小鼠Lewis肺癌组织中糖肽的分离纯化及其对肿瘤细胞与层粘连蛋白基质粘着的影响

Isolation of Clycopeptides from Murine Lewis Lung Carcinoma and their Roles in the recognition and attachment of tumor cells to Laminin Substrate

小鼠Lewis肺癌组织经氯仿甲醇去除脂类,用木瓜蛋白酶消化,再经Sephadex柱层析分离得到总糖肽。它有明显地抑制小鼠Lewis肺癌细胞,S180肉瘤细胞及人巨细胞肺癌细胞与层粘连蛋白(Laminin,LN)基质粘着的作用;对层粘连蛋白受体(LN-R)与其配体的识别及结合也具有同样明显的阻断效应。糖肽的上述作用均具有剂量依赖性。进一步经ConA-Sepharose CL-4B亲和层析将总糖肽分为三个部分。与ConA不结合的糖肽部分对Lewis肺癌细胞与LN基质的粘着也具有剂量性抑制作用。

Clycopeptides were isolated from murine Lewis lung carcinoma by papain digestion and on Sephadex column chromatograghy.The recognition and attachment of murine Lewis lung carcinoma cells, mouse S180-V sarcoma cells and human pulmonary giant carcinoma cells to laminin substrate were markedly inhibited by the glycopeptides. The glycopeptides also obviously inhibited the attachment of the isolated laminin receptor to immobilized laminin. All the inhibitory effects were dose-dependent. The glycopeptides were fractionated into three fractions on Con A-Sepharose CL-4B affinity chromatography column. Most of the glycopeptides appeared in unbound fraction, which showed dose-dependent inhibitory activity to the attachment of Lewis lung carcinoma cells to laminiu substrate.