Cell Stress Induced by the Parkinsonian Mimetic, 6-Hydroxydopamine, is Concurrent with Oxidation of the Chaperone, ERp57, and Aggresome Formation

Kim-Han, Jeong Sook; O’Malley, Karen L.

doi:10.1089/ars.2007.1791

Cited by 39 publications

(23 citation statements)

References 47 publications

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“…28 We evaluated the redox state of ERp57 in A2780 and A2780TC1 cells by alkylation of free thiols with NEM and analysis on SDS-PAGE under nonreducing conditions. 29 Interestingly, although ERp57 was primarily reduced as already described, 30 we detected the presence of the oxidized ERp57 form ( Figure 5D), thus, indicating a DNA binding activity of ERp57 and confirming a role of ERp57 in the nucleus in the cell lines tested.…”

Section: Erp57 Associates With Tubb3 In Both Nuclei and Cytoplasmsupporting

confidence: 80%

Comparative Proteomic Analysis of Paclitaxel Sensitive A2780 Epithelial Ovarian Cancer Cell Line and Its Resistant Counterpart A2780TC1 by 2D-DIGE: The Role of ERp57

Cicchillitti

Urbani

et al. 2009

J. Proteome Res.

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Epithelial ovarian cancer is the leading cause of gynecological cancer mortality. Despite good response to surgery and initial chemotherapy, chemoresistance occurrence represents a major obstacle to a successful therapy. To better understand biological mechanisms at the basis of paclitaxel resistance, a comparative proteomic approach based on DIGE coupled with mass spectrometry (MALDI-TOF and LC-MS/MS) was applied to the human epithelial ovarian cancer cell lines A2780 and its paclitaxel resistant counterpart A2780TC1. Most of the differentially expressed proteins between the two cell lines belong to the class of stress response (29%), metabolism (21%), and cell cycle and apoptosis (17%). We focused on proteins which were most strongly modulated by paclitaxel resistance and in particular on the disulphide isomerase ERp57, which may represent a chemoresistance biomarker. ERp57 was found to interact with class III beta-tubulin (TUBB3), involved in paclitaxel resistance in ovarian and other cancers. Moreover, we demonstrated a novel localization of this protein in cytoskeleton and described that ERp57/TUBB3 interaction occurs also in the nuclear compartment and in association with a multimeric complex formed by nucleolin, nucleophosmin, hnRNPK, and mortalin. Our data suggest that ERp57 plays an important role in chemoresistance mechanisms in ovarian cancer by modulating the attachment of microtubules to chromosomes following paclitaxel treatment through its interaction with TUBB3.

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Section: Erp57 Associates With Tubb3 In Both Nuclei and Cytoplasmsupporting

confidence: 80%

Comparative Proteomic Analysis of Paclitaxel Sensitive A2780 Epithelial Ovarian Cancer Cell Line and Its Resistant Counterpart A2780TC1 by 2D-DIGE: The Role of ERp57

Cicchillitti

Urbani

et al. 2009

J. Proteome Res.

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“…Thus, in endothelial cells under hyperoxic conditions, suppression of ERp57 actually opposes apoptotic events [87]. The ER stress induced by dopamine or by 6-hydroxydopamine (6-OHDA) on neurological tissues or cells has been related to Parkinson's disease [88,89]. As expected, in these conditions ERp57 is usually overexpressed [88,90], although not necessarily able to counteract the damaging effects of the stress.…”

Section: Erp57 As a Stress-response Proteinmentioning

confidence: 91%

“…As expected, in these conditions ERp57 is usually overexpressed [88,90], although not necessarily able to counteract the damaging effects of the stress. In particular, it has been observed that in murine mesencephalic dopaminergic cells (MN9D), treated with 6-OHDA, ERp57 becomes oxidized and self-aggregated, leading to the formation of aggresomes [89], which might be at least in part responsible for the cellular damage found in Parkinson's disease.…”

