Changes in serum glycoprotein glycosylation during experimental inflammation in mice are general, unrelated to protein type, and opposite changes in man and rat: studies on mouse serum alpha 1-acid glycoprotein, alpha 1-esterase, and alpha 1-protease inhibitor.
Using the method of crossed affinity immunoelectrophoresis with concanavalin A in combination with digital image processing, unrelated serum glycoproteins from normal mice and from mice undergoing an experimentally induced inflammation were analyzed for their carbohydrate-derived microheterogeneity profile. This profile changed in a generalized way in mouse serum samples taken at various time intervals after the initial induction of inflammation. The changes are not related to the acute-phase behavior of the protein itself (be it positive, negative, or nonreacting), and they are opposite to the changes in microheterogeneity profiles reported previously for glycoproteins during the acute phase in human and rat sera. These findings are discussed in the context of the biosynthetic control of glycoprotein glycosylation during the acute-phase response.
Heegaard
P M
PM
Protein Laboratory, University of Copenhagen, Panum Institute, Denmark.
D000210:Acute-Phase Reaction / Q000097:blood; D000818:Animals; D004950:Esterases / Q000097:blood*; D005260:Female; D006031:Glycosylation; D006801:Humans; D007091:Image Processing, Computer-Assisted; D007249:Inflammation / Q000097:blood* / Q000139:chemically induced; D051379:Mice; D009961:Orosomucoid / Q000378:metabolism*; D051381:Rats; D013045:Species Specificity; D000515:alpha 1-Antitrypsin / Q000378:metabolism*
D009961:Orosomucoid; D000515:alpha 1-Antitrypsin; D004950:Esterases