INTERACTION OF FIBRONECTIN WITH COLLAGEN - AGE-SPECIFIC DEFECT IN THE BIOLOGICAL-ACTIVITY OF HUMAN FIBROBLAST FIBRONECTIN
INTERACTION OF FIBRONECTIN WITH COLLAGEN - AGE-SPECIFIC DEFECT IN THE BIOLOGICAL-ACTIVITY OF HUMAN FIBROBLAST FIBRONECTIN
复制标题
DOI：
10.1073/pnas.80.15.4747
复制
发表时间：
1983-01-01
期刊：
影响因子：
--
通讯作者：
MILLIS, AJT
中科院分区：
文献类型：
--
作者：
CHANDRASEKHAR, S;SORRENTINO, JA;MILLIS, AJT
从早期传代和晚期传代（体外老化）人成纤维细胞分离的纤连蛋白显示出不同的支持细胞粘附和影响细胞形态的能力。由于成纤维细胞粘附需要纤连蛋白、细胞表面和细胞外基质组分之间的相互作用，因此检查了分离的细胞纤连蛋白中的那些功能。与从早期传代细胞中分离的纤连蛋白相比，来自晚期传代细胞的纤连蛋白与天然I型和II型胶原蛋白的结合较差。2种纤连蛋白与变性胶原的结合无差异。两种纤连蛋白与天然胶原蛋白的结合同样受到肝素的促进。通过使用Boyden室测定来测量响应于纤连蛋白的趋化性来评价细胞结合活性。在细胞结合中未检测到差异。分子量的比较NaDodSO 4 [十二烷基硫酸钠]/聚丙烯酰胺凝胶电泳显示，纤维连接蛋白从晚传细胞大于从早传细胞。在从条件培养基分离的纤连蛋白和从细胞层分离的纤连蛋白中均观察到该差异。晚期传代细胞显然产生结构和功能不同的纤连蛋白。与天然胶原蛋白的结合缺陷可能是衰老表型的某些方面。
Fibronectins isolated from early-passage and late-passage (in vitro aged) human fibroblasts were shown to differ in their ability to support cell adhesion and to influence cell morphology. Because fibroblast adhesion requires interactions between fibronectin, the cell surface and the components of the extracellular matrix, those functions in isolated cellular fibronectin were examined. In comparison to fibronectin isolated from early-passage cells, fibronectin from late-passage cells bound poorly to native collagen types I and II. No differences were observed in the binding of the 2 fibronectins to denatured collagen. The binding of both fibronectins to native collagen was similarly promoted by heparin. Cell binding activity was evaluated by using a Boyden chamber assay to measure chemotaxis in response to either fibronectin. No differences were detected in cell binding. Comparisons of MW by NaDodSO4[sodium dodecyl sulfate]/polyacrylamide gel electrophoresis reveal that fibronectin from late-passage cells is larger than that from early-passage cells. That difference is observed both in fibronectins isolated from conditioned media and in fibronectins isolated from the cell layer. Late-passage cells apparently produce a structurally and functionally distinct fibronectin. The defective binding to native collagen may account for some aspects of the aged phenotype.