Asian Pacific Journal of Cancer Prevention

Asian Pacific Journal of Cancer Prevention (아시아태평양암예방학회)
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CK2 Enzyme Affinity Against c-myc424-434 Substrate in Human Lung Cancer Tissue

  • Yaylim, Ilhan (Department of Molecular Medicine, Institute of Experimental Medicine, Istanbul University) ;
  • Ozkan, Nazli Ezgi (Department of Molecular Medicine, Institute of Experimental Medicine, Istanbul University) ;
  • Isitmangil, Turgut (Department of Thoracic Surgery, GATA Haydarpasa Training Hospital) ;
  • Isitmangil, Gulbu (Laboratory of Immunology, Haydarpasa Numune Training and Research Hospital) ;
  • Turna, Akif (Department of Thoracic Surgery, Cerrahpasa Medical Faculty, Istanbul University) ;
  • Isbir, Turgay (Multidiciplinary Molecular Medicine Department, Institute of Health Sciences, Yeditepe University)
  • Published : 2012.10.31
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Abstract

CK2 is a serine threonine kinase that participates in a variety of cellular processes with more than 300 defined substrates. This critical enzyme is known to be upregulated in cancers, but the role of this upregulation in carcinogenesis is not yet fully understood but c-myc, one of the defined CK2 substrates, is a well-known proto-oncogene that is normally essential in developmental process but is also involved in tumor development. We evaluated the optimal enzyme and substrate concentrations for CK2 activity in both neoplastic and non-neoplastic human lung tissues using the c-$myc^{424-434}$ peptide (EQKLISEEDL) as a substrate. The activities measured for the neoplastic tissue were 600-750 U/mg protein while those for the control tissue was in the range of 650-800 U/mg. $K_m$ value for c-myc peptide was determined as $0.33{\mu}M$ in non-neoplastic tissue and $0.18{\mu}M$ in neoplastic tissue. In this study, we did not observe an increased activity in the neoplastic tissue when compared with the non-neoplastic lung tissue, but we recorded two times higher affinity for c-$myc^{424-434}$ in cancer tissue. Considering the metabolic position of c-$myc^{424-434}$, our results suggest that phosphorylation by CK2 may be important in dimerization and thus it might affect the regulation of c-myc in cancer tissues.

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References

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