Kramer R H, Fuh G M, Karasek M A
Biochemistry. 1985 Dec 3;24(25):7423-30. doi: 10.1021/bi00346a059.
Cultured microvascular endothelial cells isolated from human dermis were examined for the synthesis of basement membrane specific (type IV) collagen and its deposition in subendothelial matrix. Biosynthetically radiolabeled proteins secreted into the culture medium were analyzed by sodium dodecyl sulfate gel electrophoresis after reduction, revealing a single collagenous component with an approximate Mr of 180 000 that could be resolved into two closely migrating polypeptide chains. Prior to reduction, the 180 000 bands migrated as a high molecular weight complex, indicating the presence of intermolecular disulfide bonding. The 180 000 material was identified as type IV procollagen on the basis of its selective degradation by purified bacterial collagenase, moderate sensitivity to pepsin digestion, immunoprecipitation with antibodies to human type IV collagen, and comigration with type IV procollagen purified from human and murine sources. In the basement membrane like matrix elaborated by the microvascular endothelial cells at their basal surface, type IV procollagen was the predominant constituent. This matrix-associated type IV procollagen was present as a highly cross-linked and insoluble complex that was solubilized only after denaturation and reduction of disulfide bonds. In addition, there was evidence of nonreducible dimers and higher molecular weight aggregates of type IV procollagen. These findings support the suggestion that the presence of intermolecular disulfide bonds and other covalent interactions stabilizes the incorporation of the type IV procollagen into the basement membrane matrix. Cultured microvascular endothelial cells therefore appear to deposit a basal lamina-like structure that is biochemically similar to that formed in vivo, providing a unique model system that should be useful for understanding microvascular basement membrane metabolism, especially as it relates to wound healing, tissue remodeling, and disease processes.
对从人真皮中分离出的培养微血管内皮细胞进行了检查,以检测基底膜特异性(IV型)胶原蛋白的合成及其在内皮下基质中的沉积。分泌到培养基中的经生物合成放射性标记的蛋白质在还原后通过十二烷基硫酸钠凝胶电泳进行分析,结果显示有一个单一的胶原蛋白成分,其近似分子量为180000,可分解为两条迁移紧密的多肽链。在还原之前,180000条带以高分子量复合物的形式迁移,表明存在分子间二硫键。基于其被纯化的细菌胶原酶选择性降解、对胃蛋白酶消化的中度敏感性、用人IV型胶原蛋白抗体进行免疫沉淀以及与从人和鼠源纯化的IV型前胶原共迁移,将180000的物质鉴定为IV型前胶原。在微血管内皮细胞在其基底表面形成的类似基底膜的基质中,IV型前胶原是主要成分。这种与基质相关的IV型前胶原以高度交联且不溶性的复合物形式存在,只有在二硫键变性和还原后才会溶解。此外,有证据表明存在IV型前胶原的不可还原二聚体和更高分子量的聚集体。这些发现支持了以下观点,即分子间二硫键和其他共价相互作用的存在稳定了IV型前胶原掺入基底膜基质的过程。因此,培养的微血管内皮细胞似乎沉积了一种在生化上与体内形成的结构相似的基底膜样结构,提供了一个独特的模型系统,这对于理解微血管基底膜代谢应该是有用的,特别是在涉及伤口愈合、组织重塑和疾病过程方面。