can be induced if the mitochondria are depleted of divalent cations [l] and/or the pH is raised to about 8 [I, 4-81. Transport through this pathway is characterized by three properties: (a) it is inhibited by matrix protons [l], (b) it is inhibited by N,W-dicyclohexylcarbodiimide (DCCD) [9, 201, and (c) it is inhibited by cationic amphiphiles such as propranolol [l I]. These properties distinguish the uniporter from other anion transport pathways in the inner membrane [9,1 I], including an anion-conducting pathway observed by patchclamping the inner membrane 1121.…”

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confidence: 99%

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The mitochondrial inner‐membrane anion channel possesses two mercurial‐reactive regulatory sites

Beavis¹

1989

European Journal of Biochemistry

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The mitochondrial inner membrane anion channel catalyzes the electrophoretic transport of a wide variety of anions and is inhibited by matrix divalent cations and protons. In this paper, evidence is provided that mersalyl and p-chloromercuribenzene-sulfonate each interact with this uniporter at two distinct sites. Binding to site 1 causes a shift in the pH dependence of transport, characterized by a decrease in the PICso for protons from about 7.8 to about 7.3, and leads to substantial stimulation of transport in the physiological pH range. This effect is not reversed by addition of thiols such as thioglycolate. Binding of mersalyl and p-chloromercuribenzenesulfonate to site 2 inhibits the transport of most anions including Pi, citrate, malonate, sulfate and ferrocyanide. The transport of C 1~ is inhibited about 60% by mersalyl, but is not inhibited by p-chloromercuribenzenesulfonate. These data suggest that inhibition is a stcric effect dependent on the size of the anion and the size of the R group of the mercurial. This inhibition is reversed by thioglycolate. Dose/response curves indicate that mersalyl binds to site 1 as the dose increased from 7 to 13 nmol/mg, whereas it binds to site 2 as the dose is increased from 10 to 18 nmol/mg. Thus, at certain pH values both stimulatory and inhibitory phases can be seen in the same dose/ response curve.

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Section: Discussionsupporting

confidence: 90%

Section: Discussionmentioning

confidence: 97%

mentioning

confidence: 99%

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The mitochondrial inner‐membrane anion channel possesses two mercurial‐reactive regulatory sites

Beavis¹

1989

European Journal of Biochemistry

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“…On the basis of data obtained with nonelectrophysiological methods, the existence of a high-conductance anion uniporter in the inner membrane of mitochondria has already been postulated by some authors (for reviews, see Garlid and Beavis, 1986;Beavis, 1989). It has been hypothesized that this channel would function under abnormal conditions, namely a high matrix pH or depletion of divalent cations at physiological pH.…”

Section: Discussionmentioning

confidence: 97%

Further investigation on the high-conductance ion channel of the inner membrane of mitochondria

Sorgato

Morán

Pinto

et al. 1989

J Bioenerg Biomembr

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By use of the patch-clamp technique, the inner membrane of mouse liver and heart mitochondria is shown to contain a highly conductive (around t00 pS in symmetrical 150 mM KC1) and voltage-dependent ion channel. This channel closely resembles that previously found in cuprizone-treated mouse liver inner mitochondrial membrane. The paper discusses the electrical properties of the channel and its possible physiological function. The reconstitution in giant liposomes of a partially purified ox heart inner membrane fraction containing the channel and the use of various inhibitors are also presented.

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“…These studies have supported the results obtained in other systems as far as the effect of different pharmacological agents on mitoK ATP . There are limitations associated with this technique, including the use of supraphysiological ion gradients, nucleotide concentrations or metabolic substrates, hypoosmotic conditions of the experiments to maintain linearity of the response, and the loss of normal cytoskeletal architecture [22,23]. Nevertheless, this approach is advantageous as compared to the reconstitution studies in that the mitochondrial channels and other proteins are intact, and that the pharmacological reagents can be applied directly to the mitochondria.…”

Section: 12mentioning

confidence: 99%

Mitochondrial K channels in cell survival and death

Ardehali¹,

O’Rourke²

2005

Journal of Molecular and Cellular Cardiology

196

151

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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.

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Evidence for the existence of an inner membrane anion channel in mitochondria

Cited by 122 publications

References 135 publications

The mitochondrial inner‐membrane anion channel possesses two mercurial‐reactive regulatory sites

The mitochondrial inner‐membrane anion channel possesses two mercurial‐reactive regulatory sites

Further investigation on the high-conductance ion channel of the inner membrane of mitochondria

Mitochondrial K channels in cell survival and death

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