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首页> 外文期刊>The Biochemical Journal >Calcium-binding protein S100A7 and epidermal-type fatty acid-binding protein are associated in the cytosol of human keratinocytes.
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Calcium-binding protein S100A7 and epidermal-type fatty acid-binding protein are associated in the cytosol of human keratinocytes.

机译：钙结合蛋白S100A7和表皮型脂肪酸结合蛋白在人角质形成细胞的胞质溶胶中相关。

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Expression of epidermal-type fatty acid-binding protein (E-FABP) and S100A7 has previously been shown to be elevated in psoriatic skin, a disease characterized by abnormal keratinocyte differentiation. However, no causal relationship between the up-regulation of these proteins and the disease has been shown. E-FABP is thought to be involved in cytosolic fatty acid (FA) transport, whereas the role of S100A7 is still unknown. In this report, we show by overlay assays that E-FABP, immobilized on nitrocellulose, is able to capture S100A7 from cytosolic psoriatic protein extracts and vice versa, suggesting the formation of a complex between the two proteins. Using purified E-FABP and S100A7, the complex can be reconstituted only in presence of EDTA. Moreover, we show that increased EDTA concentrations in psoriatic cytosolic protein extracts enhance complex formation. Partial complex disruption was obtained by the addition of physiological concentrations of Zn2+ (0.1 mM), whereas Ca2+ at 5 mM and Mg2+ at 30 mM had no effect. On the other hand, high Ca2+ concentrations (30 mM) resulted in partial complex disruption. Oleic acid-binding properties were observed for free E-FABP and the complex E-FABP-S100A7, but not for free S100A7. By using confocal microscopy we show that S100A7 and E-FABP are co-localized in the cytoplasm of differentiating keratinocytes from lesional psoriatic skin. These data indicate that formation of the E-FABP-S100A7 complex and its FA-binding function might be regulated at least by bivalent cations.
机译：先前已证明表皮型脂肪酸结合蛋白（E-FABP）和S100A7的表达在牛皮癣皮肤中升高，牛皮癣皮肤是一种以异常的角质形成细胞分化为特征的疾病。但是，这些蛋白质的上调与疾病之间没有因果关系。 E-FABP被认为与胞质脂肪酸（FA）的运输有关，而S100A7的作用仍是未知的。在本报告中，我们通过重叠测定法表明，固定在硝化纤维素上的E-FABP能够从胞质银屑病蛋白提取物中捕获S100A7，反之亦然，表明这两种蛋白之间形成了复合物。使用纯化的E-FABP和S100A7，仅在EDTA存在下才能还原该复合物。此外，我们显示银屑病胞质蛋白提取物中增加的EDTA浓度会增强复合物的形成。通过添加生理浓度的Zn2 +（0.1 mM）获得部分复合物破坏，而5 mM的Ca2 +和30 mM的Mg2 +没有影响。另一方面，高Ca2 +浓度（30 mM）导致部分复合物破坏。对于游离的E-FABP和复合物E-FABP-S100A7观察到油酸结合性质，而对于游离的S100A7则没有观察到。通过使用共聚焦显微镜，我们显示S100A7和E-FABP共同定位在与皮损皮损皮肤分化的角质形成细胞的细胞质中。这些数据表明E-FABP-S100A7复合物的形成及其FA结合功能可能至少受二价阳离子调节。

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