Animal Cell Culture Laboratory was founded in 2001. That was one of the first core facilities of the new Laboratory Building B. The laboratory promotes cell culture researches of all departments and training for students of Faculty of Bioengineering and Bioinformatics. The head of the laboratory is Alexander Kuimov, PhD.
Our own scientific research is a part of scientific program of the Department of nucleoprotein chemistry and biochemistry. It is based on a study of tankyrase, a signaling protein of animals and human being which catalyzes poly(ADP-ribosyl)ation, a posttranslational modification of various proteins.
Cloning of tankyrase 2 out of human breast tumor
Soon after publication of the first article about discovery of tankyrase 1 [Smith S. et al, 1998, Science] several laboratories reported about cloning of tankyrase 2 cDNA. One of them was the Laboratory of Molecular Immunology (now the Department of Molecular Immunology) where A.Kuimov worked thanadays. The cloning was performed as a part of project on research of tumor antigens using a system of bacteria and phages. One of the products was tankyrase 2 [Kuimov et al., 2001, Genes Immun]. To go on studying the human cell culture facilities were necessary, but they were available in neither the Laboratory of Molecular Immunology nor the new Laboratory Building B as a whole. This is why the new core facility named Animal Cell Culture Laboratory was created with A.Kuimov as its head.
Tissue localization of tankyrase 2
In the beginning of history of the new laboratory its main scientific problem was the localization of tankyrase 2 in human tissues. For this purpose the isoenzyme-specific antibody was developed. The highest level of tankyrase 2 was found in the epithelium of renal tubules [Sidorova N. et al, 2006, Cell Tissue Res]. Besides the human epithelial kidney cells of 293 line was established as the best model to study a function of tankyrase 2.
Isolation and purification of tankyrase 2
The 293 cells were then used as a source for tankyrase 2 isolation and purification. The enzyme was found tightly bound to other proteins in a huge partly soluble complex [Sidorova et al., 2008, Biochem (Mosc)].
Discovery of the new enzymatic reaction
Activity of tankyrase 2 led to disassembly of the complex. A substrate for poly(ADP-ribosyl)ation there was mannose-binding lectin, a serum protein which interacts with the cellular keratin 1, the basic component of the complex purified out of kidney cells [Sidorova et al, 2011, Mol.Cel.Biochem.]. Tankyrase catalyzes its posttranslational modification, what inactivates the lectin, and its complex with keratin 1 divides into separate components.
Grants and projects
Collaborations with other institutions
Memory medal “Moscow State University 250 years”.
Training of students of Faculty of Bioengineering and Bioinformatics on cell culture techniques in the courses “Gene Engineering” and “Cytogenetics”. Tutorship.
Sidorova N.N., Kurchashova S.Y., Yarahmedov T.Y., Ziganshin R.H., Kuimov A.N. (2011) Poly(ADP-ribosyl)ation of mannose-binding lectin out of human kidney cells. Molecular and Cellular Biochemistry, 352 (1): 231-238.
Seredenin S.B., Antipova T.A., Voronin M.V., Kurchashova S.Y., Kuimov A.N. (2009) Interaction of Afobazole with sigma(1)-Receptors. Bulletin of Experimental Biology and Medicine, 148 (1): 42-44.
Sidorova N.N., Fadeev A.O., Kuimov A.N. (2008) Isolation and physicochemical properties of tankyrase of human embryonic kdney cells of line 293. Biochemistry-Moscow, 73 (3): 289-295.
Sidorova N.N., Zavalishina L., Kurchashova S., Korsakova N., Nazhimov V., Frank G., Kuimov A.N. (2006) Immunohistochemical detection of tankyrase 2 in human breast tumors and normal renal tissue. Cell and Tissue Research, 323 (1): 137-145.
Kuimov A.N., Kuprash D.V., Petrov V.N., Vdovichenko K.K., Scanlan M.J., Jongeneel C.V., Lagarkova M.A., Nedospasov S.A. (2001) Cloning and characterization of TNKL, a member of tankyrase gene family. Genes and Immunity, 2 (1): 52-55.