摘要

Background: Protein oxidation is considered to be one of the main causes of cell death, and methionine is one of the primary targets of reactive oxygen species (ROS). However, the mechanisms by which nickel nanoparticles (NiNPs) cause oxidative damage to proteins remain unclear. Objectives: The objective of this study is to investigate the effects of NiNPs on the methionine sulfoxide reductases (MSR) protein repairing system. Methods: Two physically similar nickel-based nanoparticles, NiNPs and carbon-coated NiNP (C-NiNPs; control particles), were exposed to human epithelial A549 cells. Cell viability, benzo(a)pyrene diolepoxide (BPDE) protein adducts, methionine oxidation, MSRA and B3, microtubule-associated protein 1A/1B-light chain 3 (LC3) and extracellular signal-regulated kinase (ERK) phosphorylation were investigated. Results: Exposure to NiNPs led to a dose-dependent reduction in cell viability and increased BPDE protein adduct production and methionine oxidation. The methionine repairing enzymatic MSRA and MSRB3 production were suppressed in response to NiNP exposure, suggesting the oxidation of methionine to MetO by NiNP was not reversed back to methionine. Additionally, LC3, an autophagy marker, was down-regulated by NiNPs. Both NiNP and C-NiNP caused ERK phosphorylation. LC3 was positively correlated with MSRA (r = 0.929, p <0.05) and MSRB3 (r = 0.893, p <0.05). Conclusions: MSR was made aberrant by NiNP, which could lead to the dysfunction of autophagy and ERK phosphorylation. The toxicological consequences may be dependent on the chemical characteristics of the nanoparticles.
原文英語
頁(從 - 到)82-89
頁數8
期刊Chemico-Biological Interactions
236
DOIs
出版狀態已發佈 - 五月 16 2015

指紋

Methionine Sulfoxide Reductases
Nickel
Nanoparticles
Repair
Methionine
Proteins
Phosphorylation
Oxidation
Benzo(a)pyrene
Extracellular Signal-Regulated MAP Kinases
Autophagy
Light
Cell Survival
Mitogen-Activated Protein Kinase 6
Cells
Microtubule-Associated Proteins

ASJC Scopus subject areas

  • Toxicology
  • Medicine(all)

引用此文

@article{3ea4e59ca72d42e7a5399dd7ec600fa0,
title = "Dysfunction of methionine sulfoxide reductases to repair damaged proteins by nickel nanoparticles",
abstract = "Background: Protein oxidation is considered to be one of the main causes of cell death, and methionine is one of the primary targets of reactive oxygen species (ROS). However, the mechanisms by which nickel nanoparticles (NiNPs) cause oxidative damage to proteins remain unclear. Objectives: The objective of this study is to investigate the effects of NiNPs on the methionine sulfoxide reductases (MSR) protein repairing system. Methods: Two physically similar nickel-based nanoparticles, NiNPs and carbon-coated NiNP (C-NiNPs; control particles), were exposed to human epithelial A549 cells. Cell viability, benzo(a)pyrene diolepoxide (BPDE) protein adducts, methionine oxidation, MSRA and B3, microtubule-associated protein 1A/1B-light chain 3 (LC3) and extracellular signal-regulated kinase (ERK) phosphorylation were investigated. Results: Exposure to NiNPs led to a dose-dependent reduction in cell viability and increased BPDE protein adduct production and methionine oxidation. The methionine repairing enzymatic MSRA and MSRB3 production were suppressed in response to NiNP exposure, suggesting the oxidation of methionine to MetO by NiNP was not reversed back to methionine. Additionally, LC3, an autophagy marker, was down-regulated by NiNPs. Both NiNP and C-NiNP caused ERK phosphorylation. LC3 was positively correlated with MSRA (r = 0.929, p <0.05) and MSRB3 (r = 0.893, p <0.05). Conclusions: MSR was made aberrant by NiNP, which could lead to the dysfunction of autophagy and ERK phosphorylation. The toxicological consequences may be dependent on the chemical characteristics of the nanoparticles.",
keywords = "Autophagy, Benzo(a)pyrene diolepoxide protein adduct, Extracellular signal-regulated kinase, Methionine oxidation, Methionine sulfoxide reductases, Nickel nanoparticle",
author = "Feng, {Po Hao} and Huang, {Ya Li} and Chuang, {Kai Jen} and Chen, {Kuan Yuan} and Lee, {Kang Yun} and Ho, {Shu Chuan} and Bien, {Mauo Ying} and Yang, {You Lan} and Chuang, {Hsiao Chi}",
year = "2015",
month = "5",
day = "16",
doi = "10.1016/j.cbi.2015.05.003",
language = "English",
volume = "236",
pages = "82--89",
journal = "Chemico-Biological Interactions",
issn = "0009-2797",
publisher = "Elsevier Ireland Ltd",

