Journal
FRONTIERS IN PHYSIOLOGY
Volume 11, Issue -, Pages -Publisher
FRONTIERS MEDIA SA
DOI: 10.3389/fphys.2020.00595
Keywords
cyclophilin D; permeability transition pore; mitochondrial function; ATP synthase; cyclosporine A; peptidyl-prolyl cis-trans isomerase
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Funding
- National Heart Lung and Blood Institute at the National Institutes of Health [ZIA HL002066, ZIA HL006059]
- Leducq Foundation [6CVD04]
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [ZIAHL002066] Funding Source: NIH RePORTER
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Cyclophilin D (CypD) is a mitochondrial peptidyl-prolyl cis-trans isomerase, well-known for regulating the mitochondrial permeability transition pore (PTP), a nonspecific large conductance pore whose opening leads to cell death and has been implicated in ischemia/reperfusion injury in multiple organs, in neurodegenerative disorders, and in muscular dystrophies. While the main target of CypD is a matter of ongoing research, inhibiting CypD protects in models of those diseases making it an interesting therapeutic target. The present review focuses on post-translational modifications of CypD that have been identified by recent studies, which can alter the regulation of the PTP and contribute to understanding the mechanisms of action of CypD.
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