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Article: The C Ring of the F1Fo ATP Synthase Forms the Mitochondrial Permeability Transition Pore: A Critical Appraisal.

Halestrap, Andrew P

2014 Volume 4, Page(s) 234

Language	English
Publishing date	2014-08-25
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2649216-7
ISSN	2234-943X
ISSN	2234-943X
DOI	10.3389/fonc.2014.00234
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Article ; Online: Identity, structure, and function of the mitochondrial permeability transition pore: controversies, consensus, recent advances, and future directions.

Bernardi, Paolo / Gerle, Christoph / Halestrap, Andrew P / Jonas, Elizabeth A / Karch, Jason / Mnatsakanyan, Nelli / Pavlov, Evgeny / Sheu, Shey-Shing / Soukas, Alexander A

Cell death and differentiation

2023 Volume 30, Issue 8, Page(s) 1869–1885

Abstract: The mitochondrial permeability transition (mPT) describes a ... ...

Abstract	The mitochondrial permeability transition (mPT) describes a Ca
MeSH term(s)	Mitochondrial Permeability Transition Pore/analysis ; Mitochondrial Permeability Transition Pore/metabolism ; Mitochondrial Membrane Transport Proteins/metabolism ; Consensus ; Mitochondria/metabolism ; Mitochondrial Membranes/metabolism
Chemical Substances	Mitochondrial Permeability Transition Pore ; Mitochondrial Membrane Transport Proteins
Language	English
Publishing date	2023-07-17
Publishing country	England
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1225672-9
ISSN	1476-5403 ; 1350-9047
ISSN (online)	1476-5403
ISSN	1350-9047
DOI	10.1038/s41418-023-01187-0
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Article ; Online: Monocarboxylic acid transport.

Halestrap, Andrew P

Comprehensive Physiology

2013 Volume 3, Issue 4, Page(s) 1611–1643

Abstract: Monocarboxylates such as lactate, pyruvate, and the ketone bodies play major roles in metabolism and must be transported across both the plasma membrane and mitochondrial inner membrane. A family of five proton-linked MonoCarboxylate Transporters (MCTs) ... ...

Abstract	Monocarboxylates such as lactate, pyruvate, and the ketone bodies play major roles in metabolism and must be transported across both the plasma membrane and mitochondrial inner membrane. A family of five proton-linked MonoCarboxylate Transporters (MCTs) is involved in the former and the mitochondrial pyruvate carrier (MPC) mediates the latter. In the intestine and kidney, two Sodium-coupled MonoCarboxylate Transporters (SMCTs) provide active transport of monocarboxylates across the apical membrane of the epithelial cells with MCTs on the basolateral membrane transporting the accumulated monocarboxylate into the blood. The kinetics and substrate and inhibitor specificities of MCTs, SMCTs, and the MPC have been well characterized and the molecular identity of the MCTs and SMCTs defined unequivocally. The identity of the MPC is less certain. The MCTs have been extensively studied and the three-dimensional structure of MCT1 has been modeled and a likely catalytic mechanism proposed. MCTs require the binding of a single transmembrane glycoprotein (either embigin or basigin) for activity. Regulation of MCT activity involves both transcriptional and posttranscriptional mechanisms, examples being upregulation of MCT1 by chronic exercise in red muscle (which oxidizes lactate) and in T-lymphocytes upon stimulation. MCT4 has properties that make it especially suited for lactic acid export by glycolytic cells and is upregulated by hypoxia. Some disease states are associated with modulation of plasma membrane and mitochondrial monocarboxylate transport and MCTs are promising drug targets for cancer chemotherapy. They may also be involved in drug uptake from the intestine and subsequent transport across the blood brain barrier.
MeSH term(s)	Amino Acid Sequence ; Animals ; Humans ; Molecular Sequence Data ; Monocarboxylic Acid Transporters/chemistry ; Monocarboxylic Acid Transporters/genetics ; Monocarboxylic Acid Transporters/metabolism ; Organ Specificity ; Substrate Specificity
Chemical Substances	Monocarboxylic Acid Transporters
Language	English
Publishing date	2013-11-21
Publishing country	United States
Document type	Journal Article ; Review
ISSN	2040-4603
ISSN (online)	2040-4603
DOI	10.1002/cphy.c130008
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Article ; Online: The SLC16 gene family - structure, role and regulation in health and disease.

