Table of Contents
International Journal of Proteomics
Volume 2014, Article ID 153712, 8 pages
http://dx.doi.org/10.1155/2014/153712
Research Article

Dimerization of Peptides by Calcium Ions: Investigation of a Calcium-Binding Motif

1Department of Neurology, Laboratory of Neuro-Oncology, Erasmus Medical Center, 3015 GE Rotterdam, The Netherlands
2Thermo Fisher Scientific, 1046 AA Amsterdam, The Netherlands

Received 27 February 2014; Accepted 11 June 2014; Published 14 September 2014

Academic Editor: Christian Huck

Copyright © 2014 Azadeh Jamalian et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. J. Krebs and M. Michalak, Calcium: A Matter of Life or Death, Elsevier, Amsterdam, The Netherlands, 2007.
  2. D. Laurencin, A. Wong, J. V. Hanna, R. Dupree, and M. E. Smith, “A high-resolution 43Ca solid-state NMR study of the calcium sites of hydroxyapatite,” Journal of the American Chemical Society, vol. 130, no. 8, pp. 2412–2413, 2008. View at Publisher · View at Google Scholar · View at Scopus
  3. J. L. Gifford, M. P. Walsh, and H. J. Vogel, “Structures and metal-ion-binding properties of the Ca2+-binding helix-loop-helix EF-hand motifs,” Biochemical Journal, vol. 405, no. 2, pp. 199–221, 2007. View at Publisher · View at Google Scholar · View at Scopus
  4. W. Xin, D. R. Rhodes, C. Ingold, A. M. Chinnaiyan, and M. A. Rubin, “Dysregulation of the annexin family protein family is associated with prostate cancer progression,” American Journal of Pathology, vol. 162, no. 1, pp. 255–261, 2003. View at Publisher · View at Google Scholar · View at Scopus
  5. B. M. Frey, B. F. X. Reber, B. S. Vishwanath, G. Escher, and F. J. Frey, “Annexin I modulates cell functions by controlling intracellular calcium release,” The FASEB Journal, vol. 13, no. 15, pp. 2235–2245, 1999. View at Google Scholar · View at Scopus
  6. M. P. Mattson and S. L. Chan, “Neuronal and glial calcium signaling in Alzheimer's disease,” Cell Calcium, vol. 34, no. 4-5, pp. 385–397, 2003. View at Publisher · View at Google Scholar · View at Scopus
  7. K. G. Baimbridge, M. R. Celio, and J. H. Rogers, “Calcium-binding proteins in the nervous system,” Trends in Neurosciences, vol. 15, no. 8, pp. 303–308, 1992. View at Publisher · View at Google Scholar · View at Scopus
  8. H. G. Bernstein, M. Blazejczyk, T. Rudka et al., “The Alzheimer disease-related calcium-binding protein Calmyrin is present in human forebrain with an altered distribution in Alzheimer's as compared to normal ageing brains,” Neuropathology and Applied Neurobiology, vol. 31, no. 3, pp. 314–324, 2005. View at Publisher · View at Google Scholar · View at Scopus
  9. D. Foell and J. Roth, “Proinflammatory S100 proteins in arthritis and autoimmune disease,” Arthritis and Rheumatism, vol. 50, no. 12, pp. 3762–3771, 2004. View at Publisher · View at Google Scholar · View at Scopus
  10. X. Wang, M. Kirberger, F. Qiu, G. Chen, and J. J. Yang, “Towards predicting Ca2+-binding sites with different coordination numbers in proteins with atomic resolution,” Proteins: Structure, Function and Bioinformatics, vol. 75, no. 4, pp. 787–798, 2009. View at Publisher · View at Google Scholar · View at Scopus
  11. D. Chin and A. R. Means, “Calmodulin: a prototypical calcium sensor,” Trends in Cell Biology, vol. 10, no. 8, pp. 322–328, 2000. View at Publisher · View at Google Scholar · View at Scopus
