Non-enzymatic glycosylation of proteins is one of the key mechanisms in the pathogenesis of diabetic complications. Glycation of IgG is of special interest due to its possible influence on the functionality of immunoglobulins and overall immuno-competence. The aim of this study was to clarify more details of in vitro glycation of IgG and to study the effect of this modification on its interatio...

The conformational changes of the glycated ovalbumin were studied by hydrogen/deuterium exchange coupled with high resolution mass spectrometry technique (HDX-MS). After incubation with glucose at 50 °C for 6 h, 9 glycated peptides were detected and the corresponding glycation sites were identified. The glycation extent of each peptide was relatively high, almost over 0.5 in all peptides. A det...

1. The effect of in vitro glycation on delta-aminolevulinic dehydratase (ALA-D) under several experimental conditions was investigated. When preincubated with 500 mM glucose at 37 degrees C for 20 hr, ALA-D was 80% inactivated and glycated hemoglobin levels were increased more than fourfold. 2. Thiobarbituric acid species were not modified during glycation; therefore ALA-D inactivation cannot b...

Glycation of immunoglobulin G (IgG) can result from incubation with a reducing sugar in vitro or during circulation in vivo. Upon injection of a recombinantly produced human therapeutic IgG into humans, changes in the glycation levels could be observed as a function of circulation time. Mass changes on the individual IgG polypeptide chains as the results of glycation were determined using rever...

The Diabetes Control and Complications Trial (DCCT) demonstrated that intensive therapy aimed at improved glucose control markedly reduced the risk of diabetes complications compared with conventional therapy. The principal determinant of risk was the history of glycemia. Recently, McCarter et al. (Diabetes Care 27:1259-1264, 2004) have presented analyses of the publicly available DCCT data usi...

Glycation of proteins forms fructosamines and AGEs (advanced glycation end products). Oxidative and nitrosative stress leads to the formation of oxidative and nitrosative modifications. The modified amino acid residues formed in these processes are biomarkers of protein damage: some are risk markers and some may be risk factors for disease development. We developed a method for the concurrent q...

Association of rs1800624 Polymorphism in Receptor for Advanced Glycation End Products Gene Promoter with the Risk Diabetic Nephropathy

The reaction between reducing sugars and protein free amines, known as the Maillar reaction results in the formation of advanced glycation endproducts (AGEs). AGE modification changes the structure of proteins to amyloid cross-beta structure. These protein structures can activate receptors known as RAGE on glial cells (microglia and astrocytes), and induce the expression of inducible nitric oxi...

Glycation between proteins and sugars via the Maillard reaction has been shown to improve heat stability of proteins. In this study, inulin, a healthy dietary fiber, was glycated with whey protein isolate (WPI), effects conditions were investigated. Conjugates prepared by freeze-drying mixed WPI inulin solutions at 1:1 6:1 WPI-to-inulin weight ratios followed dry heating 70, 75, or 80 °C for 12...

Oxidative stress and protein glycation play pivotal roles in the pathophysiology of diabetes mellitus and its vascular complications. The present study aimed to investigate the anti-glycation properties of essential oils obtained from different parts of Juniperus communis subsp. hemisphaerica. The branchlets of male tree (BMT) and branchlets of female (BFT) tree, and fruits of J. communis subsp...