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Human PPID Protein expressed in Wheat germ - ABIN1315874
Nguyen, Stevens, Kohr, Steenbergen, Sack, Murphy: Cysteine 203 of cyclophilin D is critical for cyclophilin D activation of the mitochondrial permeability transition pore. in The Journal of biological chemistry 2011
Show all 2 Pubmed References
Binding of signal transducer and activator of transcription 3 (STAT3) to cyclophilin D (CypD) was important for reducing mitochondrial reactive oxygen species (ROS) production after oxidative stress.
Data show that cyclophilin 40 (CyP40) interacts with and dissolves amyloids forming proteins tau and alpha-synuclein aggregates.
This review discusses previous studies to provide comprehensive information on the physiological role of cyclophilin D as well as PTP opening in the cell that can be taken into consideration for the development of new PTP inhibitors. [review]
The influx of unfolded p53 (show TP53 Proteins) into the mitochondrial matrix in response to oxidative stress indirectly activates the normally inhibited CypD by displacing it from Trap1 (show TRAP1 Proteins) complexes. This activates CypD's isomerase activity. Liberated CypD then isomerizes multiple proteins including p53 (show TP53 Proteins) (causing p53 (show TP53 Proteins) aggregation) and the structural components of the mPTP (show PTPN2 Proteins) pore, inducing pore opening.
The present study is to investigate the role of CypD in regulating the mitochondrial dynamics relevant to oxidative stress induced (show SQSTM1 Proteins) neuron dysfunctions.
CyPD regulates mitochondrial metabolism, and likely cell survival, by promoting more efficient electrons flow through the respiratory chain via increased supercomplex formation
cyclophilin D may modify mitochondrial features by inducing the translocation of molecules to the mitochondria through the mechanism associated with cellular energy metabolism
The thermodynamics of binding of Cyp-40 to Hsp90 (show HSP90 Proteins) shows remarkable temperature sensitivity in the physiological temperature range.
cyclophilin-D protein could increase oxidative stress and cause endothelial cell injury and apoptosis. cyclophilin-D protein is the key factor in reactive oxygen species-induced mitochondrial damage, leading to apoptosis of endothelial cells.
Results show that CypD interacts with SPG7 and VDAC to form the mitochondrial permeability transition pore complex (PTP)and its CsA-binding region is necessary for PTP formation.
LKT-mediated cell death involve dynamin-2 and cyclophilin D.
CypD regulates complex I-induced ROS (show ROS1 Proteins) production in heart mitochondria and modulates the cardioprotective effect of isoflurane, sevoflurane, and desflurane.
Murine eosinophil necrosis is regulated in vitro and in vivo by cyclophilin D.
Cyclophilin D is an important but non-obligatory regulator of mitoflash activity in cardiac muscle, whereas it is dispensable in the skeletal muscle, due in part to differential cyclophilin D expression.
Suggest that cyclosporin A-mediated CypD inhibition may provide a promising therapeutic potential for protecting retinal ganglion cells against ischemic injury-mediated mitochondrial dysfunction.
Loss of CypD results in changes in a number of mitochondrial proteins and metabolic pathways.
CypD directs mitochondria-to-nuclei inflammatory gene expression in normal and tumor cells
BAX/BAK-independent cell death did not require Cyclophilin D (CypD) expression, an important regulator of the mitochondrial permeability transition pore
At the whole muscle level, lack of cyclophilin-D does not protect against muscle atrophy, release of mitochondrial pro-apoptotic factors and activation of caspases following denervation.
mitochondrial permeability transition was increased by hypoxia-reoxygenation but was less in normoxic and hypoxia-reoxygenation Ppif(-/-) than wild type tubules
These findings point to a possible role of immunophilin (show FKBP1A Proteins) signal transduction pathways in astrocytic modulation of neuronal activity at the tripartite synapse.
The protein encoded by this gene is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. This protein has been shown to possess PPIase activity and, similar to other family members, can bind to the immunosuppressant cyclosporin A.
peptidylprolyl isomerase D
, peptidylprolyl isomerase D (cyclophilin D)
, 40 kDa peptidyl-prolyl cis-trans isomerase D
, PPIase D
, cyclophilin 40
, cyclophilin D
, cyclophilin-related protein
, peptidyl-prolyl cis-trans isomerase D
, rotamase D
, 40 kDa peptidyl-prolyl cis-trans isomerase
, Cyclophilin D
, estrogen receptor-binding cyclophilin
, cytoplasmic cyclophilin D