Identification of clusterin sequences mediating renal tubular cell interactions.
Identification of clusterin sequences mediating renal tubular cell interactions.
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DOI：
10.1034/j.1399-3011.1999.00145.x
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发表时间：
1999-11
期刊：
影响因子：
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通讯作者：
J. Silkensen;A. Skubitz;K. Skubitz;M. Rosenberg
中科院分区：
文献类型：
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作者：
J. Silkensen;A. Skubitz;K. Skubitz;M. Rosenberg
组织损伤后糖蛋白簇蛋白的表达显着增加。簇蛋白的功能之一是促进在这些病理环境中受到干扰的细胞相互作用。凝聚蛋白在体外引起细胞聚集和粘附，但这种作用的分子机制尚不清楚。为了鉴定凝聚素的活性位点，从人凝聚素的亲水区域合成了 34 个肽，每个肽长度为 15 个氨基酸残基。单独研究时，没有任何肽引起 LLC-PK1 细胞（一种猪肾上皮细胞系）的聚集。然而，34 种肽中的两种以剂量依赖性方式抑制凝聚素诱导的细胞聚集。这两种“活性”肽的乱序版本不会抑制细胞聚集。七种肽促进细胞粘附。总之，这些发现为介导凝聚素诱导的肾细胞相互作用的新氨基酸序列提供了证据。
Expression of the glycoprotein clusterin is markedly increased following tissue injury. One function of clusterin is to promote cell interactions which are perturbed in these pathologic settings. Clusterin causes cell aggregation and adhesion in vitro yet the molecular mechanism for this effect is not known. In order to identify the active site(s) of clusterin, 34 peptides, each 15 amino acid residues in length, were synthesized from hydrophilic regions of human clusterin. When studied individually, none of the peptides caused aggregation of LLC-PK1 cells, a porcine renal epithelial cell line. However, two out of the 34 peptides inhibited clusterin-induced cell aggregation in a dose-dependent manner. Scrambled versions of these two 'active' peptides did not inhibit cell aggregation. Seven peptides promoted cell adhesion. In conclusion, these findings provide evidence for novel amino acid sequences mediating clusterin-induced renal cell interactions.