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由凝集素苹果蜗牛凝集素(HPA)识别的转移性结肠癌细胞的蛋白质组分析。

Proteome analysis of metastatic colorectal cancer cells recognized by the lectin Helix pomatia agglutinin (HPA).

作者信息

Saint-Guirons Julien, Zeqiraj Elton, Schumacher Udo, Greenwell Pamela, Dwek Miriam

机构信息

School of Biosciences, University of Westminster, London, UK.

出版信息

Proteomics. 2007 Nov;7(22):4082-9. doi: 10.1002/pmic.200700434.

Abstract

The lectin from Helix pomatia (HPA) binds to adenocarcinomas with a metastatic phenotype but the glycoconjugates of cancer cells that bind to the lectin have yet to be characterized in detail. We used a model of metastatic (HT29) and nonmetastatic (SW480) human colorectal cancer cells and a proteomic approach to identify HPA binding glycoproteins. Cell membrane proteins purified by HPA affinity chromatography, were separated by 2-DE and analyzed by MS. Competitive inhibition experiments with N-acetylgalactosamine, N-acetylglucosamine, and sialic acid confirmed that HPA binding was via a glycan-mediated interaction. Western blot analysis showed that HPA binds to proteins not recognized by an antibody against blood group A epitope. The proteomic study showed the main HPA binding partners include integrin alphav/alpha6 and annexin A2/A4. These proteins were found complexed with microfilament proteins alpha and beta tubulin, actin, and cytokeratins 8 and 18. HPA also bound to Hsp70, Hsp90, TRAP-1, and tumor rejection factor 1. This study revealed that the prognostic utility of HPA lies in its ability to bind simultaneously to many glycoproteins involved in cell migration and signaling, in addition, the proteins recognized by HPA are glycosylated with structures distinct from the blood group A epitope.

摘要

来自苹果螺(HPA)的凝集素可与具有转移表型的腺癌结合,但与该凝集素结合的癌细胞糖缀合物尚未得到详细表征。我们使用转移性(HT29)和非转移性(SW480)人结肠癌细胞模型以及蛋白质组学方法来鉴定HPA结合糖蛋白。通过HPA亲和色谱纯化的细胞膜蛋白经二维电泳分离并进行质谱分析。用N-乙酰半乳糖胺、N-乙酰葡糖胺和唾液酸进行的竞争性抑制实验证实,HPA结合是通过聚糖介导的相互作用。蛋白质印迹分析表明,HPA与抗A血型表位抗体无法识别的蛋白质结合。蛋白质组学研究表明,HPA的主要结合伙伴包括整合素αv/α6和膜联蛋白A2/A4。发现这些蛋白质与微丝蛋白α和β微管蛋白、肌动蛋白以及细胞角蛋白8和18形成复合物。HPA还与热休克蛋白70、热休克蛋白90、TRAP-1和肿瘤排斥因子1结合。这项研究表明,HPA的预后效用在于其能够同时与许多参与细胞迁移和信号传导的糖蛋白结合,此外,HPA识别的蛋白质被糖基化,其结构不同于A血型表位。

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