Behnke O
Institute of Anatomy, Panum Institute, Copenhagen, Denmark.
Thromb Haemost. 1987 Aug 4;58(2):786-9.
Adhesion of rat blood platelets to native rat tail collagen fibrils was studied in the electron microscope under conditions that preserved collagen-associated proteoglycans (CAPG). The CAPG molecules were aligned in chain-like configurations that encircled the fibrils with a 65 nm period; they appeared to coat the fibrils completely and extended 60-100 nm away from the fibril. The initial platelet-fibril contact occurred between the platelet glycocalyx and the CAPG of the fibrils i.e. between two surfaces with net-negative charges. When close contact was established between the fibril surface proper and the platelet membrane, CAPG were not identified in the area of contact, and the collagen-platelet distance was reduced to a approximately 10-12 nm wide gap traversed by delicate links in register with fibril periodicities.
在保留胶原相关蛋白聚糖（CAPG）的条件下，利用电子显微镜研究了大鼠血小板与天然大鼠尾胶原纤维的黏附情况。CAPG分子呈链状排列，以65纳米的周期环绕纤维；它们似乎完全覆盖了纤维，并从纤维向外延伸60 - 100纳米。血小板与纤维的初始接触发生在血小板糖萼与纤维的CAPG之间，即两个带净负电荷的表面之间。当纤维表面本身与血小板膜建立紧密接触时，在接触区域未发现CAPG，胶原与血小板之间的距离缩小至约10 - 12纳米宽的间隙，间隙中有与纤维周期对齐的精细连接。
