Molecular and Cellular Biochemistry

, Volume 192, Issue 1, pp 123–128

Probable interaction between S100A7 and E-FABP in the cytosol of human keratinocytes from psoriatic scales

Authors

  • Gerry Hagens
    • Department of Dermatology and DHURDVUniversity Hospital
  • Karen Roulin
    • Department of Dermatology and DHURDVUniversity Hospital
  • Raymonde Hotz
    • Department of Dermatology and DHURDVUniversity Hospital
  • Jean-Hilaire Saurat
    • Department of Dermatology and DHURDVUniversity Hospital
  • Ulf Hellman
    • Ludwig Institute for Cancer Research
  • Georges Siegenthaler
    • Department of Dermatology and DHURDVUniversity Hospital
Article

DOI: 10.1023/A:1006894909694

Cite this article as:
Hagens, G., Roulin, K., Hotz, R. et al. Mol Cell Biochem (1999) 192: 123. doi:10.1023/A:1006894909694

Abstract

The overexpression of E-FABP and S100A7 in lesional psoriatic skin suggests a possible link with this hyperproliferative skin disease. In order to investigate a role for the proteins in this disease, the purifications for both proteins were re-analyzed. Moreover, a specific antiserum directed against purified human S100A7 was generated. By SDS-PAGE immunoblotting we show that E-FABP and S100A7 are expressed in cultured human differentiating keratinocytes and confirm their overexpression in psoriatic scales. Gel filtration and non-denaturing PAGE revealed that S100A7 co-purified with E-FABP, indicating an association between the two proteins. Ion-exchange chromatography resulted in the dissociation of the complex. Finally, immunoprecipitations using antiserum against E-FABP revealed that S100A7 co-immunoprecipitated with E-FABP from protein extracts of psoriatic scales. These data indicate that E-FABP and S100A7 might form a complex in the cytosol of human keratinocytes.

psoriasiscalcium-binding proteinprotein-protein interaction
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Copyright information

© Kluwer Academic Publishers 1999