Investigation into the Concanavalin A reactivity, fucosylation and oligosaccharide microheterogeneity of α1-acid glycoprotein expressed in the sera of patients with rheumatoid arthritis

Acute Phase Proteins: Structure and Function Relationship

“…Marked changes in AGP glycoforms are observed during acute-phase reactions. The changes comprise alterations in branching pattern as revealed by reactivity with concanavalin A and the fucose-binding lectin (Elliott et al, 1997). Thus analysis of sialo-and asialo-oligosaccharides of AGP as well as its glycoforms is important for understanding the biological roles of AGP (Kakehi et al, 2002;Sei et al, 2002).…”

A preliminary evaluation of the differences in the glycosylation of alpha‐1‐acid glycoprotein between individual liver diseases

“…The intact glycoprotein was isolated, avoiding desialylation and structural degradation, by our previously reported method (Elliott et al, 1997) Briefly, extraneous proteins were precipitated from whole blood collected in heparinized tubes by mixing with poly (ethylene) glycol 3350 (PEG 3350) to a final concentration 40% (w/v) PEG, followed by centrifugation at 10,000g. AGP was purified from other soluble components from the collected supernatant by sequential pseudoligand dye (Reactive Blue Sepharose, Red Sepharose) and anionexchange (Q-Sepharose Fast Flow) low-pressure column chromatography steps.…”

“…Con A studies in other disease states have shown varying results (Pos et al, 1990). In rheumatoid arthritis, a progression for AGP glycosylation has been demonstrated in comparison to AGP from normal plasma, from an increased content of biantennary chains in the acute phase to a reduced content (and increased tri-and tetra-antennary) in the chronic patient (Clementson et al, 1997;Elliott et al, 1997;Hrycaj et al, 1993). With respect to this study Con A binding appears to provide a mechanism for distinguishing between AGP from normal plasma and Glycosylation of alpha-1-acid glycoprotein ORIGINAL RESEARCHliver disease in general however differentiation between individual liver diseases would appear to require the determination of more subtle differences in glycosylation.…”

Alpha-1-Acid Glycoprotein (AGP) as a Potential Biomarker for Breast Cancer

“…Decreased branching of the five glycans of AGP has been demonstrated in acute inflammation while an increase is associated with chronic inflammation [21][22][23]. Chronic inflammatory states such as those found in patients with RA are characterised by an increase in branching [24,25], increased fucosylation of the chains [26][27][28][29][30][31] and increased sialic acid content [32][33]. The expression of the antigen sialyl lewis X (SLe X ) has been found to increase on AGP oligosaccharides [20,[25][26] at any one of the 5 sites of glycosylation [27].…”

“…Chronic inflammatory states such as those found in patients with RA are characterised by an increase in branching [24,25], increased fucosylation of the chains [26][27][28][29][30][31] and increased sialic acid content [32][33]. The expression of the antigen sialyl lewis X (SLe X ) has been found to increase on AGP oligosaccharides [20,[25][26] at any one of the 5 sites of glycosylation [27]. SLe X is normally expressed on white blood cells and aids through binding to the endothelial ligand, E-Selectin, the extravasation of leukocytes into tissues to mount their inflammatory response.…”