Paul M, Nakamura N, Pratt R E, Dzau V J
Molecular and Cellular Vascular Research Laboratory, Brigham and Women's Hospital, Boston, Massachusetts 02115.
J Hypertens Suppl. 1988 Dec;6(4):S487-9. doi: 10.1097/00004872-198812040-00154.
The mouse pituitary tumour (AtT-20) cell transfected with the human renin gene has been shown to be a useful model system to study human renin biosynthesis. To investigate the influence of glycosylation on secretion of human renin from these cells, we performed pulse labelling experiments on transfected cells in the presence or absence of tunicamycin, a potent inhibitor of n-linked glycosylation. Intracellular and secreted renins were characterized by immunoprecipitation, sodium dodecyl sulphate (SDS) gel electrophoresis and fluorography. Our data showed that blockade of n-linked glycosylation reduced the intracellular transit time and increased the rate of prorenin secretion from transfected cells. We conclude that the carbohydrate moiety influences the kinetics of human renin secretion. This result provides one possible explanation for the observation that the secretion of glycosylated human renin is considerably slower than that of the unglycosylated mouse renin-2.
已证明转染人肾素基因的小鼠垂体肿瘤（AtT-20）细胞是研究人肾素生物合成的有用模型系统。为了研究糖基化对这些细胞中人肾素分泌的影响，我们在存在或不存在衣霉素（一种有效的N-连接糖基化抑制剂）的情况下，对转染细胞进行了脉冲标记实验。通过免疫沉淀、十二烷基硫酸钠（SDS）凝胶电泳和荧光自显影对细胞内和分泌的肾素进行了表征。我们的数据表明，N-连接糖基化的阻断减少了细胞内转运时间，并增加了转染细胞中肾素原的分泌速率。我们得出结论，碳水化合物部分影响人肾素分泌的动力学。这一结果为糖基化人肾素的分泌比未糖基化的小鼠肾素-2慢得多这一观察结果提供了一种可能的解释。
