The Human Integrin α8β1 Functions as a Receptor for Tenascin, Fibronectin, and Vitronectin (*)
The Human Integrin α8β1 Functions as a Receptor for Tenascin, Fibronectin, and Vitronectin (*)
复制标题
人类整合素 α8β1 作为腱蛋白、纤连蛋白和玻连蛋白的受体发挥作用 (*)
DOI：
--
复制
发表时间：
1995
影响因子：
4.8
通讯作者：
R. Pytela
中科院分区：
文献类型：
--
作者：
L. Schnapp;N. Hatch;D. M. Ramos;I. Klimanskaya;D. Sheppard;R. Pytela
粘附受体整合素家族由至少21种异二聚体跨膜蛋白组成，这些蛋白在组织分布和配体特异性上存在差异。最近发现的α8整合素亚基与β1相关，主要表达于成人组织的平滑肌和其他收缩细胞，以及发育过程中的间充质细胞和神经细胞。我们现在发现α8β1特异性定位于细胞外基质蛋白纤维连接蛋白或玻璃体连接蛋白上的局灶接触。此外，我们发现转染α8 cDNA的人胚胎肾细胞（293）在其表面表达α8β1，并利用该受体粘附纤维连接蛋白和玻璃体连接蛋白。此外，α8β1可以结合纤维连接蛋白-和玻璃体连接蛋白- sepharose，并且可以通过含有精氨酸-甘氨酸-天冬氨酸（RGD）的肽GRGDSP特异性地从基质蛋白中洗脱。由于纤维连接蛋白和玻璃体连接蛋白的粘附似乎是由RGD介导的，我们研究了其他含有RGD的蛋白，包括腱蛋白、纤维蛋白原、血栓反应蛋白、骨桥蛋白和变性i型胶原。我们发现只有腱蛋白能够介导α8转染的293细胞的粘附。通过在粘附实验中使用tenascin的重组片段，我们能够将tenascin的α8β1结合域定位到含有rgd的第3个纤维连接蛋白III型重复序列上。这些数据有力地表明，腱蛋白、纤维连接蛋白和玻璃体连接蛋白是α8β1的配体，并且这种整合素通过不同的机制与含有α5和αv的整合素结合到这些配体的RGD位点。
The integrin family of adhesion receptors consists of at least 21 heterodimeric transmembrane proteins that differ in their tissue distribution and ligand specificity. The recently identified α8 integrin subunit associates with β1 and is predominantly expressed in smooth muscle and other contractile cells in adult tissues, and in mesenchymal and neural cells during development. We now show that α8β1 specifically localizes to focal contacts in cells plated on the extracellular matrix proteins fibronectin or vitronectin. In addition we show that human embryonic kidney cells (293), transfected with α8 cDNA, express α8β1 on their surface and use this receptor for adhesion to fibronectin and vitronectin. Furthermore, α8β1 binds to both fibronectin- and vitronectin-Sepharose and can be specifically eluted from either matrix protein by the arginine-glycine-aspartic acid (RGD)-containing peptide, GRGDSP. Because fibronectin and vitronectin adhesion appeared to be mediated by RGD, we examined additional RGD-containing proteins, including tenascin, fibrinogen, thrombospondin, osteopontin, and denatured collagen type I. We found that only tenascin was able to mediate adhesion of α8-transfected 293 cells. By using recombinant fragments of tenascin in adhesion assays, we were able to localize the α8β1 binding domain of tenascin to the RGD-containing, third fibronectin type III repeat. These data strongly suggest that tenascin, fibronectin, and vitronectin are ligands for α8β1 and that this integrin binds to the RGD site in each of these ligands through mechanisms that are distinct and separate from α5-and αv-containing integrins.
登录
查看更多内容
影响因子：
4
作者：
Karl R. Fath;C.-J. S. Edgell;Keith Burridge
通讯作者：
Karl R. Fath;C.-J. S. Edgell;Keith Burridge
影响因子：
4
作者：
L. M. Schnapp;Johannes M. Breuss;Daniel M. Ramos;D. Sheppard;R. Pytela
通讯作者：
L. M. Schnapp;Johannes M. Breuss;Daniel M. Ramos;D. Sheppard;R. Pytela
DOI：
10.1016/s0021-9258(18)47074-3
发表时间：
1994-10
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Y. Yokosaki;E. Palmer;A. L. Prieto;K. L. Crossin;M. Bourdon;R. Pytela;D. Sheppard
通讯作者：
Y. Yokosaki;E. Palmer;A. L. Prieto;K. L. Crossin;M. Bourdon;R. Pytela;D. Sheppard
DOI：
10.1073/pnas.90.21.10154
发表时间：
1993-11-01
影响因子：
11.1
作者：
PRIETO, AL;EDELMAN, GM;CROSSIN, KL
通讯作者：
CROSSIN, KL
影响因子：
20.1
作者：
CLYMAN, RI;MCDONALD, KA;KRAMER, RH
通讯作者：
KRAMER, RH