  12. V. Gerke and S. E. Moss, “Annexins: from structure to function,” Physiological Reviews, vol. 82, no. 2, pp. 331–371, 2002. View at Google Scholar · View at Scopus
  13. D. E. Clapham, “Calcium signaling,” Cell, vol. 131, no. 6, pp. 1047–1058, 2007. View at Publisher · View at Google Scholar · View at Scopus
  14. Y. Zhou, W. Yang, M. Kirberger, H. Lee, G. Ayalasomayajula, and J. J. Yang, “Prediction of EF-hand calcium-binding proteins and analysis of bacterial EF-hand proteins,” Proteins: Structure, Function and Genetics, vol. 65, no. 3, pp. 643–655, 2006. View at Publisher · View at Google Scholar · View at Scopus
  15. J. J. Falke, S. K. Drake, A. L. Hazard, and O. B. Peersen, “Molecular tuning of ion binding to calcium signaling proteins,” Quarterly Reviews of Biophysics, vol. 27, no. 3, pp. 219–290, 1994. View at Publisher · View at Google Scholar · View at Scopus
  16. S. Linse and S. Forsén, “Determinants that govern high-affinity calcium binding.,” Calcium Regulation of Cellular Function, vol. 30, pp. 89–151, 1995. View at Google Scholar · View at Scopus
  17. W. Cho and R. V. Stahelin, “Membrane binding and subcellular targeting of C2 domains,” Biochimica et Biophysica Acta: Molecular and Cell Biology of Lipids, vol. 1761, no. 8, pp. 838–849, 2006. View at Publisher · View at Google Scholar · View at Scopus
  18. K. J. Jobst, J. K. Terlouw, P. J. A. Ruttink, and P. C. Burgers, “Dissociation of CuH+ center dot and ZnH+ complexes of ethylenediamine and their n-methylated homologues: family and neighbours, but not the same,” International Journal of Mass Spectrometry, vol. 354-355, pp. 144–151, 2013. View at Publisher · View at Google Scholar · View at Scopus
  19. G. P. F. Wood, L. Radom, G. A. Petersson, E. C. Barnes, M. J. Frisch, and J. A. Montgomery, “A restricted-open-shell complete-basis-set model chemistry,” Journal of Chemical Physics, vol. 125, no. 9, Article ID 094106, 2006. View at Publisher · View at Google Scholar · View at Scopus
  20. M. J. Frisch, G. W. Trucks, H. B. Schlegel et al., Gaussian 03, Rev D. 01, Gaussian Inc., Wallingford, UK, 2004.
  21. K. J. Jobst, J. K. Terlouw, T. M. Luider, and P. C. Burgers, “On the interaction of peptides with calcium ions as studied by matrix-assisted laser desorption/ionization fourier transform mass spectrometry: towards peptide fishing using metal ion baits,” Analytica Chimica Acta, vol. 627, no. 1, pp. 136–147, 2008. View at Publisher · View at Google Scholar · View at Scopus
  22. J. B. Cumming and P. Kebarle, “Summary of gas phase acidity measurements involving acids AH. Entropy changes in proton transfer reactions involving negative ions. Bond dissociation energies D(A-H) and electron affinities EA(A),” Canadian Journal of Chemistry, vol. 56, no. 1, pp. 1–9, 1978. View at Publisher · View at Google Scholar
  23. M. Meot-Ner and L. W. Sieck, “Relative acidities of water and methanol and the stabilities of the dimer anions,” Journal of Physical Chemistry, vol. 90, no. 25, pp. 6687–6690, 1986. View at Publisher · View at Google Scholar · View at Scopus
  24. R. G. Cooks, J. T. Koskinen, and P. D. Thomas, “Special feature: commentary - the kinetic method of making thermochemical determinations,” Journal of Mass Spectrometry, vol. 34, pp. 85–92, 1999. View at Google Scholar
