CHANGES IN KERATINOCYTE ADHESION DURING TERMINAL DIFFERENTIATION - REDUCTION IN FIBRONECTIN BINDING PRECEDES ALPHA-5-BETA-1-INTEGRIN LOSS FROM THE CELL-SURFACE
CHANGES IN KERATINOCYTE ADHESION DURING TERMINAL DIFFERENTIATION - REDUCTION IN FIBRONECTIN BINDING PRECEDES ALPHA-5-BETA-1-INTEGRIN LOSS FROM THE CELL-SURFACE
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DOI：
10.1016/0092-8674(90)90175-e
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发表时间：
1990-10-19
期刊：
影响因子：
64.5
通讯作者：
WATT, FM
中科院分区：
文献类型：
--
作者：
ADAMS, JC;WATT, FM
在终末分化过程中，角质形成细胞从表皮的基底层移出，从而失去与基膜的接触。我们发现，在培养中，终末分化包括纤维连接蛋白、层粘连蛋白和I型和IV型胶原的黏附性丧失。黏附性的改变发生在. α .2. β蛋白丧失几个小时之前。1, .alpha.3.beta。1和。alpha.5.beta。细胞表面的1个整合素。角化细胞与纤维连接蛋白的粘附是由α .5. β介导的。完整细胞对纤维连接蛋白粘附能力的下降与。α。5. β的能力下降有关。1个受体结合纤维连接蛋白。因此，在终末分化早期，整合素功能的调节可能是决定细胞向基底层迁移的早期事件。
During terminal differentiation keratinocytes move out of the basal layer of the epidermis and thereby lose contact with the basement membrane. We show that terminal differentiation in culture involves loss of adhesiveness of fibronectin, laminin, and collagen types I and IV. The adhesive changes precede, by several hours, loss of the .alpha.2.beta.1, .alpha.3.beta.1, and .alpha.5.beta.1 integrins from the cell surface. Keratinocyte adhesion to fibronectin is mediated by the .alpha.5.beta.1 integrin, and the decrease in adhesion of intact cells to fibronectin is correlated with a decrease in the ability of .alpha.5.beta.1 receptors to bind fibronectin. Thus modulation of integrin function early in terminal differentiation may be an early event determining cell migration out of the basal layer.