Role of extracellular matrix-cell interaction and epidermal growth factor (EGF) on EGF-receptors and actin cytoskeleton arrangement in infantile pituitary cells
Role of extracellular matrix-cell interaction and epidermal growth factor (EGF) on EGF-receptors and actin cytoskeleton arrangement in infantile pituitary cells
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DOI：
10.1007/s00441-006-0248-7
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发表时间：
2007-01-01
影响因子：
3.6
通讯作者：
Mendoza-Garrido, M. Eugenia
中科院分区：
文献类型：
--
作者：
Toral, Claudia;Solano-Agama, Carmen;Mendoza-Garrido, M. Eugenia
表皮生长因子 (EGF) 会诱导培养的婴儿垂体细胞的细胞形态、肌动蛋白细胞骨架和粘附过程发生变化。细胞外基质通过整合素参与，与细胞信号传导中的生长因子协作。我们研究了胶原蛋白 I/III 和胶原蛋白加纤连蛋白在婴儿垂体细胞 EGF 反应中的细胞形态和肌动蛋白细胞骨架的参与情况。作为比较，我们使用聚赖氨酸作为底物。当婴儿细胞与细胞外基质蛋白结合时，它们会引发 EGF 反应，但以聚赖氨酸为底物则无法获得反应。细胞获得扁平形状并组织其肌动蛋白丝和纽蛋白，就像粘着斑一样。由于 EGF 受体 (EGFR) 与其他细胞中的肌动蛋白细胞骨架相连，构成细胞信号传导的微域，因此我们研究了婴儿垂体细胞中的这种关联和底物粘附参与。 EGFR与肌动蛋白细胞骨架相关的比例约为31%；所使用的基材之间没有观察到差异。悬浮细胞显示肌动蛋白相关的 EGFR，表明这种关联不依赖于细胞粘附。然而，没有观察到 EGFR 与肌动蛋白纤维共定位，这表明存在间接关联。与通过结构蛋白与肌动蛋白纤维连接的β(1)-整合素相比，EGFR 与肌动蛋白细胞骨架的结合更牢固。因此，这项研究表明细胞粘附依赖于肌动蛋白细胞骨架排列中的 EGF 效应；这可能受到肌动蛋白纤维/EGFR关联的青睐，该关联促进了婴儿垂体细胞中肌动蛋白细胞骨架组织的细胞信号传导途径。
Epidermal growth factor (EGF) induces changes in cell morphology, actin cytoskeleton, and adhesion processes in cultured infantile pituitary cells. The extracellular matrix, through integrin engagement, collaborates with growth factors in cell signaling. We have examined the participation of collagen I/III and collagen plus fibronectin in the EGF response of infantile pituitary cells with respect to their cell morphology and actin cytoskeleton. As a comparison, we have used poly-lysine as a substrate. Infantile cells elicit the EGF response when they are associated with extracellular matrix proteins, but no response can be obtained with poly-lysine as the substrate. Cells acquire a flattened shape and organize their actin filaments and vinculin as in focal adhesions. Because the EGF receptor (EGFR) is linked to the actin cytoskeleton in other cells structuring a microdomain in cell signaling, we have investigated this association and substrate adhesion participation in infantile pituitary cells. The proportion of EGFR associated with the actin cytoskeleton is approximately 31%; no difference has been observed between the substrates used. Cells in suspension show actin-associated EGFR, suggesting an association independent of cell adhesion. However, no colocalization of EGFRs with actin fibers has been observed, suggesting an indirect association. Compared with beta(1)-integrin, which is linked to actin fibers through structural proteins, EGFR binds more strongly with the actin cytoskeleton. This study thus shows cell adhesion dependence on the EGF effect in the actin cytoskeleton arrangement; this is probably favored by the actin fiber/EGFR association that facilitates the cell signaling pathways for actin cytoskeleton organization in infantile pituitary cells.