Riddle V G, Dubrow R, Pardee A B
Proc Natl Acad Sci U S A. 1979 Mar;76(3):1298-302. doi: 10.1073/pnas.76.3.1298.
The synthesis of both cytoplasmic and nuclear proteins has been studied as quiescent, serum-deprived Swiss mouse 3T3 cells are stimulated to transit the cell cycle. In serum-arrested cells a 200,000 dalton cytoplasmic protein and a 51,000 dalton nuclear protein were found to be preferentially synthesized. In serum-stimulated cells the first major protein whose synthesis was seen to increase had a molecular mass of 42,000 daltons. This protein also showed the greatest change in synthesis during the transit from G0 to S phase. Its synthesis rose to a maximum 4--6 hr after stimulation and then declined as cells entered S phase. The protein was present in both nuclear and cytoplasmic extracts. It was identified as actin on the basis of its mobility on sodium dodecyl sulfate and isoelectric focusing polyacrylamide gels. Other proteins synthesized preferentially by stimulated cells had molecular masses of 57,000 daltons (cytoplasmic), 33,000 daltons (cytoplasmic and nuclear), and 15,000 daltons (nuclear). The synthesis of the 57,000 and 33,000 dalton proteins increased gradually after stimulation and remained high during S phase. The 15,000 dalton proteins began to be synthesized as cells entered S phase. The preferential synthesis of these proteins provides biochemical markers for the transition from quiescence to proliferation.
在静止的、血清饥饿的瑞士小鼠3T3细胞被刺激进入细胞周期时,对细胞质蛋白和核蛋白的合成进行了研究。在血清停滞的细胞中,发现一种200,000道尔顿的细胞质蛋白和一种51,000道尔顿的核蛋白被优先合成。在血清刺激的细胞中,首先观察到合成增加的主要蛋白分子量为42,000道尔顿。这种蛋白在从G0期到S期的转变过程中合成变化也最大。其合成在刺激后4 - 6小时升至最高,然后随着细胞进入S期而下降。该蛋白存在于核提取物和细胞质提取物中。根据其在十二烷基硫酸钠和等电聚焦聚丙烯酰胺凝胶上的迁移率,它被鉴定为肌动蛋白。受刺激细胞优先合成的其他蛋白分子量分别为57,000道尔顿(细胞质)、33,000道尔顿(细胞质和细胞核)和15,000道尔顿(细胞核)。57,000道尔顿和33,000道尔顿蛋白的合成在刺激后逐渐增加,并在S期保持高水平。15,000道尔顿的蛋白在细胞进入S期时开始合成。这些蛋白的优先合成提供了从静止到增殖转变的生化标记。