BMB Reports

Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
권호 표지
DOI QR코드

DOI QR Code

Capsaicin, a component of red peppers, stimulates protein kinase CKII activity

  • Rho, Yun-Wha (School of Life Sciences and Biotechnology, College of Natural Sciences, Kyungpook National University) ;
  • Bae, Young-Seuk (School of Life Sciences and Biotechnology, College of Natural Sciences, Kyungpook National University)
  • Received : 2010.01.26
  • Accepted : 2010.03.03
  • Published : 2010.05.31
Download PDF
⟨ Previous Next ⟩

Abstract

Protein kinase CKII (CKII), a heterotetramer composed of two catalytic ($\alpha$ or $\alpha$') subunits and two regulatory ($\beta$) subunits, plays a critical role in cell proliferation and anti-apoptosis. Recently, capsaicin was shown to trigger apoptosis. Therefore, we examined the effect of capsaicin on CKII activity. Although capsaicin induced apoptotic death in HeLa cells, CKII activity was increased in the cytosolic fraction of HeLa cells after treatment. Capsaicin did not change the expression of the $CKII{\alpha}$ and $CKII{\beta}$ proteins. Capsaicin stimulated the catalytic activity of recombinant CKII tetramer, but not the $CKII{\alpha}$ subunit. Moreover, capsaicin enhanced the autophosphorylation of $CKII{\alpha}$ and $CKII{\beta}$. Taken together, our data suggest that capsaicin stimulates the phosphotransferase activity of CKII holoenzyme by interacting with the $CKII{\beta}$ subunit.

