Biochemical evidence for a homophilic interaction of the alpha 3 beta 1 integrin.
Biochemical evidence for a homophilic interaction of the alpha 3 beta 1 integrin.
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发表时间：
1993-10
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通讯作者：
P. Sriramarao;P. Steffner;K. Gehlsen
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作者：
P. Sriramarao;P. Steffner;K. Gehlsen
这项研究的目的是确定α3β1整合素是否可以以亲和性的方式相互作用。一些早期的报告表明，某些整合素黏附受体，即α2β1、α3β1和α6β4定位于细胞间黏附结构，因此可能参与细胞-细胞相互作用(Carter，W.G.，Wayner，E.A.，Bouchard，T.S.和Kaur，P.(1990)J.Cell Biol)。110,1387-1404；Kaufmann，R.，Frosch，D.，Westphal，C.，Weber，L.和Klein，C.E.(1989)J.细胞生物学。109,1807-1815；Hynes，R.O.(1987)Cell 48,549-554；Symington，B.E.，Takada，Y.和Carter，W.G.(1993)J.120、523-)。我们在此提供的数据表明，整合素α3β1可能在含有这种特定受体的细胞-细胞黏附结构中同源相互作用，或者，在局灶性黏附中发现的受体聚集体中也可能存在同源作用。通过人层粘连蛋白或多肽GD-6-Sepharose的亲和层析纯化了α3β1受体，并将其用作细胞黏附分析的底物。固定化的α3β1支持含有α3β1的细胞的黏附，这种黏附被抗β1和α3亚基的单抗特异性地抑制。此外，含有纯化的α3β1的亲和矩阵只与细胞表面蛋白洗涤剂提取物中的α3β1特异结合，这种结合是阳离子依赖的。最后，利用涉及表面等离子体共振原理的生物传感器技术(Biacore，Pharmacia生物传感器)，当α3β1结合到羧甲基葡聚糖修饰的金表面时，被发现只与其他可溶的α3β1受体结合，而不结合其他纯化的整合素，包括α5β1和αvβ3。这些数据强烈表明，在我们的实验条件下，α3β1可能以亲和性的方式相互作用。
The purpose of this study was to determine if the alpha 3 beta 1 integrin could interact in a homophilic manner. Several earlier reports have shown that certain integrin adhesion receptors, namely alpha 2 beta 1, alpha 3 beta 1, and alpha 6 beta 4 localize to intercellular adhesion structures and, therefore, may participate in cell-cell interactions (Carter, W. G., Wayner, E. A., Bouchard, T. S., and Kaur, P. (1990) J. Cell Biol. 110, 1387-1404; Kaufmann, R., Frosch, D., Westphal, C., Weber, L., and Klein, C. E. (1989) J. Cell Biol. 109, 1807-1815; Hynes, R. O. (1987) Cell 48, 549-554; Symington, B. E., Takada, Y., and Carter, W. G. (1993) J. Cell Biol. 120, 523-535). We present data herein suggesting that the integrin alpha 3 beta 1 may interact homophilically in such cell-cell adhesion structures which contain this specific receptor or, alternatively, in receptor aggregates found in focal adhesions. The alpha 3 beta 1 receptor was purified by affinity chromatography on either human laminin or peptide GD-6-Sepharose and subsequently used as a substrate in cell adhesion assays. The immobilized alpha 3 beta 1 supported the adhesion of cells containing alpha 3 beta 1, and this attachment was specifically inhibited by monoclonal antibodies to both beta 1 and alpha 3 subunits. In addition, an affinity matrix containing purified alpha 3 beta 1 showed specific binding of only alpha 3 beta 1 from detergent extracts of cell surface proteins and such binding was cation-dependent. Finally, using biosensor technology involving the principle of surface plasmon resonance (BIAcore, Pharmacia Biosensor), alpha 3 beta 1, when bound to a carboxymethyl dextran-modified gold surface, was found to bind only other soluble alpha 3 beta 1 receptors and did not bind other purified integrins, including alpha 5 beta 1 and alpha v beta 3. These data strongly suggest that alpha 3 beta 1 likely interacts in a homophilic manner under our experimental conditions.