Exogenous glycosphingolipids suppress growth rate of transformed and untransformed 3T3 mouse cells.
Exogenous glycosphingolipids suppress growth rate of transformed and untransformed 3T3 mouse cells.
复制标题
外源鞘糖脂抑制转化和未转化的 3T3 小鼠细胞的生长速率。
DOI：
10.1016/0014-4827(75)90379-1
复制
发表时间：
1975
影响因子：
3.7
通讯作者：
H. Wiegandt
中科院分区：
文献类型：
--
作者：
T. W. Keenan;E. Schmid;Werner W. Franke;H. Wiegandt
在培养基中添加神经节苷类物质降低了转化和未转化sv40病毒的3T3细胞的生长速度和饱和密度。单胞脂苷比双胞脂苷更有效地抑制生长速率。这些神经节苷对单个细胞几乎没有或没有造成细胞损伤或显著的形态改变。三棱脂苷显著降低生长速率，但在一些实验中也引起细胞损伤和裂解。分离的神经节苷脂GGtet1的碳水化合物部分，唾液寡糖半乳糖酰氨基- n -乙酰-半乳糖胺基-（n -乙酰神经胺基）-半乳糖葡萄糖，在培养中不抑制SV40 3T3细胞的生长。神经酰胺单独作为生长抑制剂也是无效的。然而，由上述神经节苷脂衍生的四己糖基神经酰胺在延缓SV40 3T3细胞生长方面与母体化合物同样有效。同样，单、二、三己基神经酰胺也能有效抑制这些细胞的生长。添加到培养基中的神经节苷脂被细胞迅速积累，显然在质膜上。积累的神经节苷脂不被细胞降解。然而，积累的神经节苷脂可以与体内合成的神经节苷脂区分开来，因为前者对神经氨酸酶的不稳定性。
Gangliosides added to culture media reduced both the growth rate and saturation density of SV40-virus transformed and untransformed 3T3 cells. Monosialogangliosides were much more effective than disialogangliosides in inhibiting growth rate. These gangliosides caused little or no cell damage or significant morphological alteration of the individual cells. Trisialoganglioside markedly reduced growth rate but in some experiments also caused cell damage and lysis. The isolated carbohydrate moiety of the ganglioside GGtet1, the sialo-oligosaccharide galactopyranosyl-N-acetyl-galactosaminyl-(N-acetylneuraminyl)-galactosyl-glucose, did not inhibit growth of SV40 3T3 cells in culture. Ceramide alone was also ineffective as a growth inhibitor. However, the tetrahexosyl ceramide derived from the above ganglioside was equally as effective as the parent compound in retarding growth of SV40 3T3 cells. Similarly, mono-, di- and trihexosyl ceramides were also effective in inhibiting growth of these cells. Gangliosides added to the culture media were rapidly accumulated by cells, apparently at the plasma membrane. The accumulated ganglioside was not degraded by the cells. However, the accumulated ganglioside could be distinguished from gangliosides synthesized in vivo by the lability of the former to neuraminidase.