Keywords

References

  1. Pinna, L. A. (1990) Casein kinase 2: an 'eminence grise' in cellular regulation? Biochim. Biophys. Acta. 1054, 267-284. https://doi.org/10.1016/0167-4889(90)90098-X
  2. Issinger, O. G. (1993) Casein kinases: pleiotropic mediators of cellular regulation. Pharmacol. Ther. 59, 1-30. https://doi.org/10.1016/0163-7258(93)90039-G
  3. Litchfield, D. W. (2003) Protein kinase CK2: structure, regulation and role in cellular decisions of life and death. Biochem. J. 369, 1-5. https://doi.org/10.1042/BJ20021469
  4. Lin, W. J., Tuazon, P. T. and Traugh, J. A. (1991) Characterization of the catalytic subunit of casein kinase II expressed in Escherichia coli and regulation of activity. J. Biol. Chem. 266, 5664-5669.
  5. Jakobi, R. and Traugh, J. A. (1992) Characterization of the phosphotransferase domain of casein kinase II by site-directed mutagenesis and expression in Escherichia coli. J. Biol. Chem. 267, 23894-23902.
  6. Gietz, R. D., Graham, K. C. and Litchfield, D. W. (1995) Interactions between the subunits of casein kinase II. J. Biol. Chem. 270, 13017-13021. https://doi.org/10.1074/jbc.270.22.13017
  7. Hathaway, G. M., Lubben, T. H. and Traugh, J. A. (1980) Inhibition of casein kinase II by heparin. J. Biol. Chem. 255, 8038-8041.
  8. Cochet, C. and Chambaz, E. M. (1983) Polyamine-mediated protein phosphorylations: a possible target for intracellular polyamine action. Mol. Cell. Endocrinol. 30, 247-266. https://doi.org/10.1016/0303-7207(83)90062-X
  9. Seldin, D. C. and Leder, P. (1995) Casein kinase II? transgene-induced murine lymphoma: relation to theileriosis in cattle. Science 267, 894-897. https://doi.org/10.1126/science.7846532
  10. Hanna, D. E., Rethinaswamy, A. and Glover, C. V. (1995) Casein kinase II is required for cell cycle progression during G1 and G2/M in Saccharomyces cerevisiae. J. Biol. Chem. 270, 25905-25914. https://doi.org/10.1074/jbc.270.43.25905
  11. Krippner-Heidenreich, A., Talanian, R. V., Sekul, R., Kraft, R., Thole, H., Ottleben, H. and Luscher, B. (2001) Targeting of the transcription factor Max during apoptosis: phosphorylation-regulated cleavage by caspase-5 at an unusual glutamic acid residue in position P1. Biochem. J. 358, 705-715. https://doi.org/10.1042/0264-6021:3580705
  12. Desagher, S., Osen-Sand, A., Montessuit, S., Magnenat, E., Vilbois, F., Hochmann, A., Journot, L., Antonsson, B. and Martinou, J. C. (2001) Phosphorylation of Bid by casein kinases I and II regulates its cleavage by caspase 8. Mol. Cell. 8, 601-611. https://doi.org/10.1016/S1097-2765(01)00335-5
  13. Shin, S., Lee, Y., Kim, W., Ko, H., Choi, H. and Kim, K. (2005) Caspase-2 primes cancer cells for TRAIL-mediated apoptosis by processing procaspase-8. EMBO. J. 24, 3532-3542. https://doi.org/10.1038/sj.emboj.7600827
  14. Jung, M. Y., Kang, H. J. and Moon, A. (2001) Capsaicininduced apoptosis in SK-Hep-1 hepatocarcinoma cells involves Bcl-2 down-regulation and caspase-3 activation. Cancer Lett 165, 139-145. https://doi.org/10.1016/S0304-3835(01)00426-8
  15. Lee, Y. S., Nam, D. H. and Kim, J. A. (2000) Induction of apoptosis by capsaicin in A172 human glioblastoma cells. Cancer Lett. 161, 121-130. https://doi.org/10.1016/S0304-3835(00)00608-X
  16. Zhang, R., Humphreys, I., Sahu, R. P., Shi, Y. and Srivastava, S. K. (2008) In vitro and in vivo induction of apoptosis by capsaicin in pancreatic cancer cells is mediated through ROS generation and mitochondrial death pathway. Apoptosis 13, 1465-1478. https://doi.org/10.1007/s10495-008-0278-6
  17. Tewari, M., Quan, L. T., O'Rourke, K., Desnoyers, S., Zeng, Z., Beidler, D. R., Poirier, G. G., Salvesen, G. S. and Dixit, V. M. (1995) Yama/CPP32?, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell 81, 801-809. https://doi.org/10.1016/0092-8674(95)90541-3
  18. Hathaway, G. M. and Traugh, J. A. (1979) Cyclic nucleotide-independent protein kinases from rabbit reticulocytes. Purification of casein kinases. J. Biol. Chem. 254, 762-768.
  19. Kuenzel, E. A. and Krebs, E. G. (1985) A synthetic peptide substrate specific for casein kinase II. Proc. Natl. Acad. Sci. U.S.A. 82, 737-741. https://doi.org/10.1073/pnas.82.3.737
  20. Meggio, F., Brunati, A. M. and Pinna, L. A. (1983) Autophosphorylation of type 2 casein kinase TS at both its ${\alpha}-$ and ${\beta}-subunits$. Influence of different effectors. FEBS Lett. 160, 203-208. https://doi.org/10.1016/0014-5793(83)80967-3
  21. Meggio, F., Boldyreff, B., Issinger, O. G. and Pinna, L. A. (1994) Casein kinase 2 down-regulation and activation by polybasic peptides are mediated by acidic residues in the 55-64 region of the ${\beta}-subunit$. A study with calmodulin as phosphorylatable substrate. Biochemistry 33, 4336-4342. https://doi.org/10.1021/bi00180a030
  22. Lin, W. J., Tuazon, P. T. and Traugh, J. A. (1991) Characterization of the catalytic subunit of casein kinase II expressed in Escherichia coli and regulation of activity. J. Biol. Chem. 266, 5664-5669.
  23. Kim, M. S., Lee, Y. T., Kim, J. M., Cha, J. Y. and Bae, Y. S. (1988) Characterization of protein interaction among subunits of protein kinase CKII in vivo and in vitro. Mol. Cells 8, 43-48.