α₁‐Acid glycoprotein fucosylation as a marker of carcinoma progression and prognosis

Abstract

BACKGROUNDSerum α1‐acid glycoprotein (AGP), an acute‐phase protein secreted by the liver, carries α(1,3)‐fucosylated structures on its 5 highly branched, N‐linked sugar chains.METHODSSerum AGP levels in patients with various types of malignancies (n = 214 patients) were measured using an enzyme‐linked immunosorbent assay with anti‐AGP antibody. To investigate glycoforms that differed in their degree of branching and extent of fucosylation, serum AGP samples were analyzed by crossed affinoimmunoelectrophoresis (CAIE) with concanavalin A, and Aleuria aurantia lectin (AAL), and anti‐AGP antibody.RESULTSA significant difference (P < 0.001) in serum AGP levels was observed in preoperative patients compared with levels in the healthy control group, but the levels in individual patients did not reflect their clinical status. Conversely, it was found not only that the patterns of AGP glycoforms differed widely in the patient group compared with the healthy control group, but they also changed depending on each patient's clinical status. Furthermore, AGP glycoforms seemed to be appropriate markers of disease progression and prognosis according to follow‐up studies of 45 patients during prolonged preoperative and postoperative periods.CONCLUSIONSPatients with advanced malignancies who had AGP glycoforms that contained highly fucosylated triantennary and tetraantennary sugar chains for long periods after surgery were likely to have a poor prognosis. However, patients who had AGP glycoforms without such changes were expected to have a good prognosis. Cancer 2004. © 2004 American Cancer Society.

Multilectin Assay for Detecting Fibrosis-Specific Glyco-Alteration by Means of Lectin Microarray

“…In particular, the fucose-binding lectins (Fucbinders) AOL and AAL preferentially bound to the AGPs of the cirrhosis group compared with those of the noncirrhosis group. These results are consistent with previous reports showing that ␣-1,3 fucosylation of a lactosamine unit, the Lewis X antigen, is increased in AGP molecules (19,28 ).…”

Serum Protein Profiling to Identify High-Risk Neuroblastoma: Preclinical Relevance of Blood-Based Biomarkers

“…As these serum proteins belong to the family of APPs in mice, the clinical significance of each was evaluated in relation to tumor growth. All proteins identified have links to cancer progression [8][9][10][11][12][13][14][15][16] and we demonstrated an increase of each of these APPs in tumor-bearing mouse sera (Figure 2). The serum immunoglobulin protein Ig κ-C was found to decrease in mice harboring NB as compared to controls.…”

Elevated core-fucosylated IgG is a new marker for hepatitis B virus-related hepatocellular carcinoma

“…To validate the existence of a core-fucosylated structure in IgG-L3, N-glycan profiles of IgG, IgG-L3, and IgG-L3 lacking the core-fucose were analyzed by DSA-FACE as described previously. 26,27 IgG showed 7 main biantennary glycans in the N-glycan profiling ( Supplementary Fig. S1).…”