Publications by authors named "Maria Grechnikova"

Copper plays a fundamental role in aerobic metabolism, but its role is double-edged, given its toxicity. Our understanding of copper metabolism in parasites remains rudimentary, despite its significance in virulence. Here we discuss how parasitic protists control copper homeostasis and show the potential key players identified by our bioinformatic analysis.

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Acanthamoeba castellanii is a ubiquitously distributed amoeba that can be found in soil, dust, natural and tap water, air conditioners, hospitals, contact lenses and other environments. It is an amphizoic organism that can cause granulomatous amoebic encephalitis, an infrequent fatal disease of the central nervous system, and amoebic keratitis, a severe corneal infection that can lead to blindness. These diseases are extremely hard to treat; therefore, a more comprehensive understanding of this pathogen's metabolism is essential for revealing potential therapeutic targets.

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Although copper is an essential nutrient crucial for many biological processes, an excessive concentration can be toxic and lead to cell death. The metabolism of this two-faced metal must be strictly regulated at the cell level. In this study, we investigated copper homeostasis in two related unicellular organisms: nonpathogenic and the "brain-eating amoeba" .

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Copper is a trace metal that is necessary for all organisms but toxic when present in excess. Different mechanisms to avoid copper toxicity have been reported to date in pathogenic organisms such as Cryptococcus neoformans and Candida albicans. However, little if anything is known about pathogenic protozoans despite their importance in human and veterinary medicine.

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Naegleria fowleri is a single-cell organism living in warm freshwater that can become a deadly human pathogen known as a brain-eating amoeba. The condition caused by N. fowleri, primary amoebic meningoencephalitis, is usually a fatal infection of the brain with rapid and severe onset.

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Background: The aim of the present study was to examine the effect of aldehyde modification on antioxidant enzyme activity in diabetic patients.

Methods: The activity of commercially available antioxidant enzymes (catalase, glutathione peroxidase [GPx], and Cu,Zn-superoxide dismutase [SOD]) was determined in vitro prior to and after aldehyde modification. The activity of erythrocyte Cu,Zn-SOD was assayed in blood drawn from healthy donors, diabetic patients with decompensated carbohydrate metabolism, and diabetic patients after glucose-lowering therapy.

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