Biological and Pathological Roles of Ganglioside Sialidases

Progress in Molecular Biology and Translational Science
Taeko MiyagiKazunori Yamaguchi

Abstract

Sialidases are glycosidases responsible for the removal of α-glycosidically linked sialic acid residues from carbohydrate portions of glycoproteins and glycolipids, this process being the initial step in the degradation of such glycoconjugates. Sialic acids are considered to play important roles in various biological processes largely in two ways, one related to their hydrophilic and acidic properties exerting physicochemical effects on the glycoconjugates to which they are attached, and the other as recognition sites or in an opposing fashion as masking sites. The removal of sialic acids catalyzed by a sialidase, therefore greatly influences many biological processes through changing the conformation of glycoproteins and through recognition and masking of biological sites of functional molecules. Sialidases are found widely distributed in metazoan animals, from echinoderms to mammals, and are also present in viruses and other microorganisms, including fungi, protozoa, and bacteria even mostly lacking sialic acids. In mammals, there are four forms of sialidase (Neu1, Neu2, Neu3, and Neu4), differing in their major subcellular localization and enzymatic properties. They have been implicated in regulation of various cellular acti...Continue Reading

Citations

Apr 11, 2020·International Journal of Molecular Sciences·Bernadette Breiden, Konrad Sandhoff
Jul 31, 2020·International Journal of Molecular Sciences·Cara-Lynne Schengrund
May 15, 2019·Journal of the Chinese Medical Association : JCMA·Wen-Ling Lee, Peng-Hui Wang
Jan 31, 2020·Frontiers in Cellular and Infection Microbiology·Yan-Hua Wang
Feb 10, 2021·Scientific Reports·Akira MinamiTakashi Suzuki
Nov 24, 2018·Biochemical and Biophysical Research Communications·Flavia OrizioRoberto Bresciani
May 23, 2021·Biochimie·Matilde ForcellaEugenio Monti
Jul 21, 2020·The Biochemical Journal·Keiji OkadaKazuhiro Shiozaki

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