Dysfunction of methionine sulfoxide reductases to repair damaged proteins by nickel nanoparticles. (5th July 2015)

• Record Type: Journal Article
• Authors: Feng, Po-Hao; Huang, Ya-Li; Chuang, Kai-Jen; Chen, Kuan-Yuan; Lee, Kang-Yun; Ho, Shu-Chuan; Bien, Mauo-Ying; Yang, You-Lan; Chuang, Hsiao-Chi
• Is Part Of: Chemico-biological interactions. Volume 236(2015)
• Page Start: 82
• Page End: 89
• Publication Date: 2015-07-05
• Subjects: Bcl-2 B-cell lymphoma 2 -- BPDE benzo(a)pyrene diolepoxide -- C-NiNPs carbon-coated nickel nanoparticles -- EDX energy-dispersive X-ray -- p-ERK1/2 extracellular signal-regulated kinase phosphorylation -- ERK extracellular signal-regulated kinase -- FE-SEM field emission-scanning electron microscope -- MSRA methionine sulfoxide reductases A -- MSRB methionine sulfoxide reductases B -- MetO methionine sulfoxide -- LC3 microtubule-associated protein 1A/1B-light chain 3 -- NiNPs nickel nanoparticles -- RNS reactive nitrogen species -- ROS reactive oxygen species -- SRB sulphorhodamine B; Autophagy -- Benzo(a)pyrene diolepoxide protein adduct -- Extracellular signal-regulated kinase -- Methionine oxidation -- Methionine sulfoxide reductases -- Nickel nanoparticle; Biochemistry -- Periodicals; Toxicological chemistry -- Periodicals; Biochemistry -- Periodicals; Biologie moléculaire -- Périodiques; Biochimie -- Périodiques; Toxicologie biochimique -- Périodiques; 572
• DOI: 10.1016/j.cbi.2015.05.003
• Languages: English
• ISSNs: 0009-2797

Abstract

Highlights: Cell death and BPDE protein adduct was occurred by NiNPs. MSR protein repairing system was dysfunction by NiNPs. LC3 down-regulation was occurred by NiNPs. p-ERK was produced by NiNPs and C-NiNPs. MSRA and MSRB were correlated with LC3. 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.