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Relevant bibliographies by topics / DJ-1 Family Protein

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Journal articles

Academic literature on the topic 'DJ-1 Family Protein'

Author: Grafiati

Published: 6 September 2023

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Journal articles on the topic "DJ-1 Family Protein"

1

Lin, Rong-Rong, Qing-Qing Tao, and Zhi-Ying Wu. "Early-Onset Parkinson’s Disease and Brain Iron Accumulation Caused by a Novel Homozygous DJ-1 Mutation." Journal of Parkinson's Disease 12, no. 3 (2022): 813–19. http://dx.doi.org/10.3233/jpd-213033.

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DJ-1 mutations are rare causes of autosomal recessive early-onset Parkinson’s disease (AR-EOPD) and relatively rarely reported in the Chinese population. Here, we used the whole-exome sequencing and Sanger sequencing to investigate DJ-1 mutations in the Chinese population and confirmed the pathogenicity of the mutation using primary fibroblasts established from skin biopsies. We identified a novel homozygous mutation (c.390delA, p.D131Tfs*3) in DJ-1 in a consanguineous Chinese family. The proband in this family had parkinsonism at the age of 22. His brain MRI indicated brain iron accumulation

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2

Qin, Li-xia, Jie-qiong Tan, Hai-nan Zhang, et al. "BAG5 Interacts with DJ-1 and Inhibits the Neuroprotective Effects of DJ-1 to Combat Mitochondrial Oxidative Damage." Oxidative Medicine and Cellular Longevity 2017 (2017): 1–10. http://dx.doi.org/10.1155/2017/5094934.

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Loss-of-function mutations in gene encoding DJ-1 contribute to the pathogenesis of autosomal recessive early-onset familial forms of Parkinson’s disease (PD). DJ-1 is a multifunctional protein and plays a protective role against oxidative stress-induced mitochondrial damage and cell death, but the exact mechanism underlying this is not yet clearly understood. Here, using coimmunoprecipitation (Co-IP) and immunofluorescence methods, we prove that Bcl-2-associated athanogene 5 (BAG5), a BAG family member, interacts with DJ-1 in mammalian cells. Moreover, we show that BAG5 could decrease stabilit

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3

Lewandowska, Aleksandra, Trung Nghia Vo, Thuy-Dung Ho Nguyen, et al. "Bifunctional Chloroplastic DJ-1B from Arabidopsis thaliana is an Oxidation-Robust Holdase and a Glyoxalase Sensitive to H2O2." Antioxidants 8, no. 1 (2019): 8. http://dx.doi.org/10.3390/antiox8010008.

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Members of the DJ-1 protein family are multifunctional enzymes whose loss increases the susceptibility of the cell to oxidative stress. However, little is known about the function of the plant DJ-1 homologs. Therefore, we analyzed the effect of oxidation on the structure and function of chloroplastic AtDJ-1B and studied the phenotype of T-DNA lines lacking the protein. In vitro oxidation of AtDJ-1B with H2O2 lowers its glyoxalase activity, but has no effect on its holdase chaperone function. Remarkably, upon oxidation, the thermostability of AtDJ-1B increases with no significant alteration of

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4

Kolisek, Martin, Augusto C. Montezano, Gerhard Sponder, et al. "PARK7/DJ-1 dysregulation by oxidative stress leads to magnesium deficiency: implications in degenerative and chronic diseases." Clinical Science 129, no. 12 (2015): 1143–50. http://dx.doi.org/10.1042/cs20150355.

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Disturbed magnesium (Mg2+) homoeostasis and increased levels of OS (oxidative stress) are associated with poor clinical outcomes in patients suffering from neurodegenerative, cardiovascular and metabolic diseases. Data from clinical and animal studies suggest that MD (Mg2+ deficiency) is correlated with increased production of ROS (reactive oxygen species) in cells, but a straightforward causal relationship (including molecular mechanisms) between the two conditions is lacking. The multifactorial protein PARK7/DJ-1 is a major antioxidant protein, playing a key role in cellular redox homoeostas

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5

Melvin, Prasad, Kondalarao Bankapalli, Patrick D’Silva, and P. V. Shivaprasad. "Methylglyoxal detoxification by a DJ-1 family protein provides dual abiotic and biotic stress tolerance in transgenic plants." Plant Molecular Biology 94, no. 4-5 (2017): 381–97. http://dx.doi.org/10.1007/s11103-017-0613-9.

