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Molecular and Morphological Adaptations in Compressed Articular Cartilage by Polarized Light Microscopy and Fourier-Transform Infrared Imaging

机译：偏振光显微镜和傅立叶变换红外成像在关节软骨压缩中的分子和形态学适应

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Fifteen articular cartilage-bone specimens from one canine humeral joint were compressed in the strain range of 0% to 50%. The deformation of the extracellular matrices in cartilage was preserved and the same tissue sections were studied using polarized light microscopy (PLM) and Fourier-transform infrared imaging (FTIRI). The PLM results show that the most significant changes in the apparent zone thickness due to ‘re-organization’ of the collagen fibrils based on the birefringence occur between 0% to 20% strain values, where the increase in the superficial zone and decrease in the radial zone thicknesses are approximately linear with the applied strain. The FTIRI anisotropy results show that the two amide components with bond direction perpendicular to the external compression retain anisotropy (amide II in the superficial zone and amide I in the radial zone). In contrast, the measured anisotropy from the two amide components with bond direction parallel to the external compression change their anisotropy significantly (amide I in the superficial zone and amide II in the radial zone). Statistical analysis shows that there is an excellent correlation (r=0.98) between the relative depth of the minimum retardance in PLM and the relative depth of the Amide II anisotropic cross-over. The changes in amide anisotropies in different histological zones are explained by the strain-dependent tipping angle of the amide bonds. These depth-dependent adaptations to static loading in cartilage’s morphological structure and chemical distribution could be useful in the future studies of the early diseased cartilage.
机译：在0％至50％的应变范围内压缩来自15个犬肱关节的15个关节软骨骨标本。保留了软骨中细胞外基质的变形，并使用偏振光显微镜（PLM）和傅立叶变换红外成像（FTIRI）研究了相同的组织切片。 PLM结果表明，基于双折射的胶原纤维的“重新组织”导致表观区域厚度的最显着变化发生在0％至20％的应变值之间，其中表层区域的增大和表面区域的减小。径向区域的厚度与所施加的应变大致成线性关系。 FTIRI各向异性结果表明，键方向垂直于外部压缩的两个酰胺组分均保持各向异性（表层区域为酰胺II，径向区域为酰胺I）。相反，从具有平行于外部压缩的键方向的两个酰胺组分测得的各向异性将显着改变其各向异性（浅层区域为酰胺I，径向区域为酰胺II）。统计分析表明，PLM中最小延迟的相对深度与Amide II各向异性交叉的相对深度之间存在极好的相关性（r = 0.98）。在不同的组织学区域，酰胺各向异性的变化是由酰胺键的应变依赖性倾角来解释的。这些对软骨形态结构和化学分布的静态负荷的深度依赖性适应可能在将来对早期患软骨的研究中很有用。

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