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by performing protein profiling on isolated astrocytes we showed that an increase in astrocytic DJ-1 expression up-regulated a large group of proteins associated with redox regulation, inflammation and mitochondrial respiration. The majority of these proteins have also been shown to be regulated by Nrf2.
Melatonin, added together with MPTP or added once MPTP was removed, prevented and recovered, respectively, the parkinsonian phenotype once it was established, restoring gene expression and normal function of the parkin/PINK1/DJ-1/MUL1 loop and also the normal motor activity of the embryos.
These studies show that zDJ-1 is very similar to human DJ-1 and is evolutionarily conserved and expressed in dopaminergic neurons.
Interruption of LAMP-2 expression did not result in an increase of the steady-state protein levels of DJ-1 /PARK7, as it would have been expected. No change in DJ-1 /PARK7 protein levels were observed upon inhibition of lysosomal function with NH4Cl or NH4Cl plus leupeptin, or after activation of CMA by serum starvation for 24h.
DJ-1 protein concentration was significantly increased during the clinical phase in cerebrospinal fluid of sporadic Creutzfeldt-Jakob disease patients.
The molecular mechanism linking miR-221 to genetic forms of Parkinson's disease (PD) has not been studied. Consistent with the microarray data, miR-221 expression is also decreased in DJ-1(-/-) mouse brains. Re-introduction of wild-type DJ-1, but not its PD-linked pathogenic M26I mutant, restores miR-221 expression.
the results of this study suggest that male DJ-1 KO mice exhibit defects in brown adipose tissue (BAT) activity but do not gain more weight, revealing that BAT activity is not necessarily required for predisposing DJ-1 KO mice to obesity. Therefore, therapeutic targeting of DJ-1 in BAT could provide novel insights into the treatment of obesity.
Results suggest that protein deglycase DJ-1 (DJ-1) plays a role in bone homeostasis in normal physiology and in bone-associated pathology by negatively regulating osteoclastogenesis.
Silencing the DJ-1 gene uncovers a link between mitochondria-associated Parkinson's disease and mitotic pressure.
Low DJ-1 expression impairs synaptic vesicle endocytosis and reavailability at nerve terminals.
DJ-1 deficiency causes defects in astrocyte-mediated repair of brain damage.
In cultured neurons and forebrain samples from Dj1(-/-) animals, there was chloride damage and a profound structural remodeling of the mitochondrial respiratory chain.
DJ-1 has a role in glutamate uptake into astrocytes by regulating flotillin-1 and caveolin-1 expression
Network analysis reveals DJ-1/LDLR as common host proteins modulating pathogenesis of neurotropic viruses.
Induction of DJ-1 may serve as a novel regulator for hepatocellular carcinoma cell proliferation and HCC development possibly through enhanced MAPK signaling and inflammation.
chaperone-mediated autophagy protects mitochondrial function by degrading nonfunctional PARK7 and maintaining its homeostasis, and dysregulation of this pathway may contribute to the neuronal stress and death in Parkinson disease pathogenesis
Knockdown of DJ-1 attenuates Nurr1 activity.
These results demonstrate that DJ-1 KO mice display progressive signs of retinal/RPE degeneration in association with higher levels of oxidative stress markers. Collectively this analysis indicates that DJ-1 plays an important role in protecting photoreceptors and RPE from oxidative damage during aging
DJ-1 activates autophagy to alleviate cardiac hypertrophy.
These results indicate that up-regulation of GH in the lungs of DJ-1 KO mice may enhance the malignancy of B16F10 cells and nodule formation in pulmonary metastasis of melanoma.
DJ-1 is a powerful regulator of reactive oxygen species production as well as NHE1 expression and activity in CD4(+) T cells.
DJ-1 deficiency negatively regulates liver progenitor cells (LPC) proliferation by impairing the formation of LPC-associated fibrosis and inflammatory niches.
regulation of reactive oxygen species (ROS) and of the antioxidant protein DJ-1 (PARK-7), which increases with cancer progression and acts to lessen oxidative damage to malignant cells, in relationship with systemic mastocytosis severity, was examined.
