Chen J J, London I M
Massachusetts Institute of Technology, Harvard-MIT Division of Health Sciences and Technology, Cambridge 02139, USA.
Trends Biochem Sci. 1995 Mar;20(3):105-8. doi: 10.1016/s0968-0004(00)88975-6.
Protein synthesis is regulated by the phosphorylation of the alpha-subunit of eukaryotic initiation factor 2 (eIF-2 alpha) in a variety of cells. At present, there are two distinct mammalian eIF-2 alpha kinases that have been cloned, the double-stranded-RNA-dependent eIF-2 alpha kinase (PKR) and the heme-regulated eIF-2 alpha kinase (HRI). HRI is activated under conditions of heme deficiency in immature erythroid cells, and its activity is inhibited by heme. The high levels of HRI in reticulocytes indicate that its major physiological role is the regulation of protein synthesis, particularly of hemoglobin, according to the concentration of heme in these cells.
蛋白质合成在多种细胞中受真核生物起始因子2(eIF - 2α)α亚基磷酸化的调控。目前,已克隆出两种不同的哺乳动物eIF - 2α激酶,即双链RNA依赖性eIF - 2α激酶(PKR)和血红素调节性eIF - 2α激酶(HRI)。HRI在未成熟红细胞血红素缺乏的条件下被激活,其活性受血红素抑制。网织红细胞中高水平的HRI表明,根据这些细胞中血红素的浓度,其主要生理作用是调节蛋白质合成,尤其是血红蛋白的合成。