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首页> 外文期刊>Cellular Oncology: Analytical Cellular Pathology >Integrin-Linked Kinase: A Multi-functional Regulator Modulating Extracellular Pressure-Stimulated Cancer Cell Adhesion through Focal Adhesion Kinase and AKT
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Integrin-Linked Kinase: A Multi-functional Regulator Modulating Extracellular Pressure-Stimulated Cancer Cell Adhesion through Focal Adhesion Kinase and AKT

机译：整合素链接的激酶：多功能调节器通过粘着斑激酶和AKT调节细胞外压力刺激癌细胞的粘附。

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摘要

Cell adhesion is important in cancer metastasis. Malignant cells in cancer patients may be exposed to physical forces such as extracellular pressure and shear, that stimulate their adhesion to matrix proteins, endothelium and surgical wounds. Pressure induces phosphorylation of AKT and focal adhesion kinase (FAK), which are required for pressure-stimulated cancer cell adhesion, but what mediates this effect is unknown. ILK may influence cell adhesion and FAK and AKT phosphorylation in other settings. We therefore hypothesized that ILK might also regulate pressure-stimulated cancer cell adhesion through AKT and FAK phosphorylation. Silencing ILK by siRNA reduced basal cancer cell adhesion and prevented the stimulation of adhesion by pressure. ILK mediated pressure-stimulated adhesion through specifically regulating phosphorylation of AKT at Ser473 and FAK at Tyr397 and 576 as well as ILK association with FAK and AKT. The siRNA-mediated loss of function of ILK in regulating increase in adhesion by pressure was not rescued by overexpression ofα-parvin, an important ILK binding partner, although pressure promoted ILK–α-parvin association and translocated both ILK andα-parvin from cytosol to membrane/cytoskeleton. ILK may be a key mediator of mechanotransduced signals in cancer cells and an important therapeutic target to inhibit metastatic cancer cell adhesion.
机译：细胞粘附在癌症转移中很重要。癌症患者的恶性细胞可能会受到细胞外压力和剪切力等物理作用力的刺激，从而刺激其与基质蛋白，内皮和外科伤口的粘附。压力会诱导AKT和粘着斑激酶（FAK）的磷酸化，这是压力刺激癌细胞粘附所必需的，但介导此作用的是未知的。在其他情况下，ILK可能会影响细胞粘附以及FAK和AKT磷酸化。因此，我们假设ILK也可能通过AKT和FAK磷酸化来调节压力刺激的癌细胞粘附。通过siRNA沉默ILK可减少基础癌细胞的粘附并防止压力刺激粘附。 ILK通过特异性调节Ser473的AKT和Tyr397和576的FAK的磷酸化以及ILK与FAK和AKT的缔合来介导压力刺激的粘附。 siRNA介导的ILK通过压力调节粘附增加的功能丧失不能通过过表达α-parvin（一种重要的ILK结合伴侣）来挽救，尽管压力促进了ILK-α-parvin的结合并使ILK和α-parvin都从细胞质中转移到细胞质中。膜/细胞骨架。 ILK可能是癌细胞中机械转导信号的关键介体，并且是抑制转移性癌细胞粘附的重要治疗靶标。

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