Article

Molecular and Cellular Biochemistry

, Volume 192, Issue 1, pp 123-128

First online:

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

  • Gerry HagensAffiliated withDepartment of Dermatology and DHURDV, University Hospital
  • , Karen RoulinAffiliated withDepartment of Dermatology and DHURDV, University Hospital
  • , Raymonde HotzAffiliated withDepartment of Dermatology and DHURDV, University Hospital
  • , Jean-Hilaire SauratAffiliated withDepartment of Dermatology and DHURDV, University Hospital
  • , Ulf HellmanAffiliated withLudwig Institute for Cancer Research
  • , Georges SiegenthalerAffiliated withDepartment of Dermatology and DHURDV, University Hospital

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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.

psoriasis calcium-binding protein protein-protein interaction