Insights into binding of S100 proteins to scavenger receptors: class B scavenger receptor CD36 binds S100A12 with high affinity

Research output: Contribution to journalResearch articleContributedpeer-review


  • Christoph Tondera - , Faculty of Chemistry and Food Chemistry, Helmholtz-Zentrum Dresden-Rossendorf (Author)
  • Markus Laube - , Helmholtz-Zentrum Dresden-Rossendorf (Author)
  • Jens Pietzsch - , Helmholtz-Zentrum Dresden-Rossendorf, Dresden University of Technology (Author)


The EF-hand type calcium-binding protein S100A12 exerts numerous intra- and extracellular functions of (patho)physiological relevance. Therefore, receptors of S100A12 are of high interest for research and clinical applications. Beside the extensively studied receptor for advanced glycation endproducts (RAGE), G-protein coupled receptors and more recently, scavenger receptors are suggested to be putative S100A12 receptors. Own findings and further information from the literature predestined CD36, a class B scavenger receptor, as promising candidate. To substantiate or prove against this hypothesis, this study aimed at investigation of interaction of S100A12 and CD36 on molecular and cellular level by the use of surface plasmon resonance (SPR), radio- and fluorescence-tracer-based cell binding, and cell activation experiments. S100A12 revealed binding affinity to CD36 in the low nanomolar range, essentially, at the CD36 thrombospondin-1 binding site. Additionally, S100A12-mediated translocation of CD36 to the membrane and elevation of both CD36 and peroxisome proliferator-activated receptor γ (PPARγ) expression was observed, which suggest a potential regulatory function of S100A12–CD36 interaction.


Original languageEnglish
Pages (from-to)183-191
Number of pages9
JournalAmino acids
Issue number1
Publication statusPublished - 1 Jan 2017

External IDs

PubMed 27734162
Scopus 84991107838



  • Damage-associated molecular patterns, EF-hand calcium-binding proteins, Pattern recognition receptors, Receptor for advanced glycation endproducts (RAGE), Surface plasmon resonance