Mouse Protein DJ-1(PARK7) ELISA kit

Multifunctional protein with controversial molecular function which plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor and redox-sensitive chaperone and protease. It is involved in neuroprotective mechanisms like the stabilization of NFE2L2 and PINK1 proteins, male fertility as a positive regulator of androgen signaling pathway as well as cell growth and transformation through, for instance, the modulation of NF-kappa-B signaling pathway. Has been described as a protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. But this function is rebuted by other works. As a protein deglycase, repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage. Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Protects histones from adduction by methylglyoxal, controls the levels of methylglyoxal-derived argininine modifications on chromatin. Able to remove the glycations and restore histone 3, histone glycation disrupts both local and global chromatin architecture by altering histone-DNA interactions as well as histone acetylation and ubiquitination levels. Displays a very low glyoxalase activity that may reflect its deglycase activity. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. Required for correct mitochondrial morphology and function as well as for autophagy of dysfunctional mitochondria. Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking. Regulates astrocyte inflammatory responses, may modulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells. In pancreatic islets, involved in the maintenance of mitochondrial reactive oxygen species (ROS) levels and glucose homeostasis in an age- and diet dependent manner. Protects pancreatic beta cells from cell death induced by inflammatory and cytotoxic setting. Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Metal-binding protein able to bind copper as well as toxic mercury ions, enhances the cell protection mechanism against induced metal toxicity. In macrophages, interacts with the NADPH oxidase subunit NCF1 to direct NADPH oxidase-dependent ROS production, and protects against sepsis.

