Immunocytochemical study of BCR and bcr-abl localization in K562 cells

• Veröffentlicht in: Experimental Oncology
• Datum: 2010
• Hauptverfasser: Telegeev, G.D., Dubrovska, A.N., Nadgorna, V.A., Dybkov, M.V., Zavelevich, M.P., Maliuta, S.S., Gluzman, D.F.
• Format: Artikel
• Sprache: English
• Veröffentlicht: Інститут експериментальної патології, онкології і радіобіології ім. Р.Є. Кавецького НАН України 2010
• Schlagworte: Original contributions
• Online Zugang: https://nasplib.isofts.kiev.ua/handle/123456789/138603
• Назва журналу: Digital Library of Periodicals of National Academy of Sciences of Ukraine
• Zitieren: Immunocytochemical study of BCR and bcr-abl localization in K562 cells / G.D. Telegeev, A.N. Dubrovska, V.A. Nadgorna, M.V. Dybkov, M.P. Zavelevich, S.S. Maliuta, D.F. Gluzman // Experimental Oncology. — 2010. — Т. 32, № 2. — С. 81-83. — Бібліогр.: 13 назв. — англ.

Aim: To obtain polyclonal antibodies against recombinant proteins recognizing Bcr domain and fusion region of Bcr-Abl and analyze the patterns of intracellular distribution of Bcr and Bcr-Abl proteins in K562 cells of chronic myelogenous leukemia. Methods: The coding sequences of DН and РН domains of Bcr-Abl were cloned, and the recombinant proteins were expressed in E. coli. The rabbit polyclonal antibodies were produced and used for immunocytochemical study of Bcr and Bcr-Abl localization in K562 cells. Results: The gene constructs containing sequences coding for DН and РН domains of Bcr-Abl have been obtained. The antibodies with relative specificity to corresponding recombinant proteins differ by the patterns of their intracellular reactivity with Bcr- and Bcr-Abl related structures. While Bcr protein is located predominantly perinuclearly, antibody against hybrid Bcr-Abl protein is reacted with the structures in cell periphery, namely on cell membranes. Conclusion: Antibodies against DН and РН domains of Bcr-Abl react with proteins located differently in chronic myelogenous leukemia cells. The difference in intracellular localization of Bcr and Bcr-Abl may be attributable to the different domains interacting with different multiprotein complexes.