Marina Kriajevskaia, PhD

Associate Professor

Accepting PhD Students

Calculated based on number of publications stored in Pure and citations from Scopus
1993 …2023

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Personal profile

Personal profile

Marina Kriajevska graduated from the Moscow State University, where she studied virology and biochemistry. She obtained her PhD in biochemistry from the Institute of Genetics of the Russian Academy of Sciences. She undertook post-doctoral training in the laboratory of Professor Saida Zain at the University of Rochester, NY, USA. She then worked as a research scientist in the laboratory of Professor Eugene Lukanidin at the Danish Cancer Society in Copenhagen.

Marina started her independent research as a Lecturer in Cancer Cell Biology in the Department of Cancer Studies and Molecular Medicine, University of Leicester, UK. She studied calcium-binding S100 proteins in regulating myosin dynamics and tumor cell motility in cellular models of Epithelial Mesenchymal transition. She analyzed cell motility and invasiveness in zebrafish embryo tumor xenografts.

Currently, her research focuses on mechanisms of tumor cell plasticity and cell signaling in bladder cancer and, in particular, on how TAM receptors control cell-to-cell communications and invasiveness.


Research interests

My research focuses on cell signaling in bladder cancer. I study how the members of the TAM family of receptor tyrosine kinases (TYRO3, AXL, and MER), contribute to bladder cancer progression by integrating stimuli present in the tumor microenvironment.

We evaluate the association between the TAM receptors' expression levels and patients’ survival and the effects of TAM receptors activation on tumor cell viability and proliferation. In my group, we search for the biomarkers of tumor response to TAM-targeted therapy. We use Western blotting, ELISA, and immunohistochemistry to analyze the expression of membranous TAM receptors, and their shed ectodomains in urine and tumor samples. In addition, we establish and apply various cancer models including tumor explants and 2D & 3D cultures of the commercial bladder cancer cell lines.  As an approach to personalized medicine, I am passionate to generate patient-derived bladder cancer organoid cultures.  These preclinical cancer models closely recapitulate the architecture and heterogeneity of original tumors. Tumor organoids enable us to perform preclinical studies validating TAM receptors as therapeutic targets in bladder cancer.       


