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Measuring Binding of S100 Proteins to RAGE by Surface Plasmon Resonance

  • Estelle Leclerc
Protocol
Part of the Methods in Molecular Biology book series (MIMB, volume 963)

Abstract

Surface plasmon resonance (SPR) is a label-free biophysical method that allows to measure the binding parameters (ka, kd, KD) of the interaction between two molecules. In this method, one protein/molecule (ligand) is immobilized on the surface of a sensor chip, while the other molecule (analyte) is in solution.

We describe here the use of SPR to measure the binding parameters of the interaction between S100 proteins and isolated domains of the receptor for advanced glycation endproducts (RAGE). In particular, we present the protocols that allow to measure the binding of S100B to RAGE V domain, and the binding of S100A1 and S100A6 to RAGE V-C1-C2 domain fused to a Glutathione S-Transferase (GST) moiety (GST-RAGE).

Key words

Surface plasmon resonance SPR S100B S100A1 S100B Receptor for advanced ­glycation endproducts RAGE Calcium-binding proteins EF-hand 

References

  1. 1.
    Berridge MJ, Lipp P, Bootman MD (2000) The versatility and universality of calcium signalling. Nat Rev Mol Cell Biol 1:11–21PubMedCrossRefGoogle Scholar
  2. 2.
    Heizmann CW, Krebs J, Moss SE (2004) Calcium signal transduction and cellular control mechanisms. Biochim Biophys Acta 1742:1–206CrossRefGoogle Scholar
  3. 3.
    Chazin WJ (2011) Relating form and function of EF-hand calcium binding proteins. Acc Chem Res 44:171–179PubMedCrossRefGoogle Scholar
  4. 4.
    Kawasaki H, Nakayama S, Kretsinger RH (1998) Classification and evolution of EF-hand proteins. Biometals 11:277–295PubMedCrossRefGoogle Scholar
  5. 5.
    Leclerc E, Stürchler E, Heizmann CW (2009) Calcium regulation by EF-hand proteins in the brain. In: Mikoshiba K (ed) Handbook of neurochemistry and molecular neurobiology. Springer, New York, pp 509–532CrossRefGoogle Scholar
  6. 6.
    Bernstein HG, Blazejczyk M, Rudka T, Gundelfinger ED, Dobrowolny H, Bogerts B et al (2005) 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. Neuropathol Appl Neurobiol 31:314–324PubMedCrossRefGoogle Scholar
  7. 7.
    Donato R (2003) Intracellular and extracellular roles of S100 proteins. Microsc Res Tech 60:540–551PubMedCrossRefGoogle Scholar
  8. 8.
    Dattilo BM, Fritz G, Leclerc E, Kooi CW, Heizmann CW, Chazin WJ (2007) The extracellular region of the receptor for advanced glycation end products is composed of two independent structural units. Biochemistry 46:6957–6970PubMedCrossRefGoogle Scholar
  9. 9.
    Ostendorp T, Leclerc E, Galichet A, Koch M, Demling N, Weigle B et al (2007) Structural and functional insights into RAGE activation by multimeric S100B. EMBO J 26:3868–3878PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 2013

Authors and Affiliations

  1. 1.Department of Pharmaceutical SciencesNorth Dakota State UniversityFargoUSA

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