Manose- and sialospecific lectines as markers of the inflammatory process

Most human proteins are modified by the covalent addition of complex oligosaccharides - glycans. The carbohydrate part of the protein affects their structure and function. Due to differences in the nature of changes in glycoforms of glycoproteins depending on the type and stage of a particular pathological process, there are new approaches to the differential diagnosis of diseases, which are based on their detection.The study of glycosylation processes and elucidation of the causes of their violation allows us to judge not only the morphology and degree of differentiation of immunocompetent cells, but also the level of their functional activity and ability to migrate, and therefore the immunological resistance of the organism as a whole severity. Lectins, proteins that specifically interact with certain carbohydrate sequences, recognizing not only their monomer composition but also their spatial configuration, are today an accessible and effective research tool. The aim of the study was to compare the number of lymphocytes in the blood that contain glycans on their surface in different diseases. The object of the study were blood lymphocytes of patients with chronic lymphocytic leukemia (CLL) (n = 10) and liver disease (n = 10). The control group consisted of 10 relatively healthy donors. The number of glycosylated blood cells was determined by flow cytofluorimetry using fluorescein isothiocyanate-conjugated (FITC) lectins of different specificity. Studies of terminal residues of N-acetylneuraminic acid were performed using lectins - Sambucus nigra (SNA), which is affine to α (2 → 6) - bonds of N-glycans, as mannose-174specific lectin used Canavalia ensiformis (ConA). The analysis was performed on a flow cytometer Soulter Epics XL. The calculation of changes in exposure density was performed in accordance with the program FCS Express 3. All subjects gave written consent to participate in the study