  1. Zhu W, Kriajevskaia M, Chou WG: A retroviral sequence of the Chinese hamster ovary cell line. Oncogene, 7,  2081-2083, 1992.
  2. Zhu W, Kriajevskaia M, Chou WG: A "trans-acting" factor for activation of transcription is defective in the xrs-5 mutant of the chinese hamster ovary cell line. Mutation Research, 294, 101-108, 1993.
  3. Kriajevska MV, Zakharova LG, Altstein AD: Viable double vaccinia virus recombinants with the non-inducible phage T7 expression system. J Gen Virol, 74, 47-53, 1993.
  4. Kriajevska MV, Zakharova LG, Altstein AD: Genetic instability of vaccinia virus containing artificially duplicated genome regions. Virus Res, 31, 123-137 1994.
  5. Grigorian, M, Tulchinsky E, Zain S, Ebralidze A, Kramerov D, Kriajevska M, Georgiev G, Lukanidin E: The mts1 gene and control of tumor metastasis. Gene, 135, 229-238, 1993.
  6. Kriajevska M, Neira M, Ambartsumian N, Georgiev GP, Lukanidin E: Non-muscle myosin as a posible target for protein encoded by metastasis-related mts1 gene. J Biol Chem, 239, 19679-19682, 1994.
  7. Ambartsumian N, Grigorian M, Kriajevska M, Tulchinsky E, Lukanidin E: Metastasis associated mts1 gene: regulation of RNA expression and identification of its target. Clin Exp Metastasis, 12, 7, 1994.
  8. Kriajevska M, Tarabykina S, Bronstein I, Maitland N, Lomonosov M, Hansen K, Georgiev G, Lukanidin E: Metastasis associated Mts1 (S100A4) protein modulates protein kinase C phosphorylation of the heavy chain of nonmuscle myosin. J Biol Chem,  273, 9852-9856, 1998.
  9. Tarabykina S, Kriajevska M, Scott D, Hill T, Lafitte D, Derrick P, Dodson G, Lukanidin E, Bronstein I: Heterocomplex formation between metastasis-related protein S100A4 (Mts1) and S100A1 as revealed by the yeast two-hybrid system. FEBS Letters, 475, 187-191, 2000.
  10. Kriajevska M, Bronstein I, Scott D, Tarabykina S, Fisher-Larsen M, Issinger O-G, Lukanidin E: Metastasis-associated protein Mts1(S100A4) inhibits CK2-mediated phosphorylation and self-assembly of the heavy chain of nonmuscle myosin. Biochem Biophys Acta, 1498, 252-263, 2000.
  11. Novitskaya V, Grigorian M, Kriajevska M, Tarabykina S, Bronstein I, Berezin V, Bock E, Lukanidin E: Oligomeric forms of the metastasis related Mts1 (S100A4) protein stimulate neuronal differentiation in cultures of rat hippocampal neurons. J  Biol  Chem, 275, 41278-41286, 2000.
  12. Grigorian M, Andersen S, Tulchinsky E, Kriajevska M, Carlberg C, Kruse C, Cohn M, Ambartsumian N, Selivanova G, Lukanidin E: Tumor suppressor p53protein is a new target for the metastasis-associated Mts1/S100A4 protein: functional consequences of their interaction. J Biol Chem, 276, 22699-22708, 2001. 
  13. Tarabykina S., Scott D.J., Herzyk P., Hill T.J., Tame J.R., Kriajevska M, Lafitte D., Derrick P.J., Dodson G.G., Maitland N.J., Lukanidin E.M., Bronstein I.B.: The dimerisation interface of the metastasis associated protein S100A4 (Mts1): In vivo and In vitro studies. J Biol Chem, 276, 24212-2422, 2001.
  14. Ambartsumian N., Klingelhofer J., Grigorian M., Christensen C., Kriajevska M., Tulchinsky E., Georgiev G., Berezin V., Bock E., Rygaard J., Cao R., Cao Y., Lukanidin E.: The metastasis-associated Mts1 (S100A4) protein could act as an agiogenic factor. Oncogene, 20, 4685-4695, 2001. 
  15. Mikkelsen S.E., Novitskaya V., Kriajevska M., Berezin V., Bock E., Norrild B., Lukanidin E: S100A12 protein is a strong inducer of neurite outgrowth from primary hippocampal neurons. J. Neurochemistry, 79, 767-776, 2001. 
  16. Kriajevska, M., Fischer-Larsen, M., Moertz, E., Vorm, O., Tulchinsky, E., Grigorian, M., Ambartsumian, N., and Lukanidin, E.: Liprin β1, a member of the family of LAR transmembrane tyrosine phophatase-interacting proteins, is a new target for the metastasis-associated protein S100A4 (Mts1). J Biol Chem, 277, 5229-5235, 2002.
  17. Wozniak, S.P., Colquhoun, A.J., Kriajevska, M., and Mellon, J.K. GEFITINIB ('IRESSA', ZD1839) enhances the anti-proliferative effect of radiation therapy in bladder cancer cells in vitro. European Urology, Supplements 2 (6), pp. CVII, 2003.      
  18. McHugh, L.A., Griffiths, T.R.L., Kriajevska, M, Symonds, R.P., and Mellon, J.K.: Tyrosine kinase inhibitors as adjuncts to systemic chemotherapy for muscle-invasive bladder cancer. Urology, 63, 619-624, 2004.
  19. El-Naaman,C., Grum-Schwensen, B., Mansouri, A., Grigorian, M., Santoni-Rugiu,E., Hansen,T.,                             Kriajevska, M., Schafer, B.W., Heizmann, C.W., Lukanidin, E., and Ambartsumian, N. Cancer predisposition in    mice deficient  for the metastasis-associated Mts1(S100A4) gene. Oncogene, 23, 3670-3680, 2004.
  20. Andersen, H., Mejlvang, J., Mahmood, S., Gromova, I., Gromov, P., Lukanidin, E., Kriajevska, M., Mellon, J.K., and Tulchinsky, E. Immediate and delayed effects of E-cadherin inhibition on gene regulation and cell motility in human epidermoid carcinoma cells. Mol Cell Biol, 25, 9138-9150, 2005.
