Phosphorylation of Creatine Kinase in Myogenic Cells: Effects of Okadaic Acid and other Agents Affecting Cellular Protein Phosphorylation

  • W. Hemmer
  • M. Skarli
  • H. M. Eppenberger
  • T. Wallimann
Conference paper
Part of the NATO ASI Series book series (volume 76)

Abstract

Creatine Kinase (CK) is a key enzyme of eukaryotic energy metabolism. In chicken, the two cytosolic isoforms, brain- (B-CK) and muscle-type (M-CK), are expressed in a tissue specific manner. During muscle contraction, CK catalyzes the regeneration of ATP from phosphorylcreatine (PCr) and ADP (reviewed in Wallimann et al., 1992). In differentiating chicken embryonic skeletal muscle cells, during myotube formation, a CK isoenzyme transition from B-CK to M-CK takes place, which was also observed in cultured embryonic skeletal muscle cells (Perriard et al., 1978). B-CK is expressed at a high level until shortly after M-CK expression has started. This isoenzyme switch is part of the biochemical differentiation, which accompanies the morphological development of myoblasts. After leaving the cell cycle, postmitotic myoblasts align themselves into arrays and subsequently fuse to form multinucleated myotubes (see references in David et al., 1990). The myotubes show sarcomeric striations and are able to contract in culture, suggesting that their cellular metabolism resembles that of the in vivo situation. Essential steps in the process of myoblast fusion depend on the action of various protein kinases, such as the phospholipid/Ca2+-dependent protein kinase (PKC) and the Ca2+/calmodulin-dependent protein (CaM-) kinase (David et al., 1990). Cyclic AMP-dependent protein kinase (PKA) activity is also present during the time of fusion (Rogers et al., 1985).

Keywords

Tyrosine Electrophoresis Penicillin Methionine Streptomycin 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Chida, K., K. Kasahara, M. Tsunenaga, Y. Kohno, S. Yamada, S. Ohmi and T. Kuroki. 1990a. Purification and identification of creatine phosphokinase B as a substrate of protein kinase C in mouse skin in vivo. Biochem. Biophys. Res. Commun. 173:351–357.PubMedCrossRefGoogle Scholar
  2. Chida, K., M. Tsunenaga, K. Kasahara, Y. Kohno and T. Kuroki. 1990b. Regulation of creatine phosphokinase B activity by protein kinase C. Biochem. Biophys. Res. Commun. 173:346–350.PubMedCrossRefGoogle Scholar
  3. Cohen, P. 1989. The structure and regulation of protein phosphatases. Ann. Rev. Biochem. 58:453–508.PubMedCrossRefGoogle Scholar
  4. David, J. D., C. R. Faser and G. P. Perrot. 1990. Role of protein kinase C in chick embryo skeletal myoblast fusion. Dev. Biol. 139:89–99.PubMedCrossRefGoogle Scholar
  5. Entwistle, A., D. H. Curtis and R. J. Zalin. 1986. Myoblast fusion is regulated by a prostanoid of the one series independently of a rise in cyclic AMP. J. Cell Biol. 103:857–866.PubMedCrossRefGoogle Scholar
  6. Friedman, D. L., P. R. Puelo and M. B. Perryman. 1990. Phosphorylation of MM creatine kinase in striated muscle. FASEB J. 4:A2232.Google Scholar
  7. Hemmer, W., S. J. Glaser, G. R. Hartmann, H. M. Eppenberger and T. Wallimann. 1991. Covalent modification of creatine kianse by ATP: evidence for autophosphorylation. In NATO ASI Series: “Cellular Regulation by Protein Phosphorylation.” L. M. G. Heilmeyer, eds., Springer-Verlag, Berlin. H 56:143–147.Google Scholar
  8. Kemp, B. E. and R. B. Pearson. 1990. Protein kinase recognition sequence motifs. Trends Biochem. Sci. 15:342–346.PubMedCrossRefGoogle Scholar
  9. Kim, H. S., C. H. Chung, M.-S. Kang and D. B. Ha. 1991. Okadaic acid blocks membrane fusion of chick embryonic myoblasts in culture. Biochem. Biophys. Res. Commun. 176:1044–1050.PubMedCrossRefGoogle Scholar
  10. Mahadevan, L. C., S. A. Whatley, T. K. C. Leung and L. Lim. 1984. The brain form of a key ATP-regulating enzyme, creatine kinase, is a phosphoprotein. Biochem. J. 222:139–144.PubMedGoogle Scholar
  11. Perriard, J.-C., M. Caravatti, E. R. Perriard and H. M. Eppenberger. 1978. Quantitation of creatine kinase isoenzyme transitions in differentiating chicken embryonic breast muscle and myogenic cell cultures by immunoadsorption. Arch. Biochem. Biophys. 191:90–100.PubMedCrossRefGoogle Scholar
  12. Quest, A. F. G., T. Soldati, W. Hemmer, J.-C. Perriard, H. M. Eppenberger and T. Wallimann. 1990. Phosphorylation of chicken brain-type creatine kinase affects a physiologically important kinetic parameter and gives rise to protein microheterogeneity in vivo. FEBS Lett. 269:457–464.PubMedCrossRefGoogle Scholar
  13. Rogers, J. E., S. Narindrasorasak, G. A. Cates and B. D. Sanwal. 1985. Regulation of protein kinase A and its regulatory subunits during skeletal myogenesis. J. Biol. Chem. 260:8002–8007.PubMedGoogle Scholar
  14. Rosenberg, U. B., H. M. Eppenberger and J.-C. Perriard. 1981. Occurence of heterogenous forms of the subunits of creatine kinase in various muscle and nonmuscle tissues and their behaviour during myogenesis. Eur. J. Biochem. 116:87–92.PubMedCrossRefGoogle Scholar
  15. Schäfer, B. W. and J.-C. Perriard. 1988. Intracellular targeting of isoproteins in muscle cytoarchitecture. J. Cell Biol 106:1161–1170.PubMedCrossRefGoogle Scholar
  16. Soldati, T. and J.-C. Perriard. 1991. Intracompartmental sorting of essential myosin light chains: molecular dissection and in vivo monitoring by epitope tagging. Cell. 66:277–289.PubMedCrossRefGoogle Scholar
  17. Soldati, T., B. W. Schäfer and J.-C. Perriard. 1990. Alternative ribosomal initiation gives rise to chicken brain-type creatine kinase isoproteins with heterogeneous amino termini. J. Biol. Chem. 265:4498–4506.PubMedGoogle Scholar
  18. Wallimann, T., M. Wyss, D. Brdiczka, K. Nicolay and H. M. Eppenberger. 1992. Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the ‘phosphocreatine circuit’ for cellular energy homeostasis. Biochem. J. 281:21–40.PubMedGoogle Scholar
  19. Wirz, T., U. Brändie, T. Soldati, J. P. Hossle and J.-C. Perriard. 1990. A unique chicken B-creatine kinase gene gives rise to two B-creatine kinase isoproteins with distinct N termini by alternative splicing. J. Biol. Chem. 265:11656–11666.PubMedGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1993

Authors and Affiliations

  • W. Hemmer
    • 2
  • M. Skarli
    • 1
    • 2
  • H. M. Eppenberger
    • 2
  • T. Wallimann
    • 2
  1. 1.Neuromuscular Unit, Department of Pediatrics and Neonatal MedicineRoyal Postgraduate School, Hammersmith HospitalLondonUK
  2. 2.Institute for Cell BiologyETH-HönggerbergZürichSwitzerland

Personalised recommendations