The Parkinsonism-associated protein DJ-1 and its bacterial homologs deglycase 1/Hsp31, deglycase 2/YhbO, and deglycase 3/YajL function as deglycases that repair proteins and nucleotides from endogeneous glycation by glyoxal and methylglyoxal. DJ-1, deglycase 1 and deglycase 2 repair glyoxal- and methylglyoxal-glycated substrates, whereas deglycase 3 principally repairs glyoxal-glycated substrates.
Data of this study showed that DJ-1 downregulation increased apoptosis and reduced migration by regulating matrix metalloproteinase 2 and matrix metalloproteinase 9 in HTR-8/SVneo cells under both ambient and oxidative stress.
NRF2, DJ1 and SRNX1 are commonly expressed in diffusely infiltrating astrocytomas and they can be used in predicting patient prognosis.
Low PARK7 expression is associated with pre-term birth.
The results suggest that the impaired mitochondrial activity could be due to the broken interaction between DJ-1 and NDUFS3 and that downregulation of DJ-1 in sperm and testes contributes to AS pathogenesis.
In this review, we discuss the role as well as the underlying molecular mechanisms of DJ-1 in ocular diseases, including Fuchs endothelial corneal dystrophy (FECD), age-related macular degeneration (AMD), cataracts, and ocular neurodegenerative diseases, highlighting that DJ-1 may serve as a very striking therapeutic target for ocular diseases.
Novel candidate genes of the PARK7 interactome play a role in MS.
results indicated that oxDJ-1 levels in erythrocytes can be used as a marker for the differential diagnosis of Parkinson's disease
DJ-1 promoter polymorphism is associated with male infertility.
The PD-associated L166P mutant, but not wild-type DJ-1, directly binds to and is cleaved by the mitochondrial serine protease Omi at both serine residues 3 and 121.
DJ-1 plays a major role in various signaling pathways. Related to its anti-oxidant properties, it mediates cell survival and proliferation by activating the extracellular signal-regulated kinase (ERK1/2) pathway and attenuates cell death signaling by inhibiting apoptosis signal-regulating kinase 1 (ASK1) activation. [review]
the present study highlighted the involvement of DJ1 in HGrelated EC injury and identified that DJ1 exerts a cellular protective effect in HUVECs exposed to HG induced oxidative stress via activation of the PI3K/AkteNOS signaling pathway.
These findings suggest that oxidation-induced ubiquitination and degradation can be a quality control mechanism of oxidized redox-sensitive proteins including Prxs and DJ-1.
study implies that DJ-1 may protect endothelial progenitor cells against Ang II-induced dysfunction by activating the PPARgamma/HO-1.
Studied serum levels of Parkinson's disease-associated protein 7 (DJ-1) and human epididymis protein 4 (HE4) in endometrial cancer (EC) patients and healthy controls. The median serum concentrations of DJ-1 and HE4 were found to be significantly higher in EC patients compared to controls.
Study shows the generation of oxDJ-1 in erythrocytes in early stage, unmedicated parkinson's disease (PD) patients and in non-human primates with PD symptoms. In addition, oxDJ-1 interacts with 20S proteasome in the erythrocytes of PD patients. The current findings suggest that oxidative stress is systemically present in PD patients and suggest that an early pathophysiological mechanism operates in PD.
Not only is protein deglycase DJ-1 (DJ-1) linked to familial Parkinson's disease (PD), but it is also associated with the pathogenic mechanisms of sporadic PD and other neurodegenerative disorders where oxidative stress is implicated [Review].
Studies indicate that protein deglycase DJ-1 (DJ-1) plays a critical role in cancer [Review]
The PARK7 gene was demonstrated to be located on porcine chromosome 6
The product of this gene belongs to the peptidase C56 family of proteins. It acts as a positive regulator of androgen receptor-dependent transcription. It may also function as a redox-sensitive chaperone, as a sensor for oxidative stress, and it apparently protects neurons against oxidative stress and cell death. Defects in this gene are the cause of autosomal recessive early-onset Parkinson disease 7. Two transcript variants encoding the same protein have been identified for this gene.
, parkinson disease protein 7 homolog
, protein DJ-1
, Parkinson disease 7
, RNA-binding protein regulatory subunit
, Parkinson disease (autosomal recessive, early onset) 7
, oncogene DJ1
, contraception-associated protein 1
, fertility protein SP22