Dyken J J, Sambanis A
School of Chemical Engineering, Georgia Institute of Technology, Atlanta 30332-0100.
Enzyme Microb Technol. 1994 Feb;16(2):90-8. doi: 10.1016/0141-0229(94)90069-8.
The effect of ammonium on protein processing and secretion from mouse insulinoma beta TC3 cells and recombinant mouse pituitary AtT-20 cells was investigated. Protein stored in granules of the regulated secretion pathway was discharged from cells with secretagogues, and the addition of new protein was encouraged by recharging cells in serum-containing medium with or without added ammonium. Ammonium at 6 mM inhibits the addition of insulin-related peptides to intracellular stores in both cell lines; it is not clear whether this effect is dose dependent for concentrations between 0 and 6 mM. There is a slight increase in insulin-related proteins secreted during recharging of cells in the presence of ammonium. Using reverse-phase high-performance liquid chromatography to separate proinsulin from insulin, we found that extracts from beta TC3 cells recharged in the presence of 6 mM ammonium contain significantly less insulin than control cells recharged in the absence of ammonium.
研究了铵对小鼠胰岛素瘤βTC3细胞和重组小鼠垂体AtT-20细胞中蛋白质加工和分泌的影响。储存于调节性分泌途径颗粒中的蛋白质通过促分泌剂从细胞中释放出来，在含或不含添加铵的含血清培养基中对细胞进行再充能可促进新蛋白质的添加。6 mM的铵会抑制两种细胞系中胰岛素相关肽添加到细胞内储存中；尚不清楚这种效应对于0至6 mM之间的浓度是否呈剂量依赖性。在铵存在的情况下细胞再充能过程中分泌的胰岛素相关蛋白略有增加。使用反相高效液相色谱法将胰岛素原与胰岛素分离，我们发现，在6 mM铵存在下再充能的βTC3细胞提取物中的胰岛素含量明显低于在无铵情况下再充能的对照细胞。
