van Dijk W, Pos O, van der Stelt M E, Moshage H J, Yap S H, Dente L, Baumann P, Eap C B
Department of Medical Chemistry, Faculty of Medicine, Vrije Universiteit, Amsterdam, The Netherlands.
Biochem J. 1991 Jun 1;276 ( Pt 2)(Pt 2):343-7. doi: 10.1042/bj2760343.
The relative occurrence of genetic variants of human alpha 1-acid glycoprotein (AGP) in relation to changes in glycosylation was studied in sera of patients with burn injury, media of cytokine-treated primary cultures of human hepatocytes and Hep 3B cells, and sera of transgenic mice expressing the human AGP-A gene. It is concluded (i) that the glycosylation of AGP was not dependent on its genetic expression and (ii) that both the variants determined by the AGP-A gene as well as by the AGP-B/B' genes are increased after inflammation or treatment with interleukins 1 and 6.
在烧伤患者的血清、经细胞因子处理的人原代肝细胞和Hep 3B细胞培养上清液以及表达人AGP - A基因的转基因小鼠血清中,研究了人α1 - 酸性糖蛋白(AGP)基因变体的相对发生率与糖基化变化的关系。得出的结论是:(i)AGP的糖基化不依赖于其基因表达;(ii)由AGP - A基因以及AGP - B/B'基因决定的变体在炎症或用白细胞介素1和6处理后均增加。