Schmidhauser C, Dudler R, Schmidt T, Parish R W
Institut für Pflanzenbiologie, Universität Zürich, Switzerland.
J Cell Sci. 1990 Mar;95 ( Pt 3):499-506. doi: 10.1242/jcs.95.3.499.
Fab fragments of a monoclonal antibody directed against p37, a protein associated with the surface of FS9 mouse sarcoma cells, were previously found to inhibit the highly invasive behaviour of FS9 cells in vitro. We show that p37 originates from Mycoplasma hyorhinis. Infecting various cell lines with the mycoplasma consistently increased their invasiveness when confronted with chicken heart fibroblasts using Abercrombie's confronted explant technique. Conversely, removing the mycoplasmas or blocking p37 with specific Fab fragments reduced invasiveness. Analysis of individual cell collisions using time-lapse filming showed that the addition of Fab fragments to cells infected with M. hyorhinis greatly increased the level of contact inhibition. The antibody also reduced the invasiveness of transformed cells that did not express the p37 antigen. Hence, a cellular protein or proteins that are structurally related to p37 apparently influence invasive behavior.
先前发现,一种针对p37的单克隆抗体的Fab片段可抑制FS9小鼠肉瘤细胞表面相关蛋白p37的高侵袭行为。我们发现p37源自猪鼻支原体。使用阿伯克龙比对置外植体技术,用该支原体感染各种细胞系,当与鸡心脏成纤维细胞对置时,其侵袭性持续增加。相反,去除支原体或用特异性Fab片段阻断p37可降低侵袭性。使用延时摄影对单个细胞碰撞进行分析表明,向感染猪鼻支原体的细胞中添加Fab片段可大大提高接触抑制水平。该抗体还降低了不表达p37抗原的转化细胞的侵袭性。因此,一种或多种与p37结构相关的细胞蛋白显然会影响侵袭行为。