University of Wisconsin-Madison, Department of Biomedical Engineering, Madison, Wisconsin, United States.
University of Wisconsin-Madison, Laboratory for Optical and Computational Instrumentation, Madison,, United States.
J Biomed Opt. 2018 Jun;23(6):1-8. doi: 10.1117/1.JBO.23.6.066501.
Remodeling of the extracellular matrix in human ovarian cancer can be manifested in increased collagen concentration, changes in alignment within fibrils/fibers and/or up-regulation of different collagen isoforms. We used pixel-based second harmonic generation (SHG) polarization microscopy analyses to probe these molecular changes in human ovarian tissues [normal stroma, benign tumors, and high-grade serous (HGS) tumors] by: (i) determination of the α-helical pitch angle via the single-axis molecular model, (ii) collagen alignment within fibrils via SHG anisotropy, and (iii) chirality via SHG circular dichroism (SHG-CD). Pixel approaches are required due to the complex structure of the matrix that lacks a high degree of fiber alignment. The largest differences in the helical pitch angle were between normal stroma and benign tumors, consistent with gene expression showing the Col III isoform is up-regulated in the latter. The data were not consistent with up-regulation of Col III in HGS tumors as previous reports have suggested. The different tissues also displayed differing SHG anisotropies and SHG-CD responses, consistent with either Col III incorporation or randomization of Col I alignment within benign and malignant tumors. Additionally, the high-grade tumors displayed higher collagen concentration, where this desmoplasia is consistent with the higher fiber density in these tissues. These results collectively indicate that the fibril assemblies are distinct in all tissues, where these differences likely result from the synthesis of collagen rather than remodeling of existing collagen. Importantly, these analyses are label-free and interrogate subresolution collagen structure on intact tissues, without the need for conventional structural biology tools.
人卵巢癌细胞外基质的重塑可表现为胶原蛋白浓度增加、纤维内原纤维排列的改变和/或不同胶原蛋白亚型的上调。我们使用基于像素的二次谐波产生(SHG)偏振显微镜分析,通过以下方法来探测人卵巢组织[正常基质、良性肿瘤和高级别浆液性(HGS)肿瘤]中的这些分子变化:(i)通过单轴分子模型确定α螺旋螺距角,(ii)通过 SHG 各向异性探测纤维内的胶原蛋白排列,(iii)通过 SHG 圆二色性(SHG-CD)探测手性。由于基质的复杂结构缺乏高度纤维排列,因此需要采用像素方法。正常基质和良性肿瘤之间的螺旋螺距角差异最大,与基因表达一致,表明后者中 Col III 亚型上调。数据与 HGS 肿瘤中 Col III 上调不一致,因为之前的报道表明了这一点。不同的组织还显示出不同的 SHG 各向异性和 SHG-CD 反应,这与 Col III 的掺入或良性和恶性肿瘤中 Col I 排列的随机化一致。此外,高级别肿瘤显示出更高的胶原蛋白浓度,这种纤维增生与这些组织中更高的纤维密度一致。这些结果共同表明,所有组织中的纤维组装都不同,这些差异可能是由于胶原蛋白的合成而不是对现有胶原蛋白的重塑所致。重要的是,这些分析是无标记的,并在完整组织上探测亚分辨率的胶原蛋白结构,而无需传统的结构生物学工具。