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Eur J Pharmacol. 2019 Jan 5;842:345-350. doi: 10.1016/j.ejphar.2018.11.014. Epub 2018 Nov 12.

Sialidase activity in human pathologies.

Author information

1
Department of Genetics, Cytology and Bioengineering, Faculty of Biology and Medicine, Voronezh State University, Voronezh, Russia.
2
Laboratory of Angiopathology, Institute of General Pathology and Pathophysiology, 125315 Moscow, Russia.
3
Federal Research and Clinical Center of Intensive Care Medicine and Rehabilitology, 109240 Moscow, Russia.
4
Laboratory of Angiopathology, Institute of General Pathology and Pathophysiology, 125315 Moscow, Russia; Institute for Atherosclerosis Research, Skolkovo Innovative Center, 121609 Moscow, Russia; Centre of Collective Use, Institute of Gene Biology, Russian Academy of Sciences, Moscow 121552, Russia. Electronic address: ano.inat@mail.ru.

Abstract

Sialic acid residues are frequently located at the terminal positions of glycoconjugate chains of cellular glycocalyx. Sialidases, or neuraminidases, catalyse removal of these residues thereby modulating various normal and pathological cellular activities. Recent studies have revealed the involvement of sialidases in a wide range of human disorders, including neurodegenerative disorders, cancers, infectious diseases and cardiovascular diseases. The accumulating data make sialidases an interesting potential therapeutic target. Modulating the activity of these enzymes may have beneficial effects in several pathologies. Four types of mammalian sialidases have been described: NEU1, NEU2, NEU3 and NEU4. They are encoded by different genes and characterized by different subcellular localization. In this review, we will summarize the current knowledge on the roles of different sialidases in pathological conditions.

KEYWORDS:

Cancer; Desialylation; Glycocalyx; Neuraminidase; Sialic acid; Sialidase

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