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利用二次谐波产生显微镜预测热诱导的胶原蛋白收缩

Prediction of heat-induced collagen shrinkage by use of second harmonic generation microscopy.

作者信息

Lin Sung-Jan, Lo Wen, Tan Hsin-Yuan, Chan Jung-Yi, Chen Wei-Liang, Wang Shiou-Han, Sun Yen, Lin Wei-Chou, Chen Jau-Shiuh, Hsu Chih-Jung, Tjiu Jeng-Wei, Yu Hsin-Su, Jee Shiou-Hwa, Dong Chen-Yuan

机构信息

National Taiwan University Hospital and College of Medicine, Department of Dermatology, Taipei.

出版信息

J Biomed Opt. 2006 May-Jun;11(3):34020. doi: 10.1117/1.2209959.

Abstract

Collagen shrinkage associated with denaturation from thermal treatment has a number of important clinical applications. However, individualized treatment is hindered by the lack of reliable noninvasive methods to monitor the process of collagen denaturation. We investigate the serial changes of collagen denaturation from thermal treatment of rat tail tendons at 58 degrees C by use of second harmonic generation (SHG) microscopy. We find that rat tail tendon shrinks progressively from 0 to 9 min of thermal treatment, and remains unchanged in length upon further thermal treatment. The SHG intensity also decreases from 0 to 9 min of thermal treatment and becomes barely detectable from further thermal treatment. Collagen shrinkage and the SHG intensity are well correlated in a linear model. In addition, SHG imaging reveals a tiger-tail-like pattern of collagen denaturation. The bands of denatured collagen progressively widen from increased thermal treatment and completely replace the adjacent bands of normal collagen after 9 min of thermal treatment. Our results show that collagen denaturation in rat tail tendon from thermal treatment is inhomogeneous, and that SHG intensity can be used to predict the degree of thermally induced collagen shrinkage. With additional development, this approach has the potential to be used in biomedical applications.

摘要

与热处理变性相关的胶原蛋白收缩具有许多重要的临床应用。然而,由于缺乏可靠的非侵入性方法来监测胶原蛋白变性过程,个体化治疗受到阻碍。我们使用二次谐波产生(SHG)显微镜研究了大鼠尾腱在58摄氏度热处理下胶原蛋白变性的系列变化。我们发现大鼠尾腱在热处理0至9分钟时逐渐收缩,进一步热处理后长度保持不变。SHG强度在热处理0至9分钟时也降低,进一步热处理后几乎检测不到。胶原蛋白收缩与SHG强度在线性模型中具有良好的相关性。此外,SHG成像揭示了一种虎尾状的胶原蛋白变性模式。变性胶原蛋白带随着热处理增加而逐渐变宽,热处理9分钟后完全取代相邻的正常胶原蛋白带。我们的结果表明热处理导致的大鼠尾腱胶原蛋白变性是不均匀的,并且SHG强度可用于预测热诱导的胶原蛋白收缩程度。随着进一步发展,这种方法有可能用于生物医学应用。

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