Probable interaction between S100A7 and E-FABP in the cytosol of human keratinocytes from psoriatic scales.
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.
Mesh Terms:
Calcium-Binding Proteins, Carrier Proteins, Cells, Cultured, Cytosol, Fatty Acid-Binding Proteins, Humans, Keratinocytes, Myelin P2 Protein, Neoplasm Proteins, Precipitin Tests, Protein Binding, Psoriasis, S100 Proteins, Tumor Suppressor Proteins, Up-Regulation
Calcium-Binding Proteins, Carrier Proteins, Cells, Cultured, Cytosol, Fatty Acid-Binding Proteins, Humans, Keratinocytes, Myelin P2 Protein, Neoplasm Proteins, Precipitin Tests, Protein Binding, Psoriasis, S100 Proteins, Tumor Suppressor Proteins, Up-Regulation
Mol. Cell. Biochem.
Date: Feb. 01, 1999
PubMed ID: 10331666
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