Inhibition of laminin self-assembly and interaction with type IV collagen by antibodies to the terminal domain of the long arm.
Inhibition of laminin self-assembly and interaction with type IV collagen by antibodies to the terminal domain of the long arm.
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DOI：
10.1083/jcb.103.5.1689
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发表时间：
1986-11
期刊：
影响因子：
--
通讯作者：
Furthmayr H
中科院分区：
文献类型：
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作者：
Charonis AS;Tsilibary EC;Saku T;Furthmayr H
层粘连蛋白是基底膜的主要糖蛋白。虽然其在该结构中的精确定位和取向尚不清楚，但它可能被锚定在其他大分子上，如IV型胶原或硫酸肝素蛋白。在体外，层粘连蛋白具有自组装能力，并在不同的位点与IV型胶原分子结合。为了更精确地识别参与这些相互作用的复杂的、十字形状的层粘连蛋白分子的结构域，通过旋转阴影法分析了层粘连蛋白-层粘连蛋白二聚体和层粘连蛋白IV型胶原复合物的图像。我们观察到层粘连蛋白长臂末端的复合体结构域主要参与这些相互作用。通过使用来自该复杂结构域的肽片段特异性抗体的Fab片段，通过浊度和电子显微镜测量，表明层粘连蛋白自组装在其存在下受到抑制。此外，这些抗体抑制层粘连蛋白与IV型胶原的特异性相互作用。这些数据表明，层粘连蛋白长臂末端的复杂结构域包含对基膜组装具有潜在重要性的结合位点。
Laminin is a major glycoprotein of the basement membrane. Although its precise localization and orientation within this structure is unknown, it is presumably anchored to other macromolecules such as type IV collagen or proteoheparan sulfate. In vitro, laminin has the ability to self-assemble and to bind to type IV collagen molecules at distinct sites. To identify more precisely the domains of the complex, cross- shaped laminin molecule that are involved in these interactions, images of laminin-laminin dimers and laminin-type IV collagen complexes obtained by the rotary shadowing method were analyzed. We observed that the complex domain at the end of the long arm of laminin is predominantly involved in these interactions. By using Fab fragments of antibodies specific for a peptide fragment derived from this complex domain, it is shown that laminin self-assembly is inhibited in their presence, as measured by turbidity and by electron microscopy. In addition, these antibodies inhibit the specific interaction of laminin with type IV collagen. These data suggest that the complex domain at the end of the long arm of laminin contains binding sites of potential importance for the assembly of basement membranes.