Biomaterial Database

The Role of Adenine Nucleotide Translocase in the Mitochondrial Permeability Transition. 2020

Nickolay Brustovetsky

Department of Pharmacology and Toxicology, Stark Neurosciences Research Institute, Indiana University School of Medicine, Indianapolis, IN 46202, USA.

The mitochondrial permeability transition, a Ca2+-induced significant increase in permeability of the inner mitochondrial membrane, plays an important role in various pathologies. The mitochondrial permeability transition is caused by induction of the permeability transition pore (PTP). Despite significant effort, the molecular composition of the PTP is not completely clear and remains an area of hot debate. The Ca2+-modified adenine nucleotide translocase (ANT) and F0F1 ATP synthase are the major contenders for the role of pore in the PTP. This paper briefly overviews experimental results focusing on the role of ANT in the mitochondrial permeability transition and proposes that multiple molecular entities might be responsible for the conductance pathway of the PTP. Consequently, the term PTP cannot be applied to a single specific protein such as ANT or a protein complex such as F0F1 ATP synthase, but rather should comprise a variety of potential contributors to increased permeability of the inner mitochondrial membrane.

UI	MeSH Term	Description	Entries
D008954	Models, Biological	Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.	Biological Model,Biological Models,Model, Biological,Models, Biologic,Biologic Model,Biologic Models,Model, Biologic
D011485	Protein Binding	The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.	Plasma Protein Binding Capacity,Binding, Protein
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000081406	Peptidyl-Prolyl Isomerase F	A member of the cyclophilins family of isomerases which plays a role in the regulation of the permeability transition pore in mitochondria. The protein has the alias name cyclophilin D which is also the alias name for the related protein Peptidyl-Prolyl Isomerase D.	Cyclophilin D, PPIF,Cyclophilin F,Mitochondrial Cyclophilin D,PPIF Cyclophilin,Peptidylprolyl Isomerase F,Cyclophilin D, Mitochondrial,Cyclophilin, PPIF,D, PPIF Cyclophilin,PPIF Cyclophilin D,Peptidyl Prolyl Isomerase F
D000083162	Mitochondrial Permeability Transition Pore	A multiprotein inner mitochondrial complex which opens only under certain pathological conditions (e.g., OXIDATIVE STRESS) uncoupling the membrane leading to APOPTOSIS and MITOCHONDRIAL TRANSMEMBRANE PERMEABILITY-DRIVEN NECROSIS particularly in CARDIOMYOCYTES during MYOCARDIAL REPERFUSION INJURY.	Mitochondrial Megachannel,Mitochondrial Permeability Transition Pore (mPTP),mPTP Protein
D000226	Mitochondrial ADP, ATP Translocases	A class of nucleotide translocases found abundantly in mitochondria that function as integral components of the inner mitochondrial membrane. They facilitate the exchange of ADP and ATP between the cytosol and the mitochondria, thereby linking the subcellular compartments of ATP production to those of ATP utilization.	ADP,ATP Carrier,ADP,ATP Translocator Protein,Adenine Nucleotide Translocase,ADP Translocase,ATP Translocase,ATP,ADP-Carrier,ATP-ADP Translocase,Adenine Nucleotide Carrier (Mitochondrial),Mitochondrial ADP-ATP Carriers,ADP-ATP Carriers, Mitochondrial,Mitochondrial ADP ATP Carriers
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia