Prospects for the use of indicators of sialic acid metabolism in medicine (review of literature)

Klin Lab Diagn. 2021 Jul 16;66(7):389-395. doi: 10.51620/0869-2084-2021-66-7-389-395.

Abstract

Sialic acids (SA) determine the degree of molecular hydrophilia, relieve binding together and their transportation, they increase mucin viscosity, stabilize the protein and membrane structure. Apart from that, SA are structural components of gangliosides participating in the formation of the outer layer of the plasma membrane. The degree of silyliation of glycoproteins and glycolipids is an important factor of molecular recognition in the cell, between the cells, between a cell and territorial matrix, as well as between a cell and some outer pathogenic factors. They can either mask the sites of recognition or be determinants of recognition. The most well-studied enzymes taking part in the SA metabolism and sialo-containing compounds are N-acetylneuraminate, cythydiltransferase, sialyltransferase, sialydase, aldolase SA and sialyl-O-acetylesterase. Numerous investigations have shown that aberrant sialylation is a specific feature of various changes and disorders of metabolism. Besides that, sialic acids are the first point of contact for different pathogenic microorganisms and the host's body due to their presence on the external surface of the cells and tissue of the mucous membrane. That is why the study of the above-mentioned various sialic acids fractions as well as of the activity of the enzymes participating in their metabolism in the blood plasma and tissues, and of the influence on the activity of these enzymes with the help of medicine can make an essential contribution to the diagnosis and treatment of many diseases.

Keywords: diagnostics; gangliosides; review; sialic acids; sialidase; sialidosis; sialoglycoproteins; sialyltransferase.

Publication types

  • Review

MeSH terms

  • Acetylesterase
  • Glycolipids
  • Neuraminidase*
  • Sialic Acids*

Substances

  • Glycolipids
  • Sialic Acids
  • Acetylesterase
  • Neuraminidase