Lesot H, Kubler M D, Fausser J L, Ruch J V
Institut de Biologie Médicale, INSERM CJF 88-08, Faculté de Médecine, Strasbourg, France.
Differentiation. 1990 Jul;44(1):25-35. doi: 10.1111/j.1432-0436.1990.tb00533.x.
Membrane-mediated matrix-microfilament interactions are involved in odontoblast differentiation. In this study, we analyzed the interactions of vinculin and fibronectin with plasma membrane proteins separated by sodium dodecyl sulphate (SDS) polyacrylamide gel electrophoresis, and then transferred onto polyvinylidene-difluoride (PVDF) paper. Vinculin was found to interact with 58, 63 and 165 kDa plasma membrane proteins. Fibronectin interacted with three high molecular weight (145, 165, and 185 kDa) membrane proteins. Attempts were made to characterize the 165 kDa protein which interacted with vinculin and with fibronectin. The interaction of the 165 kDa protein with fibronectin was not competitively inhibited by synthetic peptides such as GRGDS or GRGDSP, suggesting that the protein was not related to integrins. Antibodies directed against the 165 kDa protein allowed the identification of the precise localization and biological role of this membrane antigen. The data presented in this paper and previous observations indicate that the 165 kDa protein, involved in odontoblast elongation and polarization, mediates a fibronectin-vinculin transmembrane interaction.
膜介导的基质-微丝相互作用参与成牙本质细胞分化。在本研究中，我们分析了纽蛋白和纤连蛋白与经十二烷基硫酸钠（SDS）聚丙烯酰胺凝胶电泳分离后转移至聚偏二氟乙烯（PVDF）膜上的质膜蛋白之间的相互作用。发现纽蛋白与58、63和165 kDa的质膜蛋白相互作用。纤连蛋白与三种高分子量（145、165和185 kDa）的膜蛋白相互作用。我们试图对与纽蛋白和纤连蛋白相互作用的165 kDa蛋白进行表征。165 kDa蛋白与纤连蛋白的相互作用不受GRGDS或GRGDSP等合成肽的竞争性抑制，这表明该蛋白与整合素无关。针对165 kDa蛋白的抗体能够鉴定该膜抗原的精确定位和生物学作用。本文呈现的数据以及之前的观察结果表明，参与成牙本质细胞伸长和极化的165 kDa蛋白介导了一种纤连蛋白-纽蛋白跨膜相互作用。