1. DJ-1 protein concentration was significantly increased during the clinical phase in cerebrospinal fluid of sporadic Creutzfeldt-Jakob disease patients. PMID: 27975168
2. 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. PMID: 30107296
3. 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. PMID: 30142366
4. 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. PMID: 29142196
5. Silencing the DJ-1 gene uncovers a link between mitochondria-associated Parkinson's disease and mitotic pressure. PMID: 29097687
6. Low DJ-1 expression impairs synaptic vesicle endocytosis and reavailability at nerve terminals. PMID: 29386384
7. DJ-1 deficiency causes defects in astrocyte-mediated repair of brain damage. PMID: 29105838
8. In cultured neurons and forebrain samples from Dj1(-/-) animals, there was chloride damage and a profound structural remodeling of the mitochondrial respiratory chain. PMID: 28408307
9. DJ-1 has a role in glutamate uptake into astrocytes by regulating flotillin-1 and caveolin-1 expression PMID: 27346864
10. Network analysis reveals DJ-1/LDLR as common host proteins modulating pathogenesis of neurotropic viruses. PMID: 27581498
11. 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. PMID: 28036277
12. 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 PMID: 27171370
13. Knockdown of DJ-1 attenuates Nurr1 activity. PMID: 26873851
14. 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 PMID: 28088625
15. DJ-1 activates autophagy to alleviate cardiac hypertrophy. PMID: 28941803
16. 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. PMID: 27825319
17. DJ-1 deficiency negatively regulates liver progenitor cells (LPC) proliferation by impairing the formation of LPC-associated fibrosis and inflammatory niches. PMID: 27277679
18. 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. PMID: 27611333
19. Our data strengthen previous findings regarding DJ-1 diverse pathways and indicate that DJ-1 is part of a concerted and complex cellular response to OS PMID: 27109140
20. Our data demonstrates that the activation of DJ-1 in response to myocardial I/R injury protects the heart by regulating the SUMOylation status of Drp1 and attenuating excessive mitochondrial fission. PMID: 27108530
21. DJ-1(-/-) astrocytes may provide decreased neuroprotection to surrounding neurons due to alterations in pro-inflammatory mediator expression PMID: 26691871
22. Loss of DJ-1 impairs antioxidant response by altered glutamine and serine metabolism. PMID: 26836693
23. To verify our finding, we provide evidence that the protein expression of Parkinson protein 7, including new protein synthesis, is sensitive to mTORC1 inhibition PMID: 26419955
24. this study identified the anti-oxidant protein DJ-1 as being capable of protecting pancreatic islet cells from cell death induced by an inflammatory and cytotoxic setting. PMID: 26422139
25. In skeletal muscle cells, DJ-1 contributes to undernutrition-induced atrophy via MAPKs/ubiquitin ligase pathway. PMID: 26408915
26. Deficiency of DJ-1 exerts a stimulatory effect on vascular smooth muscle cell migration. PMID: 25978603
27. DJ1 maintains cellular metabolic homeostasis via modulating ROS levels in murine skeletal muscles, revealing a role of DJ1 in maintaining efficient fuel utilization. PMID: 26077864
28. DJ-1 physically binds the 20S proteasome and inhibits its activity. following oxidative stress, DJ-1 is involved in the Nrf2-dependent oxidative stress response that leads to the upregulation of both the 20S proteasome and its regulator, NQO1. PMID: 25833141
29. The Park7 has a protective role against sepsis by controlling macrophage activation, NADPH oxidase activation and inflammation responses. PMID: 26021615
30. in addition to detailing the visual defects that occur as a result of the absence of DJ-1, our data is also relevant to AMD pathogenesis. PMID: 26215528
31. DJ-1 reinforces the PI3K/AKT survival pathway and inhibits autophagy, probably by a mechanism independent from mTOR. PMID: 26222260
32. High DJ-1 contributes to adipogenesis and obesity-induced inflammation. PMID: 24925581
33. the P158Delta point mutation may contribute to neurodegeneration by protein destabilization and hence loss of DJ-1 function. PMID: 23241025
34. DJ-1 appears to have a protective role against dopaminergic degeneration triggered by alpha-syn or 6-OHDA, reinforcing the possible therapeutic importance of this protein in Parkinson's disease. PMID: 25500798
35. results indicate that DJ1 regulates cell metabolism and proliferation through Pink1 PMID: 25670069
36. Thus, our results suggest that myricitrin alleviates MPP(+)-induced mitochondrial dysfunction and increases cell viability via DJ-1. PMID: 25623535
37. Data suggest that Parkinson's disease protein DJ-1 is a common physiological sensor involved in both nutrition-induced effects and neurodegenerative disease states. PMID: 24646099
38. results suggest that DJ-1 protein is involved in SDF-1-induced CD3+ T cell migration via the overexpression of the CXCR4 receptor and that DJ-1 might act as an inhibitory regulator in vascular remodeling such as neointima formation PMID: 24953490
39. DJ-1 protein regulates the expression of renal PRR through H2O2-mediated epigenetic modification. PMID: 25463323
40. Brains from DJ-1(-/-) mice showed an increase in mitochondrial Trx activity, GSH and GSSG levels and mitochondrial glutaredoxin (GRX) activity. PMID: 24936441
41. The purpose of this study was to investigate the effects of PARK7 in muscle growth and protein accretion in response to IGF1. PMID: 24637782
42. DJ-1/park7 protein may be implicated in the regulation of vascular contractility and blood pressure PMID: 24323315
43. DJ-1 knockout mice were more susceptible to cell death from in vivo ischemic reperfusion injury with larger myocardial infarct sizes and resistance to cardioprotection by ischemic preconditioning. PMID: 24577080
44. oxidative stress-mediated intracellular trafficking of DJ-1, mediated by dynamic DJ-1 dimeric/monomeric cycling, is implicated in Parkinson disease pathogenesis. PMID: 24912681
45. is thought to be an oxidative sensor that protects cells from oxidative insult. PMID: 24269020
46. These observations suggest the relevance of DJ-1 oxidation to homeostasis in multiple brain regions, including neuromelanin-containing neurons of the substantia nigra PMID: 24918637
47. Data show the transcriptional activation of the cholecystokinin gene by DJ-1 through interaction of DJ-1 with RREB1 and the effect of DJ-1 on the cholecystokinin level. PMID: 24348900
48. Results show DJ-1 protein associated with lipid rafts. This novel function of DJ-1 in lipid rafts, may contribute the pathogenesis of Parkinson's Disease. PMID: 23847046
49. the mortalin/DJ-1 complex guards against mitochondrial oxidative stress and is indispensable for the maintenance of hematopoietic stem cells PMID: 24243970
50. The Parkinson disease-related protein DJ-1 counteracts mitochondrial impairment induced by the tumour suppressor protein p53 by enhancing endoplasmic reticulum-mitochondria tethering. PMID: 23418303

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Cell membrane; Lipid-anchor. Cytoplasm. Membrane raft. Nucleus. Mitochondrion. Endoplasmic reticulum.

Peptidase C56 family

Expressed in erythroblasts and in mature red blood cells from peripheral blood (at protein level). In pancreas, expression is higher in islets than surrounding exocrine tissues.

KEGG: mmu:57320

STRING: 10090.ENSMUSP00000030805

UniGene: Mm.277349