Agemura D H, O'Brien W D, Olerud J E, Chun L E, Eyre D E
Department of Electrical and Computer Engineering, University of Illinois, Urbana 61801.
J Acoust Soc Am. 1990 Apr;87(4):1786-91. doi: 10.1121/1.399427.
A pilot study on articular cartilage assessed the contributions of individual matrix components to ultrasound propagation. The influence of collagen fibril orientation and collagen cross linking was also assessed. Sections of adult bovine articular cartilage cut both parallel and perpendicular to the articular surface were examined using the scanning laser acoustic microscope (SLAM) operating at an ultrasonic frequency of 100 MHz. A set of samples was evaluated that had been sequentially treated by enzymes to (1) remove 85% of the chondroitin sulfate; (2) remove remaining glycosaminoglycans, glycoproteins, and other noncollagen proteins, leaving only the collagen fibril network; and (3) disrupt the collagen intermolecular cross links. Two striking observations were made: a profound effect of the "preferred" collagen fibril orientation on ultrasonic speed and a marked increase in attenuation coefficient when intermolecular cross links were broken in the collagen.
一项关于关节软骨的初步研究评估了单个基质成分对超声传播的贡献。同时也评估了胶原纤维取向和胶原交联的影响。使用工作频率为100MHz的扫描激光声学显微镜（SLAM）对成年牛关节软骨平行和垂直于关节表面切割的切片进行检查。评估了一组依次用酶处理过的样本，处理方式如下：（1）去除85%的硫酸软骨素；（2）去除剩余的糖胺聚糖、糖蛋白和其他非胶原蛋白，仅留下胶原纤维网络；（3）破坏胶原分子间交联。有两个显著发现：“优先”的胶原纤维取向对超声速度有深远影响，并且当胶原中的分子间交联被破坏时，衰减系数显著增加。