  25. H. F. Grützmacher and A. Caltapanides, “Dissociation of proton-bound complexes and proton affinity of benzamides,” Journal of the American Society for Mass Spectrometry, vol. 5, no. 9, pp. 826–836, 1994. View at Publisher · View at Google Scholar · View at Scopus
  26. O. V. Nemirovskiy and M. L. Gross, “Intrinsic Ca2+ affinities of peptides: application of the kinetic method to analogs of calcium-binding site III of rabbit skeletal troponin C,” Journal of the American Society for Mass Spectrometry, vol. 11, no. 9, pp. 770–779, 2000. View at Publisher · View at Google Scholar · View at Scopus
  27. D. Pu and C. J. Cassady, “Negative ion dissociation of peptides containing hydroxyl side chains,” Rapid Communications in Mass Spectrometry, vol. 22, no. 2, pp. 91–100, 2008. View at Publisher · View at Google Scholar · View at Scopus
  28. S. G. Lias, J. E. Bartmess, J. F. Liebman, J. L. Holmes, R. D. Levin, and W. G. Mallard, “Gas-phase ion and neutral thermochemistry,” Journal of Physical and Chemical Reference Data, vol. 17, no. 1, pp. 1–861, 1988. View at Google Scholar
  29. A. G. Harrison, “The gas-phase basicities and proton affinities of amino acids and peptides,” Mass Spectrometry Reviews, vol. 16, no. 4, pp. 201–217, 1997. View at Publisher · View at Google Scholar · View at Scopus
  30. S. W. Vetter and E. Leclerc, “Novel aspects of calmodulin target recognition and activation,” European Journal of Biochemistry, vol. 270, no. 3, pp. 404–414, 2003. View at Publisher · View at Google Scholar · View at Scopus
  31. M. Eberhard and P. Erne, “Calcium and magnesium binding to rat parvalbumin,” European Journal of Biochemistry, vol. 222, no. 1, pp. 21–26, 1994. View at Publisher · View at Google Scholar · View at Scopus
  32. M. Maki, Y. Kitaura, H. Satoh, S. Ohkouchi, and H. Shibata, “Structures, functions and molecular evolution of the penta-EF-hand Ca2+-binding proteins,” Biochimica et Biophysica Acta, vol. 1600, no. 1-2, pp. 51–60, 2002. View at Publisher · View at Google Scholar · View at Scopus
  33. E. Bastianelli, “Distribution of calcium-binding proteins in the cerebellum,” Cerebellum, vol. 2, no. 4, pp. 242–262, 2003. View at Publisher · View at Google Scholar · View at Scopus
  34. W. Witke, A. Hofmann, B. Köppel, M. Schleicher, and A. A. Noegel, “The Ca2+-binding domains in non-muscle type α-actinin: biochemical and genetic analysis,” The Journal of Cell Biology, vol. 121, no. 3, pp. 599–606, 1993. View at Publisher · View at Google Scholar · View at Scopus
  35. J. B. Ames, T. Porumb, T. Tanaka, M. Ikura, and L. Stryer, “Amino-terminal myristoylation induces cooperative calcium binding to recoverin,” The Journal of Biological Chemistry, vol. 270, no. 9, pp. 4526–4533, 1995. View at Publisher · View at Google Scholar · View at Scopus
  36. I. Marenholz, C. W. Heizmann, and G. Fritz, “S100 proteins in mouse and man: from evolution to function and pathology (including an update of the nomenclature),” Biochemical and Biophysical Research Communications, vol. 322, no. 4, pp. 1111–1122, 2004. View at Publisher · View at Google Scholar · View at Scopus
  37. S.-H. Cheng, M. R. Willmann, H.-C. Chen, and J. Sheen, “Calcium signaling through protein kinases. The Arabidopsis calcium-dependent protein kinase gene family,” Plant Physiology, vol. 129, no. 2, pp. 469–485, 2002. View at Publisher · View at Google Scholar · View at Scopus