Рапопорт Евгения Марковна

Кандидат химических наук

Старший научный сотрудник (Лаборатория углеводов)

Тел.: +7 (495) 330-66-83

Эл. почта: eugenia_rapoport@mail.ru

Личная информация


Период обученияСтрана, городУчебное заведениеДополнительная информация
1982–1988 СССР, Москва МХТИ им. Д.И.Менделеева

Научные интересы

клеточные углеводсвязывающие белки

Премии и заслуги

Основные научные результаты

Исследованы 1)специфичность галектинов в составе клетки; 2) механизмы регуляции функциональной активности клеточных галектинов   

Членство в научных обществах

Гранты и проекты

ПериодДополнительная информация

Избранные публикации

  1. Vokhmyanina O.A., Rapoport E.M., André S., Severov V.V., Ryzhov I., Pazynina G.V., Korchagina E., Gabius H.J., Bovin N.V. (2012). Comparative study of the glycan specificities of cell-bound human tandem repeat-type galectins -4, -8 and -9. Glycobiology , [+]
  2. Vokhmyanina O.A., Rapoport E.M., Ryzhov I.M., Korchagina E.Y., Pazynina G.V., Severov V.V., Kaltner H., André S., Gabius H.J., Bovin N.V. (2011). Carbohydrate specificity of chicken and human tandem-repeat-type galectins-8 in composition of cells. Biochemistry Mosc. 76 (10), 1185–92 [+]
  3. Rapoport E.M., Pochechueva T.V., Kurmyshkina O.V., Pazynina G.V., Severov V.V., Gordeeva E.A., Belyanchikov I.M., André S., Gabius H.J., Bovin N.V. (2010). Solid-phase assays for study of carbohydrate specificity of galectins. Biochemistry Mosc. 75 (3), 310–9 [+]
  4. Kurmyshkina O., Rapoport E., Moiseeva E., Korchagina E., Ovchinnikova T., Pazynina G., Belyanchikov I., Bovin N. (2010). Glycoprobes as a tool for the study of lectins expressed on tumor cells. Acta Histochem. 112 (2), 118–26 [+]
  5. Rapoport E.M., André S., Kurmyshkina O.V., Pochechueva T.V., Severov V.V., Pazynina G.V., Gabius H.J., Bovin N.V. (2008). Galectin-loaded cells as a platform for the profiling of lectin specificity by fluorescent neoglycoconjugates: a case study on galectins-1 and -3 and the impact of assay setting. Glycobiology 18 (4), 315–24 [+]

    The involvement of galectins as pleiotropic regulators of cell adhesion and growth in disease progression explains the interest to define their ligand-binding properties. Toward this end, it is desirable to approach in vivo conditions to attain medical relevance. In order to simulate physiological conditions with cell surface glycans as recognition sites and galectins as mediators of intercellular contacts we developed an assay using galectin-loaded Raji cells. The extent of surface binding of fluorescent neoglycoconjugates depended on the lectin presence and the type of lectin, the nature of the probes' carbohydrate headgroup and the density of unsubstituted beta-galactosides on the cell surface. Using the most frequently studied galectins-1 and -3, application of this assay led to rather equal binding levels for linear and branched oligomers of N-acetyllactosamine. A clear preference of galectin-3 for alpha1-3-linked galactosylated lactosamine was noted. In parallel, a panel of 24 neoglycoconjugates was tested as inhibitors of galectin binding from solution to N-glycans of surface-immobilized asialofetuin. These two assays differ in presentation of the galectin and ligand, facilitating identification of assay-dependent properties. Under the condition of the cell assay, selectivity among oligosaccharides for the lectins was higher, and extraordinary affinity of galectin-1 to 3'-O-sulfated probes in a solid-phase assay was lost in the cell assay. Having introduced and validated a cell assay, the comprehensive profiling of ligand binding to cell-surface-presented galectins is made possible.

  6. Рапопорт Е.М., Некрасов М.В., Хайдуков С.В., Свирщевская Е.В., Жигис Л.С., Козлов Л.В., Баталова Т.Н., Зубов В.П., Бовин Н.В. (2000). Изучение клеточной локализации галактозосвязывающего лектина из сыворотки крови человека. Биохимия 65 (11), 1558–1563 ID:207