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Mass spectrometry based identification of galectin-3 interacting proteins potentially involved in lung melanoma metastasis
Molecular BioSystems Pub Date : 2017-08-25 00:00:00 , DOI: 10.1039/c7mb00260b
Manohar C. Dange 1, 2, 3, 4 , Hemangi S. Bhonsle 1, 2, 3, 4, 5 , Rashmi K. Godbole 4, 5, 6, 7, 8 , Shyam K. More 1, 2, 3, 4 , Sanjay M. Bane 1, 2, 3, 4 , Mahesh J. Kulkarni 4, 5, 6, 7, 8 , Rajiv D. Kalraiya 1, 2, 3, 4
Affiliation  

Adhesive interactions between molecules on tumor cells and those on target organs play a key role in organ specific metastasis. Poly-N-acetyl-lactosamine (polyLacNAc) substituted N-oligosaccharides on melanoma cell surface glycoproteins promote lung specific metastasis via galectin-3 by facilitating their arrest and extravasation. This study reports the identification and characterization of galectin-3 interacting proteins using a combination of galectin-3 sepharose affinity and leucoagglutinating phytohemagglutinin (L-PHA) columns. A total of 83 proteins were identified as galectin-3 interacting glycoproteins, of which 35 were constituents of the L-PHA bound fraction, suggesting that these proteins carry polyLacNAc substituted β1,6 branched N-glycans. The identities of some of these proteins, like LAMP-1, LAMP-3, basigin, embigin, and α5 and β1 Integrin, have been confirmed by western blotting, and functional relevance with respect to metastatic properties has been established.

中文翻译:

基于质谱的鉴定可能与肺黑色素瘤转移有关的半乳糖凝集素-3相互作用蛋白

肿瘤细胞上的分子与靶器官上的分子之间的粘附相互作用在器官特异性转移中起关键作用。聚Ñ取代的乙酰基-乳糖胺(polyLacNAc)ñ对黑色素瘤细胞表面糖蛋白-oligosaccharides促进肺特定转移通过galectin-3通过促进其阻滞和外渗。这项研究报告了结合使用galectin-3琼脂糖亲和力和leucoagglutating植物血凝素(L-PHA)柱的结合鉴定和鉴定galectin-3相互作用蛋白。鉴定出总共有83种蛋白质是与半乳凝素3相互作用的糖蛋白,其中35种是L-PHA结合级分的组成部分,表明这些蛋白质带有多聚LacNAc取代的β1,6支链N-聚糖。这些蛋白质中的一些,例如LAMP-1,LAMP-3,basigin,embigin以及α5和β1整联蛋白的身份已通过Western印迹得到了证实,并且已经建立了与转移特性的功能相关性。
更新日期:2017-10-25
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