Modulation and Pharmacology of the Mitochondrial Permeability Transition: A Journey from F-ATP Synthase to ANT
The permeability transition (PT) is an increased permeation of the inner mitochondrial membrane due to the opening of the PT pore (PTP), a Ca<sup>2+</sup>-activated high conductance channel involved in Ca<sup>2+</sup> homeostasis and cell death. Alterations of the PTP have be...
Guardado en:
Autores principales: | , , , |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
MDPI AG
2021
|
Materias: | |
Acceso en línea: | https://doaj.org/article/fe3c2f7d65894b47a6f200869f31c7ba |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
id |
oai:doaj.org-article:fe3c2f7d65894b47a6f200869f31c7ba |
---|---|
record_format |
dspace |
spelling |
oai:doaj.org-article:fe3c2f7d65894b47a6f200869f31c7ba2021-11-11T18:28:19ZModulation and Pharmacology of the Mitochondrial Permeability Transition: A Journey from F-ATP Synthase to ANT10.3390/molecules262164631420-3049https://doaj.org/article/fe3c2f7d65894b47a6f200869f31c7ba2021-10-01T00:00:00Zhttps://www.mdpi.com/1420-3049/26/21/6463https://doaj.org/toc/1420-3049The permeability transition (PT) is an increased permeation of the inner mitochondrial membrane due to the opening of the PT pore (PTP), a Ca<sup>2+</sup>-activated high conductance channel involved in Ca<sup>2+</sup> homeostasis and cell death. Alterations of the PTP have been associated with many pathological conditions and its targeting represents an incessant challenge in the field. Although the modulation of the PTP has been extensively explored, the lack of a clear picture of its molecular nature increases the degree of complexity for any target-based approach. Recent advances suggest the existence of at least two mitochondrial permeability pathways mediated by the F-ATP synthase and the ANT, although the exact molecular mechanism leading to channel formation remains elusive for both. A full comprehension of this to-pore conversion will help to assist in drug design and to develop pharmacological treatments for a fine-tuned PT regulation. Here, we will focus on regulatory mechanisms that impinge on the PTP and discuss the relevant literature of PTP targeting compounds with particular attention to F-ATP synthase and ANT.Andrea CarrerClaudio LaquatraLudovica TommasinMichela CarraroMDPI AGarticlepermeability transitioncalciumF-ATP synthaseadenine nucleotide translocatorcyclophilin Dmitochondrial channelsOrganic chemistryQD241-441ENMolecules, Vol 26, Iss 6463, p 6463 (2021) |
institution |
DOAJ |
collection |
DOAJ |
language |
EN |
topic |
permeability transition calcium F-ATP synthase adenine nucleotide translocator cyclophilin D mitochondrial channels Organic chemistry QD241-441 |
spellingShingle |
permeability transition calcium F-ATP synthase adenine nucleotide translocator cyclophilin D mitochondrial channels Organic chemistry QD241-441 Andrea Carrer Claudio Laquatra Ludovica Tommasin Michela Carraro Modulation and Pharmacology of the Mitochondrial Permeability Transition: A Journey from F-ATP Synthase to ANT |
description |
The permeability transition (PT) is an increased permeation of the inner mitochondrial membrane due to the opening of the PT pore (PTP), a Ca<sup>2+</sup>-activated high conductance channel involved in Ca<sup>2+</sup> homeostasis and cell death. Alterations of the PTP have been associated with many pathological conditions and its targeting represents an incessant challenge in the field. Although the modulation of the PTP has been extensively explored, the lack of a clear picture of its molecular nature increases the degree of complexity for any target-based approach. Recent advances suggest the existence of at least two mitochondrial permeability pathways mediated by the F-ATP synthase and the ANT, although the exact molecular mechanism leading to channel formation remains elusive for both. A full comprehension of this to-pore conversion will help to assist in drug design and to develop pharmacological treatments for a fine-tuned PT regulation. Here, we will focus on regulatory mechanisms that impinge on the PTP and discuss the relevant literature of PTP targeting compounds with particular attention to F-ATP synthase and ANT. |
format |
article |
author |
Andrea Carrer Claudio Laquatra Ludovica Tommasin Michela Carraro |
author_facet |
Andrea Carrer Claudio Laquatra Ludovica Tommasin Michela Carraro |
author_sort |
Andrea Carrer |
title |
Modulation and Pharmacology of the Mitochondrial Permeability Transition: A Journey from F-ATP Synthase to ANT |
title_short |
Modulation and Pharmacology of the Mitochondrial Permeability Transition: A Journey from F-ATP Synthase to ANT |
title_full |
Modulation and Pharmacology of the Mitochondrial Permeability Transition: A Journey from F-ATP Synthase to ANT |
title_fullStr |
Modulation and Pharmacology of the Mitochondrial Permeability Transition: A Journey from F-ATP Synthase to ANT |
title_full_unstemmed |
Modulation and Pharmacology of the Mitochondrial Permeability Transition: A Journey from F-ATP Synthase to ANT |
title_sort |
modulation and pharmacology of the mitochondrial permeability transition: a journey from f-atp synthase to ant |
publisher |
MDPI AG |
publishDate |
2021 |
url |
https://doaj.org/article/fe3c2f7d65894b47a6f200869f31c7ba |
work_keys_str_mv |
AT andreacarrer modulationandpharmacologyofthemitochondrialpermeabilitytransitionajourneyfromfatpsynthasetoant AT claudiolaquatra modulationandpharmacologyofthemitochondrialpermeabilitytransitionajourneyfromfatpsynthasetoant AT ludovicatommasin modulationandpharmacologyofthemitochondrialpermeabilitytransitionajourneyfromfatpsynthasetoant AT michelacarraro modulationandpharmacologyofthemitochondrialpermeabilitytransitionajourneyfromfatpsynthasetoant |
_version_ |
1718431860659322880 |