Structure and function of a vimentin-associated matrix adhesion in endothelial cells
Structure and function of a vimentin-associated matrix adhesion in endothelial cells
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DOI：
10.1091/mbc.12.1.85
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发表时间：
2001-01-01
影响因子：
3.3
通讯作者：
Jones, JCR
中科院分区：
文献类型：
--
作者：
Gonzales, M;Weksler, B;Jones, JCR
α 4层粘连蛋白亚基是内皮细胞基底膜的组分。针对α 4层粘连蛋白G结构域的抗体（2A 3）染色转化的和原代微血管内皮细胞（分别为TrHBMEC和HMVEC）中的局灶性接触样结构，条件是后者细胞用生长因子活化。2A 3抗体染色与α v和β 3整联蛋白抗体产生的染色共定位，并且与该定位一致，TrHBMEC和HMVEC以α v β 3整联蛋白依赖性方式粘附于α 4层粘连蛋白亚基G结构域。α v β 3整联蛋白/2A 3抗体阳性染色的局灶性接触被粘着斑蛋白抗体以及抗凝集素的抗体识别。不寻常的是，波形蛋白中间丝，除了微丝束，与许多α v β 3整合素阳性的局灶性接触。我们研究了培养的内皮细胞中α 4-层粘连蛋白和α v β 3-整联蛋白的功能，它们是这些焦点接触的核心。针对这些蛋白质的抗体在体外抑制TrHBMEC和HMVEC的分支形态发生，以及它们在体外伤口中再增殖的能力。因此，我们已经表征了内皮细胞基质粘附，其显示复杂的细胞骨架相互作用，并且其组装受生长因子调节。我们的数据表明，这种粘附结构可能在血管生成中发挥作用。
The alpha4 laminin subunit is a component of endothelial cell basement membranes. An antibody (2A3) against the alpha4 laminin G domain stains focal contact-like structures in transformed and primary microvascular endothelial cells (TrHBMECs and HMVECs, respectively), provided the latter cells are activated with growth factors. The 2A3 antibody staining colocalizes with that generated by alphav and beta3 integrin antibodies and, consistent with this localization, TrHBMECs and HMVECs adhere to the alpha4 laminin subunit G domain in an alphav beta3-integrin-dependent manner. The alphav beta3 integrin/2A3 antibody positively stained focal contacts are recognized by vinculin antibodies as well as by antibodies against plectin. Unusually, vimentin intermediate filaments, in addition to microfilament bundles, interact with many of the alphav beta3 integrin-positive focal contacts. We have investigated the function of alpha4-laminin and alphav beta3-integrin, which are at the core of these focal contacts, in cultured endothelial cells. Antibodies against these proteins inhibit branching morphogenesis of TrHBMECs and HMVECs in vitro, as well as their ability to repopulate in vitro wounds. Thus, we have characterized an endothelial cell matrix adhesion, which shows complex cytoskeletal interactions and whose assembly is regulated by growth factors. Our data indicate that this adhesion structure may play a role in angiogenesis.