46
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access
      research-article

      Read this article at

      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          The skin is the largest organ of the human body and the one mostly exposed to outdoor contaminants. To evaluate the biological mechanisms underlying skin damage caused by fine particulate matter (PM 2.5), we analyzed the effects of PM 2.5 on cultured human keratinocytes and the skin of experimental animals. PM 2.5 was applied to human HaCaT keratinocytes at 50 µg/mL for 24 h and to mouse skin at 100 µg/mL for 7 days. The results indicate that PM 2.5 induced oxidative stress by generating reactive oxygen species both in vitro and in vivo, which led to DNA damage, lipid peroxidation, and protein carbonylation. As a result, PM 2.5 induced endoplasmic reticulum stress, mitochondrial swelling, and autophagy, and caused apoptosis in HaCaT cells and mouse skin tissue. The PM 2.5-induced cell damage was attenuated by antioxidant N-acetyl cysteine, confirming that PM 2.5 cellular toxicity was due to oxidative stress. These findings contribute to understanding of the pathophysiological mechanisms triggered in the skin by PM 2.5, among which oxidative stress may play a major role.

          Related collections

          Most cited references54

          • Record: found
          • Abstract: found
          • Article: not found

          Endoplasmic reticulum stress: cell life and death decisions.

          C. Xu (2005)
          Disturbances in the normal functions of the ER lead to an evolutionarily conserved cell stress response, the unfolded protein response, which is aimed initially at compensating for damage but can eventually trigger cell death if ER dysfunction is severe or prolonged. The mechanisms by which ER stress leads to cell death remain enigmatic, with multiple potential participants described but little clarity about which specific death effectors dominate in particular cellular contexts. Important roles for ER-initiated cell death pathways have been recognized for several diseases, including hypoxia, ischemia/reperfusion injury, neurodegeneration, heart disease, and diabetes.
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Endoplasmic reticulum stress and oxidative stress in cell fate decision and human disease.

            The endoplasmic reticulum (ER) is a specialized organelle for the folding and trafficking of proteins, which is highly sensitive to changes in intracellular homeostasis and extracellular stimuli. Alterations in the protein-folding environment cause accumulation of misfolded proteins in the ER that profoundly affect a variety of cellular signaling processes, including reduction-oxidation (redox) homeostasis, energy production, inflammation, differentiation, and apoptosis. The unfolded protein response (UPR) is a collection of adaptive signaling pathways that evolved to resolve protein misfolding and restore an efficient protein-folding environment. Production of reactive oxygen species (ROS) has been linked to ER stress and the UPR. ROS play a critical role in many cellular processes and can be produced in the cytosol and several organelles, including the ER and mitochondria. Studies suggest that altered redox homeostasis in the ER is sufficient to cause ER stress, which could, in turn, induce the production of ROS in the ER and mitochondria. Although ER stress and oxidative stress coexist in many pathologic states, whether and how these stresses interact is unknown. It is also unclear how changes in the protein-folding environment in the ER cause oxidative stress. In addition, how ROS production and protein misfolding commit the cell to an apoptotic death and contribute to various degenerative diseases is unknown. A greater fundamental understanding of the mechanisms that preserve protein folding homeostasis and redox status will provide new information toward the development of novel therapeutics for many human diseases.
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Endoplasmic reticulum stress and the inflammatory basis of metabolic disease.

              The endoplasmic reticulum (ER) is the major site in the cell for protein folding and trafficking and is central to many cellular functions. Failure of the ER's adaptive capacity results in activation of the unfolded protein response (UPR), which intersects with many different inflammatory and stress signaling pathways. These pathways are also critical in chronic metabolic diseases such as obesity, insulin resistance, and type 2 diabetes. The ER and related signaling networks are emerging as a potential site for the intersection of inflammation and metabolic disease. 2010 Elsevier Inc. All rights reserved.
                Bookmark

                Author and article information

                Contributors
                jinwonh@jejunu.ac.kr
                Journal
                Arch Toxicol
                Arch. Toxicol
                Archives of Toxicology
                Springer Berlin Heidelberg (Berlin/Heidelberg )
                0340-5761
                1432-0738
                26 March 2018
                26 March 2018
                2018
                : 92
                : 6
                : 2077-2091
                Affiliations
                [1 ]ISNI 0000 0001 0725 5207, GRID grid.411277.6, Jeju National University School of Medicine and Jeju Research Center for Natural Medicine, ; Jeju, 63243 Republic of Korea
                [2 ]ISNI 0000 0001 0725 5207, GRID grid.411277.6, Laboratory of Veterinary Anatomy, College of Veterinary Medicine, , Jeju National University, ; Jeju, 63243 Republic of Korea
                [3 ]ISNI 0000 0001 0310 3978, GRID grid.412050.2, Department of Biochemistry, College of Oriental Medicine, , Dongeui University, ; Busan, 47340 Republic of Korea
                Article
                2197
                10.1007/s00204-018-2197-9
                6002468
                29582092
                21e46a40-4855-47c6-8791-af9c4d73e736
                © The Author(s) 2018

                Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License ( http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

                History
                : 9 November 2017
                : 21 March 2018
                Funding
                Funded by: National Research Foundation of Korea (KR)
                Award ID: NRF-2017R1A4A1014512
                Award Recipient :
                Categories
                In Vitro Systems
                Custom metadata
                © Springer-Verlag GmbH Germany, part of Springer Nature 2018

                Toxicology
                pm2.5,oxidative stress,apoptosis,endoplasmic reticulum stress,mitochondrial damage,autophagy

                Comments

                Comment on this article