Barouki R, Chobert M N, Finidori J, Billon M C, Hanoune J
Mol Cell Biochem. 1983;53-54(1-2):77-88. doi: 10.1007/BF00225247.
Gamma glutamyltransferase (GGT) is a membrane-bound enzyme that is involved in glutathione metabolism and aminoacids uptake. GGT activity is stimulated by a number of hormones and pharmacological agents in certain animal tissues. In rat liver, adrenalectomy causes a 2-fold decrease in GGT activity and hydrocortisone treatment of adrenalectomized animals specifically stimulates this enzyme activity. In a highly differentiated hepatoma cell line, Fao, GGT activity is similar to rat liver and is under glucocorticoids control. These hormones specifically stimulate GGT activity (2- to 3-fold). Translation and transcription inhibitors prevent the hormonal effect. The stimulation of GGT activity is therefore probably due to an increase in GGT mRNA synthesis. The results reported suggest that the Fao cell line is a very convenient system for the study of the molecular mechanisms of both the glucocorticoid effects on differentiated cells as well as the modulation of membrane-bound enzymes biosynthesis.
γ-谷氨酰转移酶(GGT)是一种膜结合酶,参与谷胱甘肽代谢和氨基酸摄取。在某些动物组织中,多种激素和药物可刺激GGT活性。在大鼠肝脏中,肾上腺切除导致GGT活性降低两倍,而对肾上腺切除的动物进行氢化可的松治疗可特异性刺激该酶活性。在高度分化的肝癌细胞系Fao中,GGT活性与大鼠肝脏相似,且受糖皮质激素控制。这些激素可特异性刺激GGT活性(增加2至3倍)。翻译和转录抑制剂可阻止激素效应。因此,GGT活性的刺激可能是由于GGT mRNA合成增加所致。所报道的结果表明,Fao细胞系是研究糖皮质激素对分化细胞的作用以及膜结合酶生物合成调节的分子机制的非常便利的系统。