THE HUMAN INTEGRIN VLA-2 IS A COLLAGEN RECEPTOR ON SOME CELLS AND A COLLAGEN LAMININ RECEPTOR ON OTHERS
THE HUMAN INTEGRIN VLA-2 IS A COLLAGEN RECEPTOR ON SOME CELLS AND A COLLAGEN LAMININ RECEPTOR ON OTHERS
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DOI：
10.1073/pnas.86.24.9906
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发表时间：
1989-12-01
影响因子：
11.1
通讯作者：
HEMLER, ME
中科院分区：
文献类型：
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作者：
ELICES, MJ;HEMLER, ME
整合素异二聚体VLA-2以前被称为胶原受体，现在被证明也是层粘连蛋白受体。抗VLAα2抗体可抑制人黑色素瘤细胞株LOX与层粘连蛋白的黏附。由于VLA-2介导的LOX细胞与层粘连蛋白的黏附不会被胶原酶消化所抑制，因此层粘连蛋白的胶原污染不是一个因素。此外，来自LOX细胞的VLA-2可与固定化层粘连蛋白结合，EDTA可阻断其结合，但Arg-Gly-Asp(RGD)肽不能阻断其结合。VLA-3也与层粘连蛋白-琼脂糖结合，尽管不如VLA-2强烈。因此，整合素β1亚家族中至少有四个独立的成员作为层粘连蛋白受体，即VLA-2和VLA-3(本研究)以及VLA-1和VLA-6(其他报道)。虽然LOX和其他细胞系同时使用VLA-2作为层粘连蛋白和胶原受体，但成纤维细胞VLA-2介导胶原而不是层粘连蛋白结合。同样，来自血小板的VLA-2不与层粘连蛋白相互作用。尽管有这种功能上的不一致，来自层粘连蛋白结合和非结合来源的VLA-2在所有检测的免疫化学和生化标准中都是无法区分的。因此，VLA-2的功能差异可能是由于细胞类型特定的调节所致。
The integrin heterodimer VLA-2, previously known as a collagen receptor, is now shown also to be a laminin receptor. Adhesion of the human melanoma cell line LOX to laminin was inhibited by anti-VLA .alpha.2 antibodies. Because VLA-2-mediated LOX cell attachment to laminin was not inhibited by digestion with collagenase, collagen contamination of laminin was not a factor. In addition, VLA-2 from LOX cells bound to immobilized laminin, and binding was disrupted by EDTA but not by Arg-Gly-Asp (RGD) peptides. VLA-3 also bound to laminin-Sepharose, although less avidly than VLA-2. Thus, at least four separate members of the integrin .beta.1 subfamily serve as laminin receptors.sbd.i.e., VLA-2 and VLA-3 (this study) together with VLA-1 and VLA-6 (other reports). Whereas LOX and other cell lines used VLA-2 as both a laminin and collagen receptor, fibroblast VLA-2 mediated collagen but not laminin binding. Likewise, VLA-2 from platelets did not interact with laminin. Despite this functional discordancy, VLA-2 from laminin-binding and nonbinding sources was indistinguishable by all immunochemical and biochemical criteria examined. Thus, functional differences in VLA-2 may be due to cell type-specific modulation.