| Autor: |
Poland DC; Glycoimmunology Group, Department of Molecular Cell Biology & Immunology, VU Medical Center, Amsterdam, The Netherlands., Kulik W, van Dijk W, Hallemeesch MM, Jakobs C, de Meer K |
| Jazyk: |
angličtina |
| Zdroj: |
Glycoconjugate journal [Glycoconj J] 2004; Vol. 20 (2), pp. 99-105. |
| DOI: |
10.1023/B:GLYC.0000018584.66712.2c |
| Abstrakt: |
Various alpha1-acid glycoprotein (AGP) glycoforms are present in plasma differing in extent of branching and/or fucosylation of their 5 N-linked glycans, as well as in concentration. It is assumed that hepatic synthesis determines the relative occurrence of the AGP-glycoforms in plasma, but experimental evidence is lacking. In this study, we have investigated the contribution of fractional synthesis rates to the plasma concentration of AGP-glycoforms that differed in relative occurrence in healthy human plasma. During a [13C]valine infusion, AGP was isolated from the plasma of healthy volunteers. Four AGP-glycoforms, differing strongly in plasma concentration were obtained by sequential affinity chromatography over concanavalin-A- and Aleuria aurantia -agarose columns. The incorporation of the [13C]valine tracer into the AGP-glycoforms was measured by gas chromatography combustion isotope ratio mass spectrometry. The mean fractional synthesis rates of the four AGP-glycoforms did not differ significantly between each other as well between individuals. The results indicated a renewal of about 15%/day of the plasma pools of each of the AGP-glycoforms. This is in support to the assumption that the differences in plasma concentration of the AGP-glycoforms are a reflection of the state of the hepatic glycosylation process. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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