  21. Kriajevska, M, Bronstein, I. and Lukanidin, E.: Assembly/disassembly of myosin filaments in the presence of EF-hand calcium-binding protein S100A4 in vitro. Chapter 6.44 in the Book Cell Biology Protocols. J.R. Harris (Edit), G.M. Graham (Co-Edit.), D.Rickwood (Co-Edit) , March  2006.
  22. McHugh, L.A., Kriajevska, M., Mellon, J.K., Griffiths, T.R.L. Combined treatment of bladder cancer cell lines with lapatinib and varying chemotherapy regimens – evidence of schedule-dependent synergy . Urology, 69, 390-394, 2007.    
  23. Mejlvang, J., Kriajevska, M., Berditchevski, F., Bronstein, I., Lukanidin, E., Pringle, H., Mellon, J.K., and Tulchinsky, E. Characterization of E-cadherin-dependent and -independent events in a new model of c-Fos-mediated epithelial-mesenchymal transition. Exp Cell Res, 313, 380-393, 2007.
  24. Tarabykina, S., Griffiths, T.R.L., Tulchinsky, E, Mellon, K., Bronstein, I.B., and Kriajevska, M. Metastasis-associated protein S100A4: spotlight on its role in cell migration. Current Cancer Drug Targets, 7, 217-228, 2007.
  25. Colquhoun, A.J., McHugh LA, Tulchinsky, E., Kriajevska, M., and Mellon, J.K. Combination treatment with ionising radiation and gefitinib (‘Iressa’, ZD1839), an epidermal growth factor receptor (EGFR) inhibitor, significantly inhibits bladder cancer cell growth in vitro and in vivo. J Radiat Res (Tokyo), 48, 351-360, 2007.
  26. Mejlvang,J., Kriajevska,M., Vandewalle,C., Chernova,T., Berx,G., Mellon, JK., and Tulchinsky, E.   Direct repression of cyclin D1 by SIP1 attenuates cell cycle progression in cells undergoing an epithelial mesenchymal transition. Mol Biol Cell, 18, 4615-4624, 2000. Gingras, A., Basran,,J.,  Prescott ,A.,  Kriajevska, M., Bagshaw , C., Barsukov, I. Crystal structure of the Ca(2+)-form and Ca(2+)-binding kinetics of metastasis-associated protein, S100A4. FEBS Lett, 582, 1651-1656, 2008.
  27. McHugh, L.A, Sayan, A.E, Mejlvang, J., Griffiths, T.R., Sun ,Y., Manson,  M.M., Tulchinsky, E., Mellon, J.K., and Kriajevska, M. Lapatinib, a dual inhibitor of ErbB-1/-2 receptors, enhances effects of combination chemotherapy in bladder cancer cells. Int J Oncol. 34, 1155-1163, 2009.
  28. Sayan, A.E., Griffiths, T.R., Pal, R., Browne, G.J., Ruddick, A., Yagci, T., Edwards, R., Mayer, N.J., Qazi, H., Goyal, S., Fernandez, S., Straatman, K., Jones, G.D., Bowman, K.J., Colquhoun, A., Mellon, J.K., Kriajevska, M.,  and Tulchinsky, E. SIP1 protein protects cells from DNA damage-induced apoptosis and has independent prognostic value in bladder cancer. Proc Natl Acad Sci U S A. 106, 14884-14889, 2009.
  29. Badyal, S.K., Basran, J., Bhanji, N., Kim, J.H., Chavda, A.P., Jung, H.S., Craig, R., Elliott, P.R., Irvine, A.F., Barsukov, I.L., Kriajevska, M.,  and Bagshaw, C.R. Mechanism of the Ca(2+)-Dependent Interaction between S100A4 and Tail Fragments of Nonmuscle Myosin Heavy Chain IIA. J Mol Biol.  405, 1004-1026, 2011. 
  30. Sayan AE, Stanford R, Vickery R, Grigorenko E, Diesch J, Kulbicki K, Edwards R, Pal R, Greaves P, Jariel-Encontre I, Piechaczyk M, Kriajevska M, Mellon JK, Dhillon AS, Tulchinsky E. Fra-1 controls motility of bladder cancer cells via transcriptional upregulation of the receptor tyrosine kinase AXL. Oncogene. 31, 493-1503, 2012. 
  31. Elliott PR, Irvine AF, Jung HS, Tozawa K, Pastok MW, Picone R, Badyal SK, Basran J, Rudland PS, Barraclough R, Lian LY, Bagshaw CR, Kriajevska M, Barsukov IL. Asymmetric Mode of Ca(2+)-S100A4 Interaction with Nonmuscle Myosin IIA Generates Nanomolar Affinity Required for Filament Remodeling. Structure, 20, 654-666, 2012. 
  32. Sun Y, Cheng MK, Griffiths TR, Mellon JK, Kai B, Kriajevska M, Manson MM. Inhibition of STAT signalling in bladder cancer by diindolylmethane: relevance to cell adhesion, migration and proliferation. Current Cancer Drug Targets, 1, 57-68, 2013. 
  33. Tulchinsky E, Demidov O, Kriajevska M, Barlev N, Imyanitov E. EMT: a mechanism for escape from EGFR-targeted therapy in lung cancer. Biochim Biophys Acta Rev Cancer, 1871, 29-39, 2019.
  34. Al-Ismaeel Q, Neal CP, Al-Mahmoodi H, Almutairi Z, Al-Shamarti I, Straatman K, Jaunbocus N, Irvine A, Eyad I,  Moreman C, Dennison AR, A. Sayan E, McDearmid J, Greaves P, Tulchinsky E, and Kriajevska M. ZEB1 and IL-6/11-STAT3 signalling cooperate to define invasive potential of pancreatic cancer cells via differential regulation of the expression of S100 proteins. BJC, 121, 65-75, 2019. 
  35. Auyez A, Sayan AE, Kriajevska M, and Tulchinsky E. AXL receptor in cancer metastasis and drug resistance: when normal functions go askew. Cancers (Basel), 13, 4864-4881, 2021.                                                                                                                                                                                                                                                           


Education/Academic qualification

Virology/Biochemistry, BSc/MSc

Biochemistry, PhD


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