Halestrap, Andrew P

Molecular aspects of medicine

2013 Volume 34, Issue 2-3, Page(s) 337–349

Abstract: The SLC16 gene family has fourteen members. Four (SLC16A1, SLC16A3, SLC16A7, and SLC16A8) encode monocarboxylate transporters (MCT1, MCT4, MCT2, and MCT3, respectively) catalysing the proton-linked transport of monocarboxylates such as l-lactate, ... ...

Abstract	The SLC16 gene family has fourteen members. Four (SLC16A1, SLC16A3, SLC16A7, and SLC16A8) encode monocarboxylate transporters (MCT1, MCT4, MCT2, and MCT3, respectively) catalysing the proton-linked transport of monocarboxylates such as l-lactate, pyruvate and ketone bodies across the plasma membrane. SLC16A2 encodes a high affinity thyroid hormone transporter (MCT8) and SLC16A10 an aromatic amino acid transporter (TAT1). The substrates and roles of the remaining eight members are unknown. All family members are predicted to have 12 transmembrane helices (TMs) with intracellular C- and N-termini and a large intracellular loop between TMs 6 and 7. This topology has been confirmed for MCT1 and a three-dimensional structure has been modelled that suggests a plausible molecular mechanism. For correct plasma membrane expression and activity MCTs1-4, but not MCT8, require association with basigin or embigin; these are glycoproteins with a single TM and 2-3 extracellular immunoglobulin domains. SLC16 family members are involved in a wide range of metabolic pathways including energy metabolism of the brain, skeletal muscle, heart and tumour cells, gluconeogenesis, T-lymphocyte activation, bowel metabolism, spermatogenesis, pancreatic β-cell malfunction, thyroid hormone metabolism, and drug transport. MCTs 1-4 have distinct properties, tissue distribution and subcellular localisation that are appropriate for these metabolic roles. Their potential as pharmacological targets has been recognised with the discovery of potent and specific MCT1 inhibitors that act as immunosuppressant drugs by preventing proliferation of T-lymphocytes. It is suggested that the development of other drugs specifically targeting different MCT isoforms may provide a novel approach to cancer chemotherapy.
MeSH term(s)	Animals ; Basigin/metabolism ; Caenorhabditis elegans ; Gene Expression Profiling ; Humans ; Lactic Acid/metabolism ; Longevity/physiology ; Membrane Glycoproteins/metabolism ; Models, Molecular ; Molecular Chaperones/metabolism ; Monocarboxylic Acid Transporters/genetics ; Monocarboxylic Acid Transporters/metabolism ; Monocarboxylic Acid Transporters/physiology ; Multigene Family/genetics ; Phylogeny ; Protein Conformation ; Pyruvic Acid/metabolism ; Symporters/genetics ; Symporters/metabolism ; Symporters/physiology ; Xenopus laevis
Chemical Substances	EMB protein, human ; Membrane Glycoproteins ; Molecular Chaperones ; Monocarboxylic Acid Transporters ; Symporters ; Basigin (136894-56-9) ; Lactic Acid (33X04XA5AT) ; Pyruvic Acid (8558G7RUTR)
Language	English
Publishing date	2013-04
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	197640-0
ISSN	1872-9452 ; 0098-2997
ISSN (online)	1872-9452
ISSN	0098-2997
DOI	10.1016/j.mam.2012.05.003
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Article ; Online: Quantification of active mitochondrial permeability transition pores using GNX-4975 inhibitor titrations provides insights into molecular identity.

Richardson, Andrew P / Halestrap, Andrew P

The Biochemical journal

2016 Volume 473, Issue 9, Page(s) 1129–1140

Abstract: Inhibition of the mitochondrial permeability transition pore (MPTP) by the novel inhibitor GNX-4975 was characterized. Titration of MPTP activity in de-energized rat liver mitochondria allowed determination of the number of GNX-4975-binding sites and ... ...