}

TY - JOUR

T1 - Dysfunction of methionine sulfoxide reductases to repair damaged proteins by nickel nanoparticles

AU - Feng, Po Hao

AU - Huang, Ya Li

AU - Chuang, Kai Jen

AU - Chen, Kuan Yuan

AU - Lee, Kang Yun

AU - Ho, Shu Chuan

AU - Bien, Mauo Ying

AU - Yang, You Lan

AU - Chuang, Hsiao Chi

PY - 2015/5/16

Y1 - 2015/5/16

N2 - Background: Protein oxidation is considered to be one of the main causes of cell death, and methionine is one of the primary targets of reactive oxygen species (ROS). However, the mechanisms by which nickel nanoparticles (NiNPs) cause oxidative damage to proteins remain unclear. Objectives: The objective of this study is to investigate the effects of NiNPs on the methionine sulfoxide reductases (MSR) protein repairing system. Methods: Two physically similar nickel-based nanoparticles, NiNPs and carbon-coated NiNP (C-NiNPs; control particles), were exposed to human epithelial A549 cells. Cell viability, benzo(a)pyrene diolepoxide (BPDE) protein adducts, methionine oxidation, MSRA and B3, microtubule-associated protein 1A/1B-light chain 3 (LC3) and extracellular signal-regulated kinase (ERK) phosphorylation were investigated. Results: Exposure to NiNPs led to a dose-dependent reduction in cell viability and increased BPDE protein adduct production and methionine oxidation. The methionine repairing enzymatic MSRA and MSRB3 production were suppressed in response to NiNP exposure, suggesting the oxidation of methionine to MetO by NiNP was not reversed back to methionine. Additionally, LC3, an autophagy marker, was down-regulated by NiNPs. Both NiNP and C-NiNP caused ERK phosphorylation. LC3 was positively correlated with MSRA (r = 0.929, p <0.05) and MSRB3 (r = 0.893, p <0.05). Conclusions: MSR was made aberrant by NiNP, which could lead to the dysfunction of autophagy and ERK phosphorylation. The toxicological consequences may be dependent on the chemical characteristics of the nanoparticles.

AB - Background: Protein oxidation is considered to be one of the main causes of cell death, and methionine is one of the primary targets of reactive oxygen species (ROS). However, the mechanisms by which nickel nanoparticles (NiNPs) cause oxidative damage to proteins remain unclear. Objectives: The objective of this study is to investigate the effects of NiNPs on the methionine sulfoxide reductases (MSR) protein repairing system. Methods: Two physically similar nickel-based nanoparticles, NiNPs and carbon-coated NiNP (C-NiNPs; control particles), were exposed to human epithelial A549 cells. Cell viability, benzo(a)pyrene diolepoxide (BPDE) protein adducts, methionine oxidation, MSRA and B3, microtubule-associated protein 1A/1B-light chain 3 (LC3) and extracellular signal-regulated kinase (ERK) phosphorylation were investigated. Results: Exposure to NiNPs led to a dose-dependent reduction in cell viability and increased BPDE protein adduct production and methionine oxidation. The methionine repairing enzymatic MSRA and MSRB3 production were suppressed in response to NiNP exposure, suggesting the oxidation of methionine to MetO by NiNP was not reversed back to methionine. Additionally, LC3, an autophagy marker, was down-regulated by NiNPs. Both NiNP and C-NiNP caused ERK phosphorylation. LC3 was positively correlated with MSRA (r = 0.929, p <0.05) and MSRB3 (r = 0.893, p <0.05). Conclusions: MSR was made aberrant by NiNP, which could lead to the dysfunction of autophagy and ERK phosphorylation. The toxicological consequences may be dependent on the chemical characteristics of the nanoparticles.

KW - Autophagy

KW - Benzo(a)pyrene diolepoxide protein adduct

KW - Extracellular signal-regulated kinase

KW - Methionine oxidation

KW - Methionine sulfoxide reductases

KW - Nickel nanoparticle

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U2 - 10.1016/j.cbi.2015.05.003

DO - 10.1016/j.cbi.2015.05.003

M3 - Article

VL - 236

SP - 82

EP - 89

JO - Chemico-Biological Interactions

JF - Chemico-Biological Interactions

SN - 0009-2797

ER -