Murine neuroblastoma cells express ganglioside binding sites on their cell surface.
Murine neuroblastoma cells express ganglioside binding sites on their cell surface.
复制标题
鼠神经母细胞瘤细胞在其细胞表面表达神经节苷脂结合位点。
DOI：
10.1111/j.1471-4159.1990.tb01235.x
复制
发表时间：
1990
影响因子：
4.7
通讯作者：
Schengrund,CL
中科院分区：
文献类型：
--
作者：
Fueshko,SM;Schengrund,CL
研究了S20Y胆碱能和N115肾上腺素能小鼠神经母细胞瘤细胞对固定化神经节苷的粘附能力。与GM2、GD1a或GT1b包被的塑料孔相比，有活力的S20Y细胞在GM1包被的塑料孔上粘附更强。GM1的低聚糖部分抑制了S20Y细胞对GM1包被孔的粘附，表明GM1的碳水化合物部分具有识别位点。分析S20Y细胞对GM1衍生物包被的孔的粘附性表明，细胞不粘附于asialo‐GM1，并且对甲酯或去N‐乙酰基衍生物的粘附性显著降低。GM1结合位点在S20Y细胞中的表达似乎与密度有关；在融合期收获的细胞比在融合前收获的细胞贴壁更强。胰蛋白酶处理S20Y和N115细胞导致与GM1包被孔的结合丧失，这表明细胞表面GM1结合位点是一种蛋白质。相比之下，在与S20Y细胞相同的条件下，N115细胞对GM1、GD1a、GT1b、Gal‐Cer、asialo‐GM1或GM1甲酯包被孔的粘附性没有显著差异。N115细胞确实显示出对GM2包被孔的粘附减少，这表明它们识别了末端半乳糖部分。
The ability of S20Y cholinergic, and N115 adrenergic, murine neuroblastoma cells to adhere to immobilized gangliosides was studied. Viable S20Y cells adhered more strongly to GM1‐coated plastic wells than to those coated with GM2, GD1a, or GT1b. The oligosaccharide portion of GM1 inhibited adherence of S20Y cells to GM1‐coated wells, indicating that the carbohydrate moiety of GM1 bore the recognition site. Analysis of S20Y cell adherence to wells coated with derivatives of GM1 indicated that the cells did not adhere to asialo‐GM1 and adherence to the methyl ester or de‐N‐acetyl derivatives was significantly reduced. Expression of the GM1 binding sites by S20Y cells appears to be density dependent; cells harvested at the confluent stage of growth were more adherent than those harvested at the preconfluent stage. Trypsin treatment of the S20Y and N115 cells resulted in a loss of binding to GM1‐coated wells, suggesting that the cell surface GM1 binding site is a protein. In contrast, N115 cells showed no significant difference in their adherence to wells coated with GM1, GD1a, GT1b, Gal‐Cer, asialo‐GM1, or the methyl ester of GM1 when assayed under the same conditions as those imposed on the S20Y cells. The N115 cells did show a reduction in adherence to GM2‐coated wells, suggesting that they recognized the terminal galactosyl moiety.