Abstract	Inhibition of the mitochondrial permeability transition pore (MPTP) by the novel inhibitor GNX-4975 was characterized. Titration of MPTP activity in de-energized rat liver mitochondria allowed determination of the number of GNX-4975-binding sites and their dissociation constant (Ki). Binding sites increased in number when MPTP opening was activated by increasing [Ca(2+)], phenylarsine oxide (PAO) or KSCN, and decreased when MPTP opening was inhibited with bongkrekic acid (BKA) or ADP. Values ranged between 9 and 50 pmol/mg of mitochondrial protein, but the Ki remained unchanged at ∼1.8 nM when the inhibitor was added before Ca(2+) However, when GNX-4975 was added after Ca(2+) it was much less potent with a Ki of ∼140 nM. These data imply that a protein conformational change is required to form the MPTP complex and generate the GNX-4975-binding site. Occupation of the latter with GNX-4975 prevents the Ca(2+) binding that triggers pore opening. We also demonstrated that GNX-4975 stabilizes an interaction between the adenine nucleotide translocase (ANT), held in its 'c' conformation with carboxyatractyloside (CAT), and the phosphate carrier (PiC) bound to immobilized PAO. No components of the F1Fo-ATP synthase bound significantly to immobilized PAO. Our data are consistent with our previous proposal that the MPTP may form at an interface between the PiC and ANT (or other similar mitochondrial carrier proteins) when they adopt novel conformations induced by factors that sensitize the MPTP to [Ca(2+)]. We propose that GNX-4975 binds to this interface preventing a calcium-triggered event that opens the interface into a pore.
MeSH term(s)	Adenine Nucleotide Translocator 1/metabolism ; Animals ; Binding Sites ; Calcium/metabolism ; Male ; Mitochondria, Liver/metabolism ; Mitochondrial Membrane Transport Proteins/antagonists & inhibitors ; Mitochondrial Membrane Transport Proteins/metabolism ; Mitochondrial Permeability Transition Pore ; Oxidoreductases Acting on CH-NH Group Donors/metabolism ; Proton-Translocating ATPases/metabolism ; Rats ; Rats, Wistar
Chemical Substances	Adenine Nucleotide Translocator 1 ; Mitochondrial Membrane Transport Proteins ; Mitochondrial Permeability Transition Pore ; Oxidoreductases Acting on CH-NH Group Donors (EC 1.5.-) ; N(1)-acetylpolyamine oxidase, human (EC 1.5.3.-) ; Proton-Translocating ATPases (EC 3.6.3.14) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2016-02-26
Publishing country	England
Document type	Journal Article
ZDB-ID	2969-5
ISSN	1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
ISSN (online)	1470-8728
ISSN	0006-2936 ; 0306-3275 ; 0264-6021
DOI	10.1042/BCJ20160070
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Article ; Online: The mitochondrial pyruvate carrier: has it been unearthed at last?

Halestrap, Andrew P

Cell metabolism

2012 Volume 16, Issue 2, Page(s) 141–143

Abstract: The mitochondrial pyruvate carrier (MPC) is essential for several major pathways of carbohydrate, fat, and amino acid metabolism, yet its molecular identity has remained elusive. Two recent papers in Science (Herzig et al., 2012; Bricker et al., 2012) ... ...

Abstract	The mitochondrial pyruvate carrier (MPC) is essential for several major pathways of carbohydrate, fat, and amino acid metabolism, yet its molecular identity has remained elusive. Two recent papers in Science (Herzig et al., 2012; Bricker et al., 2012) implicate three newly identified inner mitochondrial membrane proteins as MPC components.
Language	English
Publishing date	2012-09-13
Publishing country	United States
Document type	Comment ; Journal Article
ZDB-ID	2176834-1
ISSN	1932-7420 ; 1550-4131
ISSN (online)	1932-7420
ISSN	1550-4131
DOI	10.1016/j.cmet.2012.07.013
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Article ; Online: The monocarboxylate transporter family--Structure and functional characterization.

Halestrap, Andrew P

IUBMB life

2012 Volume 64, Issue 1, Page(s) 1–9

Abstract: Monocarboxylate transporters (MCTs) catalyze the proton-linked transport of monocarboxylates such as L-lactate, pyruvate, and the ketone bodies across the plasma membrane. There are four isoforms, MCTs 1-4, which are known to perform this function in ... ...

