In Vivo Clearance of Alpha-1 Acid Glycoprotein Is Influenced by the Extent of Its N-Linked Glycosylation and by Its Interaction with the Vessel Wall
Figure 4
Recombinant AGP glycosylated in Pichia pastoris yeast is rapidly removed from the rabbit circulation via mannose receptors. (a) Shows the radioiodinated rAGP-WT or rAGP N(5)Q remaining in the plasma of rabbits 30 minutes after injection, without (no sugar) or with coadministered α-methylmannoside (+α MM) or D-galactose (+ Galactose). The mean and SD of 5–7 determinations are shown; *indicates versus the corresponding “no sugar” condition by Kruskal-Wallis test. The proportion of the two proteins remaining in plasma in the absence of added sugar was also compared; ***indicates by unpaired -test, Welch corrected. (b) (Gel) shows a Coomassie blue-stained 12% SDS reducing gel loaded with 5–10 μg per lane of AGP (plasma-derived); rAGP-WT; carboxypeptidase Y (CPY); and glutathione sulfotransferase (GST). Molecular mass marker positions, shown at left, correspond to: 100; 90; 80; 70; 60; 50; 40; 30; 25; and 20 kDa. (c) (GNA blot) is a blotted replicate of the gel shown in (b), probed with GNA lectin.
