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.
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.
van Dijk
W
W
Department of Medical Chemistry, Faculty of Medicine, Vrije Universiteit, Amsterdam, The Netherlands.
Pos
O
O
van der Stelt
M E
ME
Moshage
H J
HJ
Yap
S H
SH
Dente
L
L
Baumann
P
P
Eap
C B
CB
D000818:Animals; D002056:Burns / Q000097:blood / Q000503:physiopathology; D006528:Carcinoma, Hepatocellular; D002478:Cells, Cultured; D016207:Cytokines / Q000494:pharmacology; D015870:Gene Expression; D014644:Genetic Variation; D006031:Glycosylation; D006801:Humans; D007249:Inflammation; D008099:Liver / Q000187:drug effects / Q000378:metabolism*; D008113:Liver Neoplasms; D051379:Mice; D008822:Mice, Transgenic; D009961:Orosomucoid / Q000032:analysis / Q000096:biosynthesis / Q000235:genetics*
D016207:Cytokines; D009961:Orosomucoid