Abstract	Monocarboxylate transporters (MCTs) catalyze the proton-linked transport of monocarboxylates such as L-lactate, pyruvate, and the ketone bodies across the plasma membrane. There are four isoforms, MCTs 1-4, which are known to perform this function in mammals, each with distinct substrate and inhibitor affinities. They are part of the larger SLC16 family of solute carriers, also known as the MCT family, which has 14 members in total, all sharing conserved sequence motifs. The family includes a high-affinity thyroid hormone transporter (MCT8), an aromatic amino acid transporter (T-type amino acid transporter 1/MCT10), and eight orphan members yet to be characterized. MCTs were predicted to have 12 transmembrane helices (TMs) with intracellular C- and N-termini and a large intracellular loop between TMs 6 and 7, and this was confirmed by labeling studies and proteolytic digestion. Site-directed mutagenesis has identified key residues required for catalysis and inhibitor binding and enabled the development of a molecular model of MCT1 in both inward and outward facing conformations. This suggests a likely mechanism for the translocation cycle. Although MCT family members are not themselves glycosylated, MCTs1-4 require association with a glycosylated ancillary protein, either basigin or embigin, for their correct translocation to the plasma membrane. These ancillary proteins have a single transmembrane domain and two to three extracellular immunoglobulin domains. They must remain closely associated with MCTs1-4 to maintain transporter activity. MCT1, MCT3, and MCT4 bind preferentially to basigin and MCT2 to embigin. The choice of binding partner does not affect substrate specificity or kinetics but can influence inhibitor specificity.
MeSH term(s)	Animals ; Carboxylic Acids/chemistry ; Carboxylic Acids/metabolism ; Cell Membrane/metabolism ; Humans ; Monocarboxylic Acid Transporters/chemistry ; Monocarboxylic Acid Transporters/metabolism ; Monocarboxylic Acid Transporters/physiology ; Protein Binding ; Protein Structure, Tertiary ; Substrate Specificity
Chemical Substances	Carboxylic Acids ; Monocarboxylic Acid Transporters
Language	English
Publishing date	2012-01
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1492141-8
ISSN	1521-6551 ; 1521-6543
ISSN (online)	1521-6551
ISSN	1521-6543
DOI	10.1002/iub.573
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Article ; Online: The mitochondrial permeability transition: a current perspective on its identity and role in ischaemia/reperfusion injury.

Halestrap, Andrew P / Richardson, Andrew P

Journal of molecular and cellular cardiology

2014 Volume 78, Page(s) 129–141

Abstract: The mitochondrial permeability transition pore (MPTP) is a non-specific pore that opens in the inner mitochondrial membrane (IMM) when matrix [Ca(2+)] is high, especially when accompanied by oxidative stress, high [Pi] and adenine nucleotide depletion. ... ...

Abstract	The mitochondrial permeability transition pore (MPTP) is a non-specific pore that opens in the inner mitochondrial membrane (IMM) when matrix [Ca(2+)] is high, especially when accompanied by oxidative stress, high [Pi] and adenine nucleotide depletion. Such conditions occur during ischaemia and subsequent reperfusion, when MPTP opening is known to occur and cause irreversible damage to the heart. Matrix cyclophilin D facilitates MPTP opening and is the target of its inhibition by cyclosporin A that is cardioprotective. Less certainty exists over the composition of the pore itself, with structural and/or regulatory roles proposed for the adenine nucleotide translocase, the phosphate carrier and the FoF1 ATP synthase. Here we critically review the supporting data for the role of each and suggest that they may interact with each other through their bound cardiolipin to form the ATP synthasome. We propose that under conditions favouring MPTP opening, calcium-triggered conformational changes in these proteins may perturb the interface between them generating the pore. Proteins associated with the outer mitochondrial membrane (OMM), such as members of the Bcl-2 family and hexokinase (HK), whilst not directly involved in pore formation, may regulate MPTP opening through interactions between OMM and IMM proteins at "contact sites". Recent evidence suggests that cardioprotective protocols such as preconditioning inhibit MPTP opening at reperfusion by preventing the loss of mitochondrial bound HK2 that stabilises these contact sites. Contact site breakage both sensitises the MPTP to [Ca(2+)] and facilitates cytochrome c loss from the intermembrane space leading to greater ROS production and further MPTP opening. This article is part of a Special Issue entitled "Mitochondria: From Basic Mitochondrial Biology to Cardiovascular Disease".
MeSH term(s)	Animals ; Biological Transport ; Calcium/metabolism ; Humans ; Mitochondria/metabolism ; Mitochondrial Membrane Transport Proteins/metabolism ; Mitochondrial Permeability Transition Pore ; Molecular Targeted Therapy ; Oxidative Stress ; Permeability ; Reperfusion Injury/drug therapy ; Reperfusion Injury/metabolism ; Reperfusion Injury/prevention & control
Chemical Substances	Mitochondrial Membrane Transport Proteins ; Mitochondrial Permeability Transition Pore ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2014-08-30
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	80157-4
ISSN	1095-8584 ; 0022-2828
ISSN (online)	1095-8584
ISSN	0022-2828
DOI	10.1016/j.yjmcc.2014.08.018
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Article ; Online: A pore way to die: the role of mitochondria in reperfusion injury and cardioprotection.

