Controversial behavior of aminoguanidine in the presence of either reducing sugars or soluble glycated bovine serum albumin

Extracellular matrix is modulated in advanced glycation end products milieu via a RAGE receptor dependent pathway boosted by transforming growth factor‐β1 在晚期糖基化终末产物环境中细胞外基质通过RAGE受体依赖性途径调节，转化生长因子‐β1可以促进这种调节

“…While the AGE‐RAGE pathways have been discussed in numerous studies, there are still questions regarding the identity of the AGEs structures that initiates diabetic renal dysfunction . Our previous study, has confirmed that AG has a controversial effect, having an anti‐protein cross‐linking effect, as well as generating new AGE like‐products, similar to pentosidine or glucosepane, that could bind to and activate RAGE. The slight positive effect of AG on RAGE, TGF‐ β 1 and collagen IV downregulation, observed after 24 h of exposure at higher concentrations, may be due to the ability of AG to inhibit ROS formation and effectively trap α , β ‐dicarbonyl compounds such as methylglyoxal, glyoxal, and 3‐deoxyglucosone and form substituted 3‐amino‐1,2,4‐triazine derivatives …”

“…AGE‐BSA was prepared as previously described, by incubating bovine serum albumin (BSA) with 500 mM D ‐glucose for 3 months under aerobic conditions at 37°C. AGE‐BSA and BSA samples were free of endotoxins (E‐toxate kit, Sigma‐Aldrich, St. Louis, MO, USA).…”

“…Glycated BSA fractions were separated by fast protein liquid chromatography (FPLC) gel filtration and characterized by fluorescence spectrophotometry and sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE) as previously described …”

Proteomic and immunochemical approaches to understanding the glycation behaviour of the casein and β-lactoglobulin fractions of flavoured drinks under UHT processing conditions

“…3a , lines 2–3, 5–7, 9–11, 11, 13, 16, 17 and 19). This phenomenon might be explained by the formation of Amadori compounds on the polypeptide chains, which would contribute to a slight increase in molecular weight 35 . In glycated proteins, monomer bands (Fig.…”

AGEs-Induced IL-6 Synthesis Precedes RAGE Up-Regulation in HEK 293 Cells: An Alternative Inflammatory Mechanism?

“…Advanced glycation end products (AGEs) are the result of non-enzymatic glycation processes, a cascade of events that begins with the reversible formation of a Schiff base that undergoes rearrangement to an Amadori product through a reaction between reducing sugars and amino groups of proteins [ 1 ]. This compound is slowly degraded to a plethora of compounds of various chemical structures including: N ε -carboxymethyllysine (CML) [ 2 ], pentosidine [ 3 ], and glucosepan [ 4 ], some of which possess distinct fluorescence and a propensity to crosslink proteins [ 1 , 5 ]. In diabetes, and natural aging, AGEs accumulate in different target tissues, playing a role in the pathogenesis of various complications, particularly in nephropathy through pathways dependent or independent of AGEs receptors [ 6 , 7 , 8 , 9 ].…”