NDLI: Genetic Dissection of the Permeability Transition Pore

Content Provider	Springer Nature Link
Author	Forte, Michael Bernardi, Paolo
Copyright Year	2005
Abstract	The permeability transition pore (PTP) regulates the structural re-organization of mitochondria in response to changes in cellular Ca$^{2+}$ and is thought to be an important participant in mitochondrial responses to cell death signals. Although the proteins forming the PTP have yet to be rigorously identified, recent examination of the response of mitochondria, cells and tissues lacking putative components of the PTP have been reported. Studies on mitochondria lacking cyclophilin D (CyP-D) have proved that this protein is the target for PTP inhibition by CsA; yet they have also unequivocally demonstrated that the PTP can form and open in the absence of CyP-D. Likewise, studies in mice lacking the two adenine nucleotide translocators expressed in this species have shown that a functional PTP can form in the absence of these proteins. Thus, the inner mitochondrial membrane components of the PTP remain to be identified, and the absence of CyP-D may not preclude PTP opening in vivo – a finding that questions the conclusion that the PTP participates in cell death pathways only in response to a restricted set of challenges.
Starting Page	121
Ending Page	128
Page Count	8
File Format	PDF
ISSN	0145479X
Journal	Journal of Bioenergetics and Biomembranes
Volume Number	37
Issue Number	3
e-ISSN	15736881
Language	English
Publisher	Kluwer Academic Publishers-Plenum Publishers
Publisher Date	2005-01-01
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Permeability transition pore cyclophilin D adenine nucleotide translocator cell death apoptosis necrosis “knock-out” mice calcium Organic Chemistry Biochemistry Animal Biochemistry Animal Anatomy / Morphology / Histology Bioorganic Chemistry
Content Type	Text
Resource Type	Article
Subject	Cell Biology Physiology

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