Integrin alpha v beta 3 differentially regulates adhesive and phagocytic functions of the fibronectin receptor alpha 5 beta 1.
Integrin alpha v beta 3 differentially regulates adhesive and phagocytic functions of the fibronectin receptor alpha 5 beta 1.
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整联蛋白alpha vβ3差异调节纤连蛋白受体α5β1的粘附和吞噬功能。
DOI：
10.1083/jcb.127.4.1129
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发表时间：
1994-11
影响因子：
7.8
通讯作者：
Brown, E J
中科院分区：
文献类型：
--
作者：
Blystone, S D;Graham, I L;Lindberg, F P;Brown, E J
血浆纤维连接蛋白是创伤修复和宿主防御中的重要调理素。为了更好地理解纤连蛋白介导的吞噬作用的过程，我们用α v β 3转染了内源性表达α 5 β 1的K562细胞。在这些转染子中，针对α v β 3的抗体完全阻断纤连蛋白调理的珠粒的吞噬作用，即使一半的摄取通过内源性α 5 β 1受体发生。α 5 β 1介导的与纤连蛋白包被的表面的粘附不受α v β 3连接的影响。α v β 5和α M β 2连接均不影响表达这些受体的转染子中的α 5 β 1吞噬功能。药理学数据表明，α v β 3连接通过可能涉及蛋白激酶C的信号转导途径抑制高亲和力α 5 β 1受体的吞噬能力。除了其对吞噬作用的重要性之外，α v β 3对α 5 β 1功能的调节可能对于其在细胞迁移、转移和血管生成中的作用是重要的。
The plasma protein fibronectin is an important opsonin in wound repair and host defense. To better understand the process of fibronectin- mediated phagocytosis, we have transfected K562 cells, which endogenously express alpha 5 beta 1, with alpha v beta 3. In these transfectants, antibodies to alpha v beta 3 block phagocytosis of fibronectin-opsonized beads completely, even though half the ingestion occurs through endogenous alpha 5 beta 1 receptors. alpha 5 beta 1- mediated adhesion to fibronectin-coated surfaces is unaffected by alpha v beta 3 ligation. Neither alpha v beta 5 nor alpha M beta 2 ligation affects alpha 5 beta 1 phagocytic function in transfectants expressing these receptors. Pharmacologic data suggest that alpha v beta 3 ligation suppresses the phagocytic competence of high affinity alpha 5 beta 1 receptors through a signal transduction pathway, perhaps involving protein kinase C. In addition to its significance for phagocytosis, alpha v beta 3 regulation of alpha 5 beta 1 function may be significant for its roles in cell migration, metastasis, and angiogenesis.