The Parkinsonism-associated protein DJ-1/Park7 prevents glycation damage in human keratinocyte

Advedissian, Tamara; Deshayes, Frédérique; Poirier, Françoise; Viguier, Mireille; Richarme, Gilbert

doi:10.1016/j.bbrc.2016.03.056

Cited by 29 publications

(19 citation statements)

References 26 publications

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“…The neuroprotective effects were accompanied by a decrease in astrogliosis, microgliosis, and release of pro-inflammatory cytokines [38]. Similar effects have been demonstrated in other animal models of PD [94][95][96].…”

Section: Pharmacologic Targeting Of Nrf2 As a Disease Modifiying Thersupporting

confidence: 72%

Role of the Transcription Factor Nrf2 in Parkinson’s Disease: New Insights

Lastres‐Becker¹

2017

J Alzheimers Dis Parkinsonism

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Section: Pharmacologic Targeting Of Nrf2 As a Disease Modifiying Thersupporting

confidence: 72%

Role of the Transcription Factor Nrf2 in Parkinson’s Disease: New Insights

Lastres‐Becker¹

2017

J Alzheimers Dis Parkinsonism

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“…Moreover, yajL mutants display translational defects (20,21) and induce a DNA damage response (22,23). Because DJ-1-depleted keratinocytes display increased protein glycation levels (24), both the protein and nucleic acid deglycase activities of DJ-1 prevent cellular glycation.…”

mentioning

confidence: 99%

Guanine glycation repair by DJ-1/Park7 and its bacterial homologs

Richarme

Liu

Mihoub

et al. 2017

Science

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162

148

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DNA damage induced by reactive carbonyls (mainly methylglyoxal and glyoxal), called DNA glycation, is quantitatively as important as oxidative damage. DNA glycation is associated with increased mutation frequency, DNA strand breaks, and cytotoxicity. However, in contrast to guanine oxidation repair, how glycated DNA is repaired remains undetermined. Here, we found that the parkinsonism-associated protein DJ-1 and its bacterial homologs Hsp31, YhbO, and YajL could repair methylglyoxal- and glyoxal-glycated nucleotides and nucleic acids. DJ-1-depleted cells displayed increased levels of glycated DNA, DNA strand breaks, and phosphorylated p53. Deglycase-deficient bacterial mutants displayed increased levels of glycated DNA and RNA and exhibited strong mutator phenotypes. Thus, DJ-1 and its prokaryotic homologs constitute a major nucleotide repair system that we name guanine glycation repair.

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“…Moreover, DJ‐1 as a protein deglycase which involved in oxidative stress resistance repairs proteins from glycation by glyoxal and methylglyoxal (Advedissian et al . ). Reports suggested that DJ‐1‐mediated antioxidative defence is activated after chemotherapy in advanced‐stage ovarian cancer, which may indicate its role in chemoresistance (Pylvas‐Eerola et al .…”

Section: Discussionmentioning

confidence: 97%

Identification of DJ‐1 as a contributor to multidrug resistance in human small‐cell lung cancer using proteomic analysis

Gao

Niu

et al. 2017

Int J Experimental Path

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Proteomic approaches have been proven to provide an important tool in identifying drug resistance-associated proteins. The aim of this study was to investigate the protein profiling of drug resistance-related proteins in small-cell lung cancer (SCLC) by proteomic analysis. The proteomic profiling was performed by two-dimensional fluorescence difference gel electrophoresis (2D-DIGE) coupled with MALDI-TOF-TOF of SCLC in the multidrug-resistant cell line H69AR and its parental cell line H69. A total of 11 proteins were identified to be >2-fold up-or downregulated between the two cell lines. DJ-1, one of the differently expressed proteins identified by proteomics, was further examined by immunohistochemistry staining in 116 cases of SCLC tissues. Immunohistochemical results demonstrated that DJ-1 was expressed in 51.7% (60/116) of SCLC. DJ-1 expression was correlated significantly with survival time of SCLC patients (P < 0.05), but not with other clinical parameters such as gender, age and clinical stage (P > 0.05). Downregulation of DJ-1 using DJ-1-siRNA in H69AR cells sensitized cancer cells to chemotherapeutic drugs through increasing drug-induced cell apoptosis accompanied with G0-G1 phase arrest. These findings suggest DJ-1 may serve as a potential biomarker for chemoresistance and prognostic factor for patients with SCLC.

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The Parkinsonism-associated protein DJ-1/Park7 prevents glycation damage in human keratinocyte

Cited by 29 publications

References 26 publications

Role of the Transcription Factor Nrf2 in Parkinson’s Disease: New Insights

Role of the Transcription Factor Nrf2 in Parkinson’s Disease: New Insights

Guanine glycation repair by DJ-1/Park7 and its bacterial homologs

Identification of DJ‐1 as a contributor to multidrug resistance in human small‐cell lung cancer using proteomic analysis

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