S100 protein subcellular localization during epidermal differentiation and psoriasis
S100 protein subcellular localization during epidermal differentiation and psoriasis
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DOI：
10.1177/002215540305100513
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发表时间：
2003-05-01
影响因子：
3.2
通讯作者：
Eckert, RL
中科院分区：
文献类型：
--
作者：
Broome, AM;Ryan, D;Eckert, RL
S100蛋白是钙激活的信号蛋白，与靶蛋白相互作用以调节生物过程。我们目前的研究比较了S100A7、S100A8、S100A9、S100A10和S100A11在正常和银屑病表皮中的表达水平和细胞定位。S100A7和S100A11存在于正常表皮的基底层和棘层。这些蛋白质出现在基底细胞的细胞核和细胞质中，但在棘细胞中与质膜相关。S100A10存在于基底细胞和棘细胞、细胞质中，并与质膜结合。S100A8和S100A9在正常表皮中不存在或以最低水平表达。在受累的银屑病组织中，S100A10和S100A11水平保持不变，而S100A7、S100A8和S100A9显著过表达。S100A7在正常组织和银屑病组织中的表达和亚细胞定位模式相似。S100A8和S100A9在银屑病相关组织的基底层和棘层中强烈表达。此外，我们证明，S100A7，S100A10和S100A11被纳入洗涤剂和还原剂抗性多聚体，这表明它们是体内转氨酶底物。S100A8和S100A9没有形成这些较大的复合物。这些结果表明，S100蛋白定位于分化的角质形成细胞的质膜，这表明在调节钙依赖性，膜相关事件的作用。这些研究还表明，如前所述，S100A7、S100A8和S100A9的表达在银屑病中显著改变，表明这些蛋白在疾病发病机制中的作用。
S100 proteins are calcium-activated signaling proteins that interact with target proteins to modulate biological processes. our present studies compare the level of expression, and cellular localization of S100A7, S100A8, S100A9, S100A10, and S100A11 in normal and psoriatic epidermis. S100A7 and S100A11 are present in the basal and spinous layers in normal epidermis. These proteins appear in the nucleus and cytoplasm in basal cells but are associated with the plasma membrane in spinous cells. S100A10 is present in basal and spinous cells, in the cytoplasm, and is associated with the plasma membrane. S100A8 and S100A9 are absent or are expressed at minimal levels in normal epidermis. In involved psoriatic tissue, S100A10 and S100A11 levels remain unchanged, whereas, S100A7, S100A8, and S100A9 are markedly overexpressed. The pattern of expression and subcellular localization of S100A7 is similar in normal and psoriatic tissue. S100A8 and S100A9 are strongly expressed in the basal and spinous layers in psoriasis-involved tissue. In addition, we demonstrate that S100A7, S100A10, and S100A11 are incorporated into detergent and reducing agent-resistant multimers, suggesting that they are in vivo transglutaminase substrates. S100A8 and S100A9 did not form these larger complexes. These results indicate that S100 proteins localize to the plasma membrane in differentiated keratinocytes, suggesting a role in regulating calcium-dependent, membrane-associated events. These studies also indicate, as reported previously, that S100A7, S100A8, and S100A9 expression is markedly altered in psoriasis, suggesting a role for these proteins in disease pathogenesis.