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Glanz VY, Myasoedova VA, Grechko AV, Orekhov AN.

2018 Nov 12;842:345-350. doi: 10.1016/j.ejphar.2018.11.014. [Epub ahead of print]



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.


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