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

被引:6
作者
Gerry Hagens
Karen Roulin
Raymonde Hotz
Jean-Hilaire Saurat
Ulf Hellman
Georges Siegenthaler
机构
[1] University Hospital,Department of Dermatology and DHURDV
[2] Ludwig Institute for Cancer Research,undefined
来源
Molecular and Cellular Biochemistry | 1999年 / 192卷
关键词
psoriasis; calcium-binding protein; protein-protein interaction;
D O I
暂无
中图分类号
学科分类号
摘要
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.
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页码:123 / 128
页数:5
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