乳腺癌组织中蛋白质二级结构的Fourier变换红外光谱研究

FTIR Assessment of the Secondary Structure of Proteins in Human Breast Carcinoma Tissues

根据乳腺大汗腺癌、小管癌、黏液癌、浸润导管癌、单纯癌和髓样癌组织 Fourier变换红外光谱酰胺 I带的去卷积和拟合分析 ,获得组织中蛋白质二级结构的数目及其组成。结果表明 :这些组织中蛋白质二级结构的数目及其组成存在着显著的差异 ,并与组织的类型、分化、坏死等密切相关。其中 ,髓样癌的差异性最大 ;高分化癌中螺旋结构的含量及非典型螺旋和 α-螺旋含量的比值均比低分化癌的相应值高 ;肿瘤边缘坏死的乳腺癌组织也表现出明显的差异。乳腺癌组织蛋白质二级结构的分析对乳腺癌组织的表征和评价具有重要的意义。

Considerable different compositions of the secondary structure of protein, determined by curve fitting analysis of the amide I bands in the FTIR spectra, are found among human breast apocrine, tubular, mucinous, invasive infiltrating ductal, simplex and medullary carcinoma tissues. Among those tissues, medullary carcinoma tissue appears extremely difference, well differentiated carcinomas have higher proportions of helices, and higher ratios between the proportions of atypical helix and α helix than poorly differentiated carcinomas; obvious compositional differences are also observed between carcinoma with and without tumor necrosis. The secondary structures of proteins may have important implication for characterizing and evaluating breast carcinoma tissues.