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Stimulation of production of reactive oxygen and nitrogen species in endothelial cells by unmodified and F enton‐modified ultradisperse detonation diamond
Author(s) -
SolarskaŚciuk K.,
Gajewska A.,
Skolimowski J.,
Mitura K.,
Bartosz G.
Publication year - 2013
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1002/bab.1071
Subject(s) - glutathione , chemistry , reactive oxygen species , nuclear chemistry , glutathione peroxidase , glutathione reductase , biochemistry , antioxidant , enzyme
In recent years, the development of nanotechnology opens up new prospects for biomedical applications of unmodified and chemically modified diamond nanoparticles ( DNP s). The problem of biocompatibility of DNP s is thus of primary importance. The first step in the modification of DNP s is usually the introduction of ‒ OH groups, which can bind other functional groups. One of the basic methods to introduce ‒ OH groups onto DNP s is the Fenton reaction. The aim of this study was to compare the effect of unmodified DNP s and nanoparticles modified by the Fenton reaction on human endothelial cells. Ultradisperse diamond ( UDD ) was modified by the Fenton reaction introducing surface ‒ OH groups. Immortalized human umbilical cord endothelial cells ( HUVEC ‐ ST ) were incubated with 2–100 µg/mL nanopowders in the opti‐ MEM medium. For comparison, graphite powder ( GRAF and GRAF + OH ) was also employed. UDD and GRAF augmented generation of reactive oxygen species in the cells after 24 H incubation, estimated by oxidation of 2′,7′‐dichlorofluorescin diacetate (H2DCF‐DA). Cellular production of nitric oxide, estimated with DAF‐FM‐DA (3‐amino‐4‐aminomethyl 2′,7′‐dichlorofluorescein diacetate), was also affected by UDD and GRAF after 24 H. Fenton‐modified OH, in contrast to unmodified diamond, decreased NO production. Detonation nanoparticles also affected the cellular content of glutathione and activities of main antioxidant enzymes (superoxide dismutase, catalase, glutathione peroxidase, glutathione reductase, and glutathione S ‐transferase). This article was published online on 5 February 2013. Errors in the byline and affiliation line were subsequently identified. This notice is included in the online and print versions to indicate that both have been corrected 18 April 2013.

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