Lwebuga-Mukasa J S, Madri J A, Albert J, Furthmayr H
Coll Relat Res. 1984 Mar;4(2):95-110. doi: 10.1016/s0174-173x(84)80018-7.
Fibronectin is a ubiquitous glycoprotein found in plasma, on the surface of a number of cell types and in the extracellular matrix. It is believed to function as an adhesive protein for cells by mediating their interaction with connective tissue macromolecules. This study uses the rotary shadowing technique to investigate the interaction between human plasma fibronectin and native calf skin type I collagen molecules. Purified human plasma fibronectin appears fibrillar with a total length of 152 +/- 48 nm (n = 127). Individual molecules of fibronectin interact with one another in an apparent concentration dependent process to form linear polymeric structures up to 10 molecules by end-to-end association. Incubation of various concentrations of fibronectin with collagen results in the interaction of fibronectin with specific sites on the native collagen molecules. In addition, polymeric forms of fibronectin interact with collagen molecules and occasionally bridging structures between collagen molecules are formed. This study provides direct visual demonstration of an interaction between fibronectin and native collagen molecules. Possible physiologic implications of these observations are discussed.
纤连蛋白是一种广泛存在的糖蛋白，存在于血浆中、多种细胞类型的表面以及细胞外基质中。它被认为通过介导细胞与结缔组织大分子的相互作用，起到细胞黏附蛋白的作用。本研究采用旋转阴影技术，研究人血浆纤连蛋白与天然小牛皮肤I型胶原分子之间的相互作用。纯化的人血浆纤连蛋白呈纤维状，总长度为152±48nm（n = 127）。纤连蛋白的单个分子以明显的浓度依赖性过程相互作用，通过端对端结合形成多达10个分子的线性聚合物结构。将不同浓度的纤连蛋白与胶原一起孵育，会导致纤连蛋白与天然胶原分子上的特定位点相互作用。此外，纤连蛋白的聚合物形式与胶原分子相互作用，偶尔会在胶原分子之间形成桥接结构。本研究提供了纤连蛋白与天然胶原分子之间相互作用的直接可视化证据。讨论了这些观察结果可能的生理意义。