Section: Erp57 As a Stress-response Proteinmentioning

confidence: 99%

ERp57/GRP58: A protein with multiple functions

Turano

Gaucci

Grillo

et al. 2011

Cellular and Molecular Biology Letters

114

108

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Abbreviations used: 1α,25-(OH) 2 D 3 -1α,25-dihydroxycholecalciferol and calcitriol; APE/Ref-1 -apurinic (apyrimidinic) endonuclease/redox-factor 1; CRP -C-reactive protein; ER -endoplasmic reticulum; ERAD endoplasmic reticulum associated protein degradation; mTORC -mammalian target of rapamycin complex; PDI -protein disulfide isomerase; PKC -protein kinases C; PLA 2 -phospholipases A 2 ; Plc -peptide loading complex; PLC -phospholipase C; PrP SC -scrapie prion protein (misfolded prions); STAT -signal transducer and activator of transcription; STAT3 -signal transducer and activator of transcription 3; SV40 virus -simian virus 40; VDR -vitamin D receptor Review ERp57/GRP58: A PROTEIN WITH MULTIPLE FUNCTIONSCARLO TURANO*, ELISA GAUCCI, CATERINA GRILLO and SILVIA CHICHIARELLI Istituto Pasteur-Fondazione Cenci Bolognetti, Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Sapienza -Università di Roma, Italy Abstract: The protein ERp57/GRP58 is a stress-responsive protein and a component of the protein disulfide isomerase family. Its functions in the endoplasmic reticulum are well known, concerning mainly the proper folding and quality control of glycoproteins, and participation in the assembly of the major histocompatibility complex class 1. However, ERp57 is present in many other subcellular locations, where it is involved in a variety of functions, primarily suggested by its participation in complexes with other proteins and even with DNA. While in some instances these roles need to be confirmed by further studies, a great number of observations support the participation of ERp57 in signal transduction from the cell surface, in regulatory processes taking place in the nucleus, and in multimeric protein complexes involved in DNA repair.

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“…In particularly, this protein was down-regulated in fish exposed to VRP at environmental related concentrations, which indicated that the hepatic PDIA3 plays a role in an early adaptive response in VRP-induced ER stress. Moreover, the observed dose-dependent alterations of PDIA3 expression suggest that PDIA3 may have a protective function in the cellular stress response to VRP, in addition to its isomerase activities (33,34). According to other reports, the PDI and GRP78 are induced by ER stress caused by interference with Ca 2ϩ homeostasis, inhibition of disulfide bond formation of protein glycosylation, and oxidative stress to rescue the accumulation of misfolded or unfolded proteins with the ER (35).…”

Section: Discussionmentioning

confidence: 83%

Hepatic Proteome Sensitivity in Rainbow Trout after Chronically Exposed to a Human Pharmaceutical Verapamil

Šulc

et al. 2012

Molecular & Cellular Proteomics

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Verapamil (VRP), a cardiovascular pharmaceutical widely distributed and persistent in the aquatic environment, has potential toxicity to fish and other aquatic organisms. However, the molecular mechanisms that lead to these toxic effects are not well known. In the present study, proteomic analysis has been performed to investigate the protein patterns that are differentially expressed in liver of rainbow trout exposed to sublethal concentrations of VRP (0.5, 27.0, and 270 g/liter) for 42 days. Two-dimensional electrophoresis coupled with MALDI-TOF/TOF mass spectrometry was employed to detect and identify the protein profiles. The analysis revealed that the expression of six hepatic acidic proteins were markedly altered in the treatment groups compared with the control group; three proteins especially were significantly down-regulated in fish exposed to VRP at environmental related concentration (0.5 g/liter). These results suggested that the VRP induce mechanisms against oxidative stress (glucoseregulated protein 78 and 94 and protein disulfide-isomerase A3) and adaptive changes in ion transference regulation (calreticulin, hyperosmotic glycine-rich protein).

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Cell Stress Induced by the Parkinsonian Mimetic, 6-Hydroxydopamine, is Concurrent with Oxidation of the Chaperone, ERp57, and Aggresome Formation

Abstract: "Cell stress induced by the parkinsonian mimetic, 6-hydroxydopamine, is concurrent with oxidation of the chaperone, ERp57, and aggresome formation." Antioxidants & Redox Signaling.9,12. 2255-2264. 2255

Cited by 39 publications

References 47 publications

Comparative Proteomic Analysis of Paclitaxel Sensitive A2780 Epithelial Ovarian Cancer Cell Line and Its Resistant Counterpart A2780TC1 by 2D-DIGE: The Role of ERp57

Comparative Proteomic Analysis of Paclitaxel Sensitive A2780 Epithelial Ovarian Cancer Cell Line and Its Resistant Counterpart A2780TC1 by 2D-DIGE: The Role of ERp57

ERp57/GRP58: A protein with multiple functions

Hepatic Proteome Sensitivity in Rainbow Trout after Chronically Exposed to a Human Pharmaceutical Verapamil

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