Arianna Romani, Carlo Cervellati, Ximena M. Muresan, Giuseppe Belmonte, Alessandra Pecorelli, Franco Cervellati, Mascia Benedusi, Pablo Evelson, G. Valacchi (2017). Keratinocytes oxidative damage mechanisms related to airbone particle matter exposure. Mechanisms of Ageing and Development.
Department of Life Sciences and Biotechnology, University of Ferrara, Ferrara, Italy
Department of Biomedical and Specialist Surgical Sciences, University of Ferrara, Ferrara Italy
Universidad de Buenos Aires, CONICET, Instituto de Bioquímica Medicina Molecular (IBIMOL), Facultad de Farmacia y Bioquímica, Buenos Aires, Argentina
Department of Animal Science, North Carolina State University, Plants for Human Health Institute, NC Research Center, 28081, Kannapolis NC, USA
Epidemiological evidences have correlated airbone particulate matter (PM) to adverse health effects, mainly linking to pulmonary and cardiovascular disease. Nevertheless, only recently, some studies reported detrimental effects of PM on other organs such as skin. In a recent work, we have reported increased oxidative and inflammatory responses in Reconstituted Human Epidermis (RHE) exposed to ambient particles (CAPs) and we also demonstrated the ability of CAPs to penetrate the skin tissue.
The present study was aimed to better understand the cellular mechanisms beyond the oxidative changes induced by CAPs (5–10–25 μg/mL) in human immortalized keratinocytes (HaCaT).
After 24 h of treatment, CAPs were able to enter the cells leading to a decrease in viability, increased levels of 4-hydroxinonenal products (4-HNE) and IL-1α release. Overall these data, suggest lipid and protein oxidative damage, as well as an increase of inflammatory response after being challenged with CAPs. In addition, 3 h after CAPs exposure we found a significant increase in NF-kB and Nrf2 translocation into the nucleus. In contrast, no differences in gene expression and enzymatic activity of Nrf2 target genes were detected. This last finding could be explained by the ability of CAPs to possibly alter the binding of Nrf2 to the ARE DNA sequence.