Schwartz E, Goldfischer S, Coltoff-Schiller B, Blumenfeld O O
J Histochem Cytochem. 1985 Apr;33(4):268-74. doi: 10.1177/33.4.3980980.
Extracellular proteins of cultured calf aortic smooth muscle cells consist predominantly of microfibrils 10-20 nm in diameter typical of "elastin-associated" microfibrils described in many tissues. Chemical and immunochemical evidence is presented that microfibrils consist of at least two proteins: core protein and fibronectin. Insoluble proteins of the microfibrils were obtained in the form of a pellet and antibodies raised in rabbits against these components. The antisera reacted with the insoluble microfibrillar proteins and with soluble fibronectin in enzyme-linked immunosorbent assay, and immunostained the extracellular microfibrils in cultured cells. An immunoglobulin (Ig) fraction was prepared and absorbed with fibronectin. The absorbed IgG retained its reactivity with the microfibrillar proteins but was no longer reactive with soluble fibronectin. Immunofluorescence studies were carried out using the absorbed IgG and IgG to soluble fibronectin. Both antibodies showed immunoreactive microfibrils in the extracellular matrix of cells in log phase. However, with increasing time in culture, as the cells reached confluence, the immunofluorescence of microfibrils reacting with the absorbed IgG became less intense, whereas that of microfibrils reacting with IgG to fibronectin increased; in confluent cells, essentially no staining was detected with the absorbed IgG, and a dense network of intensely stained microfibrils was seen with IgG to fibronectin. Treatment of these cultures with urea led to partial dissociation of the fibronectin and increased visualization of the microfibrils with the absorbed IgG; double-label immunofluorescence showed that both proteins occurred on the same microfibrils. The localization of immunoreactive sites to the extracellular microfibrils was confirmed by immunoelectron microscopy. Nearly quantitative cleavage with CNBr failed to dissociate the antigenically active fragments of fibronectin from the CNBr fragments of the core proteins of the microfibrils. It was concluded that microfibrils contain core proteins and fibronectin that are codistributed in insoluble, possibly covalently cross-linked, aggregates. The core proteins are first deposited by the cell and, as a function of time in culture, fibronectin gradually coats their surface.
培养的小牛主动脉平滑肌细胞的细胞外蛋白主要由直径为10 - 20纳米的微原纤维组成,这是许多组织中描述的典型的“弹性蛋白相关”微原纤维。本文提供了化学和免疫化学证据,表明微原纤维至少由两种蛋白质组成:核心蛋白和纤连蛋白。微原纤维的不溶性蛋白以沉淀形式获得,并以此制备兔抗这些成分的抗体。在酶联免疫吸附测定中,抗血清与不溶性微原纤维蛋白以及可溶性纤连蛋白发生反应,并对培养细胞中的细胞外微原纤维进行免疫染色。制备了免疫球蛋白(Ig)组分并用纤连蛋白吸收。吸收后的IgG保留了其与微原纤维蛋白的反应性,但不再与可溶性纤连蛋白反应。使用吸收后的IgG和针对可溶性纤连蛋白的IgG进行免疫荧光研究。两种抗体在对数期细胞的细胞外基质中均显示出免疫反应性微原纤维。然而,随着培养时间的增加,当细胞达到汇合状态时,与吸收后的IgG反应的微原纤维的免疫荧光强度减弱,而与针对纤连蛋白的IgG反应的微原纤维的免疫荧光强度增加;在汇合细胞中,用吸收后的IgG基本上检测不到染色,而用针对纤连蛋白的IgG则可见密集染色的微原纤维网络。用尿素处理这些培养物导致纤连蛋白部分解离,并增加了吸收后的IgG对微原纤维的可视化;双重标记免疫荧光显示两种蛋白质存在于同一微原纤维上。免疫电子显微镜证实了免疫反应位点在细胞外微原纤维上的定位。用溴化氰进行几乎定量的切割未能使纤连蛋白的抗原活性片段与微原纤维核心蛋白的溴化氰片段解离。得出的结论是,微原纤维含有核心蛋白和纤连蛋白,它们共分布于不溶性的、可能是共价交联的聚集体中。核心蛋白首先由细胞沉积,并且随着培养时间的推移,纤连蛋白逐渐覆盖其表面。