Halestrap, Andrew P

Biochemical Society transactions

2010 Volume 38, Issue 4, Page(s) 841–860

Abstract: In addition to their normal physiological role in ATP production and metabolism, mitochondria exhibit a dark side mediated by the opening of a non-specific pore in the inner mitochondrial membrane. This mitochondrial permeability transition pore (MPTP) ... ...

Abstract	In addition to their normal physiological role in ATP production and metabolism, mitochondria exhibit a dark side mediated by the opening of a non-specific pore in the inner mitochondrial membrane. This mitochondrial permeability transition pore (MPTP) causes the mitochondria to breakdown rather than synthesize ATP and, if unrestrained, leads to necrotic cell death. The MPTP is opened in response to Ca(2+) overload, especially when accompanied by oxidative stress, elevated phosphate concentration and adenine nucleotide depletion. These conditions are experienced by the heart and brain subjected to reperfusion after a period of ischaemia as may occur during treatment of a myocardial infarction or stroke and during heart surgery. In the present article, I review the properties, regulation and molecular composition of the MPTP. The evidence for the roles of CyP-D (cyclophilin D), the adenine nucleotide translocase and the phosphate carrier are summarized and other potential interactions with outer mitochondrial membrane proteins are discussed. I then review the evidence that MPTP opening mediates cardiac reperfusion injury and that MPTP inhibition is cardioprotective. Inhibition may involve direct pharmacological targeting of the MPTP, such as with cyclosporin A that binds to CyP-D, or indirect inhibition of MPTP opening such as with preconditioning protocols. These invoke complex signalling pathways to reduce oxidative stress and Ca(2+) load. MPTP inhibition also protects against congestive heart failure in hypertensive animal models. Thus the MPTP is a very promising pharmacological target for clinical practice, especially once more specific drugs are developed.
MeSH term(s)	Animals ; Cardiomegaly/complications ; Cardiotonic Agents/pharmacology ; Cardiotonic Agents/therapeutic use ; Cytoprotection/drug effects ; Cytoprotection/physiology ; Drug Delivery Systems ; Heart/physiology ; Heart/physiopathology ; Heart Failure/etiology ; Humans ; Mitochondria/pathology ; Mitochondria/physiology ; Mitochondrial Membrane Transport Proteins/antagonists & inhibitors ; Mitochondrial Membrane Transport Proteins/metabolism ; Mitochondrial Membrane Transport Proteins/physiology ; Models, Biological ; Myocardial Reperfusion Injury/metabolism ; Myocardial Reperfusion Injury/pathology ; Myocardial Reperfusion Injury/physiopathology ; Myocardial Reperfusion Injury/prevention & control ; Myocardium/metabolism ; Myocardium/pathology
Chemical Substances	Cardiotonic Agents ; Mitochondrial Membrane Transport Proteins ; mitochondrial permeability transition pore
Language	English
Publishing date	2010-08
Publishing country	England
Document type	Lectures ; Research Support, Non-U.S. Gov't
ZDB-ID	184237-7
ISSN	1470-8752 ; 0300-5127
ISSN (online)	1470-8752
ISSN	0300-5127
DOI	10.1042/BST0380841
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Article ; Online: The roles of cytosolic and intramitochondrial Ca

Rutter, Guy A / McCormack, James G / Halestrap, Andrew P / Denton, Richard M

The Journal of biological chemistry

2020 Volume 295, Issue 30, Page(s) 10506

MeSH term(s)	Animals ; Calcium/metabolism ; Calcium Channels/metabolism ; Mitochondria/metabolism ; Oxidative Phosphorylation ; Pyruvic Acid/metabolism
Chemical Substances	Calcium Channels ; Pyruvic Acid (8558G7RUTR) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2020-07-24
Publishing country	United States
Document type	Letter ; Comment
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.L120.013975
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