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

被引：33
|
作者：
Hagens, G
Roulin, K
Hotz, R
Saurat, JH
Hellman, U
Siegenthaler, G [1 ]
机构：
[1] Univ Hosp Geneva, Dept Dermatol, CH-1211 Geneva 14, Switzerland
[2] Univ Hosp Geneva, DHURDV, CH-1211 Geneva 14, Switzerland
[3] Ludwig Inst Canc Res, S-75124 Uppsala, Sweden
来源：
MOLECULAR AND CELLULAR BIOCHEMISTRY | 1999年 / 192卷 / 1-2期
关键词：
psoriasis; calcium-binding protein; protein-protein interaction;
D O I：
10.1023/A:1006894909694
中图分类号：
Q2 [细胞生物学];
学科分类号：
071009 ; 090102 ;
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.
引用
收藏
页码：123 / 128
页数：6
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