K Kayser, S André, N V Bovin, F Y Zeng, H J Gabius
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Several probes with assumed relevance were tested with the panel of specimens for both groups, focussing on comparative analysis of alveolar lining cells. In addition to labelled neoglycoconjugates which include tissue lectin-seeking probes that expose mono-, di- and blood group-related trisaccharides, presence of calcium- and annexin-binding calcyclin, of complement component C5b, of the lymphokine macrophage migration inhibitory factor, and of ligands of the serum amyloid P component was evaluated. Compared to normal cells at the alveolar surface in controls, the preneoplastic cells displayed an apparent down-regulation of expression of A/H-trisaccharide-specific binding sites and an upregulation of expression of calcyclin. These three characteristics correlated with the phenotypic alterations and encourage further studies to elucidate the functional significance of reduced expression of the glycoligand-specific sites and the presence of this member of the S100-family of Ca(2+)-binding proteins.</p>","PeriodicalId":9552,"journal":{"name":"Cancer biochemistry biophysics","volume":"15 4","pages":"235-43"},"PeriodicalIF":0.0000,"publicationDate":"1997-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Preneoplasia-associated expression of calcyclin and of binding sites for synthetic blood group A/H trisaccharide--exposing neoglycoconjugates in human lung.\",\"authors\":\"K Kayser, S André, N V Bovin, F Y Zeng, H J Gabius\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Development of preneoplastic lesions in human lung is supposed to be accompanied with alterations of distinct biochemical features which might functionally be crucial for this alteration. 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引用次数: 0
摘要
人肺肿瘤前病变的发展被认为伴随着不同生化特征的改变,这可能在功能上对这种改变至关重要。为了帮助确定周围肺实质中的这些决定因素,我们对Thoraxklinik病理学部门的文件(共2890例)进行了相应的组织标本筛选。71例有完整的临床记录,并组成年龄、性别、疾病相匹配的对照组。与对照组患者相比,特别是肿瘤前异常的无肿瘤患者显示有外部毒物暴露史。用两组的标本面板测试了几种假定相关的探针,重点是肺泡衬里细胞的比较分析。除了标记的新糖缀合物(包括暴露单糖、二糖和血型相关的三糖的组织凝集素寻找探针)外,还评估了钙和膜联蛋白结合的钙调素、补体成分C5b、淋巴因子巨噬细胞迁移抑制因子以及血清淀粉样蛋白P成分配体的存在。与对照组肺泡表面的正常细胞相比,肿瘤前细胞表现出明显的A/ h -三糖特异性结合位点表达下调和钙调素表达上调。这三个特征与表型改变相关,并鼓励进一步研究阐明糖配体特异性位点表达减少和Ca(2+)结合蛋白s100家族成员存在的功能意义。
Preneoplasia-associated expression of calcyclin and of binding sites for synthetic blood group A/H trisaccharide--exposing neoglycoconjugates in human lung.
Development of preneoplastic lesions in human lung is supposed to be accompanied with alterations of distinct biochemical features which might functionally be crucial for this alteration. To contribute to the definition of such determinants in peripheral lung parenchyma, the files of the Department of Pathology, Thoraxklinik, (a total of 2890 cases) were screened for respective tissue specimens. Seventy one cases with complete clinical documentation were found and an age-, sex-, and disease-matched control group was formed. When compared to control group patients, especially the tumor free cases with preneoplastic aberrations revealed a history of exposure to external noxes. Several probes with assumed relevance were tested with the panel of specimens for both groups, focussing on comparative analysis of alveolar lining cells. In addition to labelled neoglycoconjugates which include tissue lectin-seeking probes that expose mono-, di- and blood group-related trisaccharides, presence of calcium- and annexin-binding calcyclin, of complement component C5b, of the lymphokine macrophage migration inhibitory factor, and of ligands of the serum amyloid P component was evaluated. Compared to normal cells at the alveolar surface in controls, the preneoplastic cells displayed an apparent down-regulation of expression of A/H-trisaccharide-specific binding sites and an upregulation of expression of calcyclin. These three characteristics correlated with the phenotypic alterations and encourage further studies to elucidate the functional significance of reduced expression of the glycoligand-specific sites and the presence of this member of the S100-family of Ca(2+)-binding proteins.