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Inflammation-induced changes in expression and glycosylation of genetic variants of alpha 1-acid glycoprotein. Studies with human sera, primary cultures of human hepatocytes and transgenic mice. 1991
W van Dijk, and
O Pos, and
M E van der Stelt, and
H J Moshage, and
S H Yap, and
L Dente, and
P Baumann, and
C B Eap
Department of Medical Chemistry, Faculty of Medicine, Vrije Universiteit, Amsterdam, The Netherlands.
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.
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