TY - JOUR
T1 - The adenine nucleotide translocator in apoptosis
AU - Belzacq, Anne Sophie
AU - Vieira, Helena L.A.
AU - Kroemer, Guido
AU - Brenner, Catherine
N1 - Funding Information:
This work has been supported by a special grant from the French National League against Cancer as well as grants from Agence nationale pour la recherche sur le SIDA, and European Commission (to G.K.), Fondation pour la recherche médicale (to G.K. and C.B.), Association pour la recherche sur le cancer (to C.B.), and French Ministry of Science (to C.B.). A-S.B. received a Fondation pour la recherche médicale fellowship. H.L.A.V. receives a fellowship from the Fundação para a Ciência e a Tecnologia PRAXIS XXI, Portugal.
PY - 2002/1/1
Y1 - 2002/1/1
N2 - Alteration of mitochondrial membrane permeability is a central mechanism leading invariably to cell death, which results, at least in part, from the opening of the permeability transition pore complex (PTPC). Indeed, extended PTPC opening is sufficient to trigger an increase in mitochondrial membrane permeability and apoptosis. Among the various PTPC components, the adenine nucleotide translocator (ANT) appears to act as a bi-functional protein which, on the one hand, contributes to a crucial step of aerobic energy metabolism, the ADP/ATP translocation, and on the other hand, can be converted into a pro-apoptotic pore under the control of onco- and anti-oncoproteins from the Bax/Bcl-2 family. In this review, we will discuss recent advances in the cooperation between ANT and Bax/Bcl-2 family members, the multiplicity of agents affecting ANT pore function and the putative role of ANT isoforms in apoptosis control.
AB - Alteration of mitochondrial membrane permeability is a central mechanism leading invariably to cell death, which results, at least in part, from the opening of the permeability transition pore complex (PTPC). Indeed, extended PTPC opening is sufficient to trigger an increase in mitochondrial membrane permeability and apoptosis. Among the various PTPC components, the adenine nucleotide translocator (ANT) appears to act as a bi-functional protein which, on the one hand, contributes to a crucial step of aerobic energy metabolism, the ADP/ATP translocation, and on the other hand, can be converted into a pro-apoptotic pore under the control of onco- and anti-oncoproteins from the Bax/Bcl-2 family. In this review, we will discuss recent advances in the cooperation between ANT and Bax/Bcl-2 family members, the multiplicity of agents affecting ANT pore function and the putative role of ANT isoforms in apoptosis control.
KW - ADP/ATP exchange
KW - Bcl-2
KW - Liposome
KW - Mitochondrion
KW - Oncogene
KW - Permeability transition
UR - http://www.scopus.com/inward/record.url?scp=0036478993&partnerID=8YFLogxK
U2 - 10.1016/S0300-9084(02)01366-4
DO - 10.1016/S0300-9084(02)01366-4
M3 - Article
C2 - 12022947
AN - SCOPUS:0036478993
SN - 0300-9084
VL - 84
SP - 167
EP - 176
JO - Biochimie
JF - Biochimie
IS - 2-3
ER -