Altered glycosylation of α1-acid glycoprotein in patients with inflammation and diabetes mellitus

Increased plasma N-glycome complexity is associated with higher risk of type 2 diabetes

“…Changes in the glycosylation of plasma proteins have been studied in many different diseases, including type 2 diabetes mellitus [8]. These changes have been confirmed in both individuals with diabetes and db/db mice [9,10]. Although many studies identified biantennary glycans with core fucose as structures of main interest, differences between populations with and without diabetes were never pronounced enough to have a diagnostic potential, probably because of relatively good glycaemic control in those with diabetes, administration of medicaments or the existence of many different molecular mechanisms that lead to type 2 diabetes development.…”

Veterinary Biomarker Discovery: Proteomic Analysis of Acute Phase Proteins

“…Studies have indicated significant enhancement of bi-antennary complex glycans and alpha-1-3fucosylated bi-, tri-, and tetra-antennary glycans, as well as decreases in tri-antennary glycans of AGP, in patients with inflammatory diseases. However, the modifications of AGP in patients with diabetes were not disease-specific (Higai, et al, 2003). Different forms of human cancer have likewise been associated with alterations in the glycosylation patterns of APPs.…”

“…The majority of published reports detailing the proteomic analysis of the PTM of APPs have focused on the glycosylation pattern of serum proteins associated with human inflammatory diseases (Higai, et al, 2003;Brinkman-van der Linden et al, 1996;Turner et al, 1992), and different forms of cancer (Mazhar et al, 2006;Saldova,et al, 2007;Latif et al, 2002). Modification of the biantennary structures and the 1, 3 fucosylated N-glycan structures of alpha-1-acid-glycoprotein (AGP) have been reported in patients with acute inflammation (Turner et al, 1992), and chronic conditions such as rheumatoid arthritis and diabetes mellitus (Higai, et al, 2003).…”

“…Modification of the biantennary structures and the 1, 3 fucosylated N-glycan structures of alpha-1-acid-glycoprotein (AGP) have been reported in patients with acute inflammation (Turner et al, 1992), and chronic conditions such as rheumatoid arthritis and diabetes mellitus (Higai, et al, 2003). A remarkable feature of AGP is the microheterogeneity of its sugar moieties and the modification of these sugars during disease.…”

“…Use of antibody-based strategies such as enzyme-linked immunosorbent assays (ELISA) in biomarker discovery analyses, however, limits the identification and characterization of novel candidates, as well as the detection of posttranslational modifications (PTM) of target proteins. Previous research has established that APPs are subject to modifications, such as glycosylation, in altered physiological states Higai, et al, 2003;Anderssen et al, 2001). While APPs are thought to lack specificity as candidate biomarkers of disease because of their prominence during the innate immune response, there is evidence to suggest that the modification of certain APPs could be disease-specific.…”