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Parkin functions to blunt excessive CHOP to prevent maladaptive ER stress-induced cell death and adverse cardiac ventricular remodeling.
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data suggested that suppressed Sirt3-Foxo3A-Parkin signaling mediated downregulation of mitophagy may play a vital role in the development of diabetic cardiomyopathy.
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Overexpression of parkin resulted in a significant reduction of total-eNOS and p-eNOS in parallel with the downregulation of ERRalpha (a regulator of eNOS) protein and the enhancement of ERRalpha ubiquitination.
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Parkin mice carrying a deletion in exon 3 display impairments in the main pathway responsible for maintaining BH4 levels in the CNS, an essential cofactor for dopamine synthesis, under inflammatory conditions. Concomitant to this alteration, striatum cells do not upregulate BDNF to confer neuroprotection in LPS-exposed mice, displaying an increased number of mitochondria of smaller size with perinuclear clustering.
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the results indicate that PICK1 is a potent inhibitor of Parkin, and the reduction of PICK1 enhances the protective effect of Parkin.
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PINK1 and PARK2 suppress pancreatic tumorigenesis through control of mitochondrial iron-mediated immunometabolism
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When fed with iron-supplemented diet, DMT1-expressing mice exhibit rather selective accumulation of iron in the substantia nigra but otherwise seem normal. Parkin expression is also enhanced, likely as a neuroprotective response. When DMT1 is overexpressed against a Parkin null background, the double-mutant mice similarly resisted a disease phenotype when fed with iron or manganese, but greater susceptibility to 6-OHDA.
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Bnip3l knockout (bnip3l(-/-)) impaired mitophagy and aggravated cerebral I-R (ischemia-reperfusion) injury in mice, which can be rescued by BNIP3L overexpression. The rescuing effects of BNIP3L overexpression can be observed in park2(-/-) mice, which showed mitophagy deficiency after I-R.
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Parkin acts as a regulator of microtubule system during neuronal aging.
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The expression of PINK1 and Parkin were elevated in white adipose tissue in obese mice.
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crossed Parkin knockouts to the Twinkle-TG mouse in which mtDNA deletions are increased specifically in substantia nigra to determine the effect of increased deletion mutagenesis in the absence of mitochondrial quality control
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These findings reveal parkin-mediated cytoprotective mechanisms against misfolded SOD1 toxicity.
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Park2 deficiency exacerbates ethanol-induced dopaminergic neuron damage through p38 kinase dependent inhibition of autophagy and mitochondrial function.
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PARK2-dependent acidic postconditioning -induced mitophagy renders the brain resistant to ischemic injury.
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Our results indicate that strict maternal transmission of mitochondria relies on mitophagy and uncover a collaboration between MUL1 and PARKIN in this process.
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an impaired PINK1-PARK2-mediated neuroimmunology pathway contributes to septic death.
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These findings suggest that insufficient mitophagy-mediated PDGFR/PI3K/AKT activation, which is mainly attributed to reduced PARK2 expression, is a potent underlying mechanism for myofibroblast differentiation and proliferation in fibroblastic foci formation during idiopathic pulmonary fibrosis pathogenesis
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Mfn2 downregulation or the exogenous expression of normal Parkin restored cytosolic Ca(2+) transients in fibroblasts from patients with PARK2 mutations, a catalytically inactive Parkinson's disease (PD)-related Parkin variant had no effect. Parkin is directly involved in regulating ER-mitochondria contacts and provide new insight into the role of the loss of Parkin function in PD development
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Our results provide a molecular explanation for the contribution of Drp1 to the pathogenesis of sporadic Parkinson's disease (PD). These findings indicate that the SNO-Parkin pathway may be a novel therapeutic target to treat PD
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These results suggest a previously unidentified role of parkin in mediating endotoxin-induced endothelial proinflammatory signaling and indicate that it may play a critical role in acute inflammation.
