Document Detail


Acute phase mediated change in glycosylation of rat alpha 1-acid glycoprotein in transgenic mice.
MedLine Citation:
PMID:  1794039     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Transgenic mouse lines carrying the gene for rat alpha 1-acid glycoprotein (AGP) express the protein in the plasma at concentrations equal to or exceeding that of acute phase rats. Owing to the high basal level, these transgenic mice represent a unique experimental system for defining the largely unknown function of AGP. Since the carbohydrate moiety of AGP has been found to be changed during acute phase and the oligosaccharide structure to be important for immunomodulating activity of the protein, the rat AGP in transgenic mice was characterized by lectin-affinity immuno-electrophoresis. Unlike in the rat, the AGP in the transgenic mouse plasma consisted primarily of strongly concanavalin A-reactive forms. Acute phase mediated a several-fold increase in the total plasma concentration of AGP concomitant with a shift toward moderately concanavalin A-reactive forms. A similar change in concanavalin A-reactive forms was observed for the endogenous acute phase plasma protein haptoglobin. To define the role of inflammatory factors in AGP production, primary cultures of hepatocytes were prepared. In contrast to in vivo, the AGP recovered from tissue culture medium represented primarily the concanavalin A-non-reactive form. Treatment of the cells with recombinant human interleukin-1, interleukin-6 and dexamethasone stimulated the production of concanavalin A-reactive AGP forms. The data indicate that the glycosylation pattern of plasma-resident AGP is modulated by acute phase, but that the profile of AGP forms does not coincide with that secreted by hepatocytes in tissue culture. This finding demands an assessment of which of the possible glycosylated forms of AGP is functionally significant in vivo.
Authors:
A Mackiewicz; M J Dewey; F G Berger; H Baumann
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Glycobiology     Volume:  1     ISSN:  0959-6658     ISO Abbreviation:  Glycobiology     Publication Date:  1991 Jun 
Date Detail:
Created Date:  1992-04-03     Completed Date:  1992-04-03     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  9104124     Medline TA:  Glycobiology     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  265-9     Citation Subset:  IM    
Affiliation:
Department of Cancer Immunology, Academy of Medicine, Poznan, Poland.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cells, Cultured
Glycosylation
Immunoelectrophoresis
Lipopolysaccharides / toxicity
Liver / metabolism*
Mice
Mice, Transgenic
Orosomucoid / genetics,  isolation & purification,  metabolism*
Rats
Grant Support
ID/Acronym/Agency:
DK 33886/DK/NIDDK NIH HHS
Chemical
Reg. No./Substance:
0/Lipopolysaccharides; 0/Orosomucoid

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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