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6

Ross, O. A., and M. J. Farrer. "Pathophysiology, pleotrophy and paradigm shifts: genetic lessons from Parkinson's disease." Biochemical Society Transactions 33, no. 4 (2005): 586–90. http://dx.doi.org/10.1042/bst0330586.

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PD (Parkinson's disease) is an aetiologically heterogeneous disorder characterized by a clinical phenotype consisting of resting tremor, rigidity and bradykinesia. Motor symptoms are associated with a progressive loss of dopaminergic neurons, with Lewy body inclusions within surviving neurons. Although heritability studies have shown evidence of familial aggregation, twin studies have provided limited support for a genetic aetiology. Nevertheless, classical linkage methods have nominated 11 regions of the genome and pathogenic mutations have been identified in several genes, including α-synucl

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7

Bankapalli, Kondalarao, SreeDivya Saladi, Sahezeel S. Awadia, Arvind Vittal Goswami, Madhuja Samaddar, and Patrick D'Silva. "Robust Glyoxalase activity of Hsp31, a ThiJ/DJ-1/PfpI Family Member Protein, Is Critical for Oxidative Stress Resistance inSaccharomyces cerevisiae." Journal of Biological Chemistry 290, no. 44 (2015): 26491–507. http://dx.doi.org/10.1074/jbc.m115.673624.

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8

Yang, Xinglong, and Yanming Xu. "Mutations in theATP13A2Gene and Parkinsonism: A Preliminary Review." BioMed Research International 2014 (2014): 1–9. http://dx.doi.org/10.1155/2014/371256.

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Parkinson’s disease (PD) is a major neurodegenerative disorder for which the etiology and pathogenesis remain as elusive as for Alzheimer's disease. PD appears to be caused by genetic and environmental factors, and pedigree and cohort studies have identified numerous susceptibility genes and loci related to PD. Autosomal recessive mutations in the genesParkin, Pink1, DJ-1, ATP13A2, PLA2G6, andFBXO7have been linked to PD susceptibility. Such mutations inATP13A2, also namedPARK9, were first identified in 2006 in a Chilean family and are associated with a juvenile-onset, levodopa-responsive type

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9

Liu, Tsai-Wei, Chiung-Mei Chen, and Kuo-Hsuan Chang. "Biomarker of Neuroinflammation in Parkinson’s Disease." International Journal of Molecular Sciences 23, no. 8 (2022): 4148. http://dx.doi.org/10.3390/ijms23084148.

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Parkinson’s disease (PD) is caused by abnormal accumulation of α-synuclein in dopaminergic neurons of the substantia nigra, which subsequently causes motor symptoms. Neuroinflammation plays a vital role in the pathogenesis of neurodegeneration in PD. This neuroinflammatory neurodegeneration involves the activation of microglia, upregulation of proinflammatory factors, and gut microbiota. In this review, we summarized the recent findings on detection of PD by using inflammatory biomarkers, such as interleukin (IL)-1β, IL-2, IL-6, IL-10, tumor necrosis factor (TNF)-α; regulated upon activation,

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10

Ohnishi, Y., and S. Horinouchi. "The A-factor regulatory cascade that leads to morphological development and secondary metabolism in Streptomyces." Biofilms 1, no. 4 (2004): 319–28. http://dx.doi.org/10.1017/s1479050504001462.

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A-factor (2-isocapryloyl-3R-hydroxymethyl-γ-butyrolactone) is a chemical signalling molecule, or microbial hormone, that triggers aerial mycelium formation and secondary metabolism in Streptomyces griseus. A-factor pro- duced in a growth-dependent manner switches on the transcription of adpA, encoding a transcriptional activator, by binding to ArpA, the A-factor receptor protein, which has bound to the adpA promoter, and dissociating the bound ArpA from the DNA. AdpA then activates a number of genes of various functions required for morphological development and secondary metabolism, forming a

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