INTEGRIN RECEPTORS AND FUNCTION ON CULTURED GLOMERULAR ENDOTHELIAL-CELLS
INTEGRIN RECEPTORS AND FUNCTION ON CULTURED GLOMERULAR ENDOTHELIAL-CELLS
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DOI：
10.1038/ki.1993.242
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发表时间：
1993-08-01
影响因子：
19.6
通讯作者：
ENG, B
中科院分区：
文献类型：
--
作者：
ADLER, S;ENG, B
研究了整合素在大鼠肾小球内皮细胞（GEndoC）克隆系上的表达和功能，以更好地了解这些细胞与肾小球基底膜成分相互作用的方式。培养GEndoC粘附于纤维连接蛋白、层粘连蛋白、I型和IV型胶原，表达alpha1beta1、alpha2beta1、alpha3beta1、alpha5beta1、α (v)beta1和α (v)beta3整合素。合成RGDS肽显著降低纤维连接蛋白粘附（53.1 +/-对照的4.7%）。大鼠β 1整合素抗体对层粘连蛋白、纤维连接蛋白、I型和IV型胶原的粘附有较强的抑制作用（分别为对照组的1.2、19.0、67.3和31.9%），而对大鼠α 1整合素链抗体对层粘连蛋白的粘附有较强的抑制作用（对照组的65.2%），对IV型胶原的粘附仅轻度抑制（对照组的77.2%），对I型胶原的粘附不产生影响（对照组的97.8%）。GEndoC裂解物在固定化I型胶原柱上的亲和层析显示，alpha3beta1整合素主要与微量的alpha1beta1和alpha2beta1结合，证明了alpha3beta1在GEndoC与胶原的粘附中起主要作用。对固定的纤维连接蛋白细胞结合片段的色谱分析显示，α (v) β 1整合素是这些细胞上主要的纤维连接蛋白受体，但α (v) β 3整合素抗体也记录了α (v) β 1或α (v) β 3在纤维连接蛋白粘附中起次要作用。培养的GEndoC在体外表达与体内相似的整合素受体阵列。进一步研究这些受体在正常和病变肾小球中的功能，可能为了解以内皮脱离或内皮下蛋白沉积为特征的疾病状态的发病机制提供重要的见解。
Integrin expression and function on a cloned line of rat glomerular endothelial cells (GEndoC) were studied in an effort to obtain a better understanding of the means by which these cells interact with components of the glomerular basement membrane. Cultured GEndoC adhered to fibronectin, laminin and types I and IV collagen and expressed alpha1beta1, alpha2beta1, alpha3beta1, alpha5beta1, alpha(v)beta1 and alpha(v)beta3 integrins. Synthetic RGDS peptides significantly decreased adhesion to fibronectin (53.1 +/- 4.7% of control). Antibody to rat beta1 integrin strongly inhibited adhesion to laminin, fibronectin and types I and IV collagen (I 1.2, 19.0, 67.3 and 31.9% of control adhesion, respectively), while antibody to the rat a, integrin chain strongly inhibited adhesion to laminin (65.2% of control), but only mildly inhibited adhesion to type IV collagen (77.2% of control) and did not affect adhesion to type I collagen (97.8% of control). Affinity chromatography of GEndoC lysates on a column of immobilized type I collagen displayed predominantly binding of alpha3beta1 integrin with trace amounts of alpha1beta1, and alpha2beta1, documenting the major role of alpha3beta1, in GEndoC adhesion to collagen. Chromatography on the immobilized cell-binding fragment of fibronectin revealed the alpha5beta1 integrin to be the major fibronectin receptor on these cells, but antibody to alpha(v)beta3 integrin also documented a minor role for alpha(v)beta1 or alpha(v)beta3 in fibronectin adhesion. Cultured GEndoC express a similar array of integrin receptors in vitro as they do in vivo. Further study of the function of these receptors in normal and diseased glomeruli may provide important insights into the pathogenesis of disease states characterized by endothelial detachment or subendothelial protein deposition.