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Fusion proteins capable of selective binding to melanoma cells for investigation of the mechanisms of cell malignizationстатья Тезисы
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 27 марта 2014 г.
- Авторы: Syrkina M.S., Rubtsov M.A., Shirokov D.A., Veiko V.P.
- Журнал: FEBS Journal
- Том: 280
- Год издания: 2013
- Издательство: Blackwell Publishing Inc.
- Местоположение издательства: United Kingdom
- Первая страница: 324
- Последняя страница: 324
- Аннотация: Metastasis is multiple-stage process, which is characterized by a number of rounds of metastasing cell attachment/detachment to extracellular matrix. Different cell adhesion molecules such as cadherins and integrins take part in this process. More over the proper cooperation of different molecular structures is required. Integrin receptors are able to take part in the regulation of such cooperation because of its ability to bidirectional signal transduction and the mediation of cell adhesion, migration, proliferation, differentiation and apoptosis [1]. Observations showng that integrin overexpression correlates with the increase of the metastatic potential of melanoma cells [2] suggest the key role of integrins in melanoma cell malignization. It is known that integrins which are overexpressed in highly-metastatic melanoma cells are capable to high affinity binding to RGD tripeptide, which has been found in a wide variety of its natural ligands [3]. So RGD-bearing proteins having the ability to selective binding with melanoma cells represent the suitable tool for investigation of the mechanisms of melanoma cell malignization. In present work expression vectors bearing the genes of fusion proteins have been constructed for producing these proteins in E. coli. Such fusion proteins consist of a peptidic ‘address’, targeting the integrins on melanoma cells, linked to an ‘adaptor’ for the attachment of a visualizing agent. The peptidic ‘address’ contains the RGD motif, which is stabilized by a disulfide bond to achieve the optimal receptor binding conformation. The ‘adaptor’ is a tetrameric protein, namely, streptavidin, that is able to achieve high-affinity binding of d-biotin, which facilitates the generation of colored proteins using the appropriate biotin derivatives. Aforementioned proteins were purified from the periplasm of E.coli using columns with 2-iminobiotin agarose and demonstrated ability to selective adhesion to murine and human melanoma cells.
- Добавил в систему: Сыркина Марина Сергеевна