The integrin alpha9beta1 mediates adhesion to activated endothelial cells and transendothelial neutrophil migration through interaction with vascular cell adhesion molecule-1.
The integrin alpha9beta1 mediates adhesion to activated endothelial cells and transendothelial neutrophil migration through interaction with vascular cell adhesion molecule-1.
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整联蛋白α9BETA1通过与血管细胞粘附分子1的相互作用而介导了激活的内皮细胞和跨内皮性嗜中性粒细胞迁移。
DOI：
10.1083/jcb.145.2.413
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发表时间：
1999-04-19
影响因子：
7.8
通讯作者：
Sheppard, D
中科院分区：
文献类型：
--
作者：
Taooka, Y;Chen, J;Yednock, T;Sheppard, D
整合素α9β1在平滑肌和上皮细胞上广泛表达，并介导与细胞外基质蛋白骨桥蛋白和腱蛋白c的粘附。我们发现该整合素在tenascin-C中识别的肽序列与密切相关的整合素α4β1在诱导内皮配体血管细胞粘附分子-1 （VCAM-1）中识别的序列高度同源。因此，我们试图确定α9β1是否也识别VCAM-1，以及这种相互作用是否具有生物学意义。在本报告中，我们证实α9β1介导了重组VCAM-1和肿瘤坏死因子-α诱导的人脐静脉内皮细胞对VCAM-1的稳定粘附。此外，我们发现α9β1在中性粒细胞上高度选择性表达，并且对中性粒细胞在VCAM-1和tenascin-C上的迁移至关重要。最后，α9β1和α4整合素参与活化的内皮单层中性粒细胞趋化。这些观察结果提示α9β1/VCAM-1相互作用可能在急性炎症部位中性粒细胞外渗中起作用。
The integrin α9β1 has been shown to be widely expressed on smooth muscle and epithelial cells, and to mediate adhesion to the extracellular matrix proteins osteopontin and tenascin-C. We have found that the peptide sequence this integrin recognizes in tenascin-C is highly homologous to the sequence recognized by the closely related integrin α4β1, in the inducible endothelial ligand, vascular cell adhesion mole-cule-1 (VCAM-1). We therefore sought to determine whether α9β1 also recognizes VCAM-1, and whether any such interaction would be biologically significant. In this report, we demonstrate that α9β1 mediates stable cell adhesion to recombinant VCAM-1 and to VCAM-1 induced on human umbilical vein endothelial cells by tumor necrosis factor-α. Furthermore, we show that α9β1 is highly and selectively expressed on neutrophils and is critical for neutrophil migration on VCAM-1 and tenascin-C. Finally, α9β1 and α4 integrins contribute to neutrophil chemotaxis across activated endothelial monolayers. These observations suggest a possible role for α9β1/VCAM-1 interactions in extravasation of neutrophils at sites of acute inflammation.