Morrison M H, Di Monte D, Jernström B
Chem Biol Interact. 1985 Feb-Apr;53(1-2):3-12. doi: 10.1016/s0009-2797(85)80079-x.
In primary cultures of rat hepatocytes the intracellular level of reduced glutathione (GSH) declines to approx. 50% of that observed in freshly isolated cells within 1 h of culture. Pretreatment of freshly isolated hepatocytes with diethylmaleate (DEM) to deplete GSH and inhibition of glutathione synthesis by buthionine sulfoximine (BSO) markedly decrease the proportion of cells attaching to the collagen coated culture dishes. A positive correlation between the intracellular content of GSH and the ability of hepatocytes to attach to collagen is observed. Presence of dithiothreitol (DTT) in the culture medium efficiently prevents hepatocyte attachment. A net increase in hepatocyte disulfides is also observed after the first hours of culture. The formation of disulfides seems to be essential for the attachment of hepatocytes to collagen. The depletion of GSH in the early period of culture is probably due to its regulatory function of thiol/disulfide groups in proteins and/or its involvement in the synthesis of essential cytoskeletal proteins.
在大鼠肝细胞原代培养中，还原型谷胱甘肽（GSH）的细胞内水平在培养1小时内降至新鲜分离细胞中观察到水平的约50%。用马来酸二乙酯（DEM）预处理新鲜分离的肝细胞以耗尽GSH，并通过丁硫氨酸亚砜胺（BSO）抑制谷胱甘肽合成，显著降低了附着在胶原包被培养皿上的细胞比例。观察到GSH的细胞内含量与肝细胞附着于胶原的能力之间呈正相关。培养基中存在二硫苏糖醇（DTT）可有效防止肝细胞附着。培养最初几小时后还观察到肝细胞二硫化物的净增加。二硫化物的形成似乎对肝细胞附着于胶原至关重要。培养早期GSH的消耗可能是由于其对蛋白质中硫醇/二硫键基团的调节功能和/或其参与必需细胞骨架蛋白的合成。
