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首页> 外文期刊>Journal of Structural Biology >Molecular and morphological adaptations in compressed articular cartilage by polarized light microscopy and Fourier-transform infrared imaging.
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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压缩性关节软骨中的分子和形态学适应。

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摘要

Fifteen articular cartilage-bone specimens from one canine humeral joint were compressed in the strain range of 0-50%. 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 'reorganization' of the collagen fibrils based on the birefringence occur between 0% and 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 changes 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0-50%的应变范围内压缩15个来自一只犬肱关节的关节软骨-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“重组”导致表观区域厚度的最显着变化发生在0%到20%应变值之间,其中表层区域增加而径向区域减少厚度与所施加的应变近似线性。 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酰胺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会在将来对早期患病软骨的研究中有用。

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