Stallmach A, Riecken E O
Klinikum Steglitz, Medizinische Klinik und Poliklinik, Freie Universität Berlin.
Digestion. 1990;46 Suppl 2:31-9. doi: 10.1159/000200364.
The regulation of cell proliferation, migration and differentiation under physiological conditions and in adaptational patterns is still not well understood. The interaction of intestinal epithelial cells with the basement membrane may influence cell adhesion and migration. One potential mechanism involves cell surface binding proteins, which induce the biological response when occupied by the basement membrane component. Immunoblotting experiments on isolated epithelial cell membranes from the normal duodenum of adult rats using specific antibodies revealed major laminin-binding cell membrane components with an Mr of 66-69 kD, similar to the putative laminin receptor described for other tissues. The specific interaction between these cell membrane binding proteins and the proteolytic fragment laminin P1 originating from the central core of the laminin molecule could be further demonstrated by slot blot assays. Immunohistological examinations of normal small intestinal mucosa revealed that the 67-kD laminin-binding proteins were present on the basolateral cell surfaces of epithelial cells lining the base of the crypt of Lieberkühn, but were absent from cells lining the mouth of the crypts or the villi.
在生理条件下以及适应性模式中,细胞增殖、迁移和分化的调控仍未被充分理解。肠上皮细胞与基底膜的相互作用可能会影响细胞黏附和迁移。一种潜在机制涉及细胞表面结合蛋白,当被基底膜成分占据时,这些蛋白会诱导生物学反应。使用特异性抗体对成年大鼠正常十二指肠分离的上皮细胞膜进行免疫印迹实验,结果显示主要的层粘连蛋白结合细胞膜成分的分子量为66 - 69 kD,这与其他组织中描述的假定层粘连蛋白受体相似。通过狭缝印迹分析可以进一步证明这些细胞膜结合蛋白与源自层粘连蛋白分子中央核心的蛋白水解片段层粘连蛋白P1之间的特异性相互作用。对正常小肠黏膜的免疫组织学检查显示,67-kD层粘连蛋白结合蛋白存在于利伯kühn隐窝底部上皮细胞的基底外侧细胞表面,但在隐窝口或绒毛处的细胞中不存在。