Rosenblatt H M, Parikh N, McClure J E, Meza I, Hwo S Y, Bryan J, Shearer W T
J Immunol. 1985 Aug;135(2):995-1000.
Monoclonal antibodies (IgM kappa) have been produced to actin isolated electrophoretically from L cell extracts. These monoclonal anti-actin antibodies bind to intact L cells and modulate DNA synthesis and cell proliferation, much like affinity-purified polyclonal rabbit antibody to the same Mr 42,000 actin. In addition, monoclonal antibodies specific for actin from Entamoeba histolytica also bound to and modulated the growth of L cells. A monoclonal antibody directed against a neuroblastoma surface antigen did not produce stimulation of L cells, and the binding activity of anti-actin monoclonal antibody to L cells was removed by absorption with actin covalently coupled to Sepharose. These observations demonstrate the specificity of interaction between the anti-actin monoclonal antibodies and the surface of intact L cells. We conclude that a surface actin-like molecule on the L cell, when bound by specific monoclonal antibody, initiates a stimulatory signal which results in enhanced cellular metabolism.
已制备出针对从L细胞提取物中通过电泳分离得到的肌动蛋白的单克隆抗体(IgM κ)。这些单克隆抗肌动蛋白抗体与完整的L细胞结合,并调节DNA合成和细胞增殖,这与针对相同分子量42,000的肌动蛋白的亲和纯化多克隆兔抗体非常相似。此外,针对溶组织内阿米巴肌动蛋白的特异性单克隆抗体也能与L细胞结合并调节其生长。一种针对神经母细胞瘤表面抗原的单克隆抗体不会刺激L细胞,并且抗肌动蛋白单克隆抗体与L细胞的结合活性可通过与共价偶联到琼脂糖凝胶上的肌动蛋白吸附而去除。这些观察结果证明了抗肌动蛋白单克隆抗体与完整L细胞表面之间相互作用的特异性。我们得出结论:L细胞表面的一种肌动蛋白样分子在被特异性单克隆抗体结合时,会引发一个刺激信号,导致细胞代谢增强。