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1

Differences in nonezymatic glycation of histones

100%
Lakatos A., Kiss N., Jobst K.
Acta Biochimica Polonica
|
1994
|
tom 41
|
nr 4
Time course of glucose binding by histone HI and total histones was followed in isolated histone preparations and in thymus nuclei. In both cases the uptake of glucose by HI was surprisingly high in contrast to a much lower uptake of glucose by total histones. DNA is not implicated in glycation of histones in nuclei.
2

Thermal glycation of proteins by D-glucose and D-fructose

75%
Kanska U., Boratynski J.
Archivum Immunologiae et Therapiae Experimentalis
|
2002
|
tom 50
|
nr 1
3

Stability of reconstituted casein systems against calcium ions, high temperature and ethanol

75%
Minkiewicz P., Dziuba J., Darewicz M., Mioduszewska H.
Polish Journal of Natural Sciences
|
2002
|
tom 10
4

Elevated advanced oxidation protein products levels in patients with liver cirrhosis

63%
Zuwala-Jagiello J., Pazgan-Simon M., Simon K., Warwas M.
Acta Biochimica Polonica
|
2009
|
tom 56
|
nr 4
679-685
Serum concentrations of advanced oxidation protein products (AOPPs) and glycation end products (AGEs) were assessed with respect to functional compromise of liver, as determined by the Child-Pugh and MELD scores. Patients with decompensated liver cirrhosis (Child-Pugh B and C) exhibited significantly higher serum concentrations of AOPPs than both patients with compensated liver cirrhosis (Child-Pugh A) and controls. The levels of plasma AGEs in all liver cirrhotic patients were higher when compared with those with the controls and this difference was statistically significant. Plasma total antioxidant status of the patients was significantly lower than that of controls. Significant positive correlations between AOPPs level and the MELD score and between the oxidative stress index and the MELD score were found in all patients with liver cirrhosis. Altered AOPPs levels in decompensated patients may influence the potency of oxidative stress and the progression of liver disease.
5
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Influence of glycation of wheat albumins and globulins on their immunoreactivity and physicochemical properties

63%
Bielikowicz K., Wojtacha P., Kostyra E., Iwan M., Jarmolowska B., Kostyra H.
Polish Journal of Food and Nutrition Sciences
|
2010
|
tom 60
|
nr 4
Glycation (non-enzymatic glycosylation) is a spontaneous reaction that occurs during food processing, storage and preparation of food, which can have a significant influence on physiochemical and biological properties of food proteins. Glycation has been used mostly for improvement of functional properties of proteins although there is increasing concern of possible changes in biologic properties of glycation products. The influence of dry-heat glycation with glucose on immunoreactive properties of wheat salt-soluble proteins has been studied. It has been shown that glycation caused differences in electrophoretic patterns (both 1D and 2D), as well as in Western-immunoblotting with rabbit IgG and human IgE. A significant increase in immunoreactivity has been observed, as well as a decrease in free amino group. Thermostable, immunoreactive and susceptible for glycation protein band with molecular weight of approximately 13 kDa (by SDS-PAGE) has been selected for the N-terminal sequence analysis and determined to be an alpha-amylase inhibitor. Dry heat glycation is a very potent but nondestructive method of protein glycation, that leads to high degree of substitution and changes in both physicochemical and biological (immunological) properties of food proteins.
6

The anti-apoptotic activity of albumin for endothelium is inhibited by advanced glycation and products restricting intramolecular movement

63%
Zoellner H., Siddiqui S., Kelly E., Medbury H.
Cellular and Molecular Biology Letters
|
2009
|
tom 14
|
nr 4
575-586
Human serum albumin (HSA) inhibits endothelial apoptosis in a highly specific manner. CNBr fragmentation greatly increases the effectiveness of this activity, suggesting that this type of protection is mediated by a partially cryptic albumin domain which is transiently exposed by intramolecular movement. Advanced glycation end-product (AGE) formation in HSA greatly reduces its intra-molecular movement. This study aimed to determine if this inhibits the anti-apoptotic activity of HSA, and if such inactivation could be reversed by CNBr fragmentation. HSA-AGE was prepared by incubating HSA with glucose, and assessed using the fructosamine assay, mass spectrometry, SDS-PAGE and fluorometry. Low levels of AGE in the HSA had little effect upon its anti-apoptotic activity, but when the levels of AGE were high and the intra-molecular movement was reduced, endothelial cell survival was also found to be reduced to levels equivalent to those in cultures without HSA or serum (p > 0.001). Survival was restored by the inclusion of native HSA, despite the presence of HSA with high levels of AGE. Also, CNBr fragmentation of otherwise inactive HSA-AGE restored the anti-apoptotic activity for endothelium. Apoptosis was confirmed by DNA gel electrophoresis, transmission electron microscopy and fluorescence-activated cell sorting analysis, and there was no evidence for direct toxicity in the HSA-AGE preparations. The results are consistent with the proposed role of intra-molecular movement in exposing the anti-apoptotic domain in HSA for endothelium. The levels of AGE formation required to inhibit the anti-apoptotic activity of HSA exceeded those reported for diabetes. Nonetheless, the data from this study seems to be the first example of reduced protein function due to AGE-restricted intra-molecular movement.
7

Characterization of bovine serum albumin glycated with glucose, galactose and lactose

63%
Ledesma-Osuna A. I., Ramos-Clamont G., Vazquez-Moreno L.
Acta Biochimica Polonica
|
2008
|
tom 55
|
nr 3
491-497
The non-enzymatic reaction between reducing sugars and proteins, known as glycation, has received increased attention from nutritional and medical research. In addition, there is a large interest in obtaining glycoconjugates of pure well-characterized oligosaccharides for biological research. In this study, glycation of bovine serum albumin (BSA) by d-glucose, d-galactose and d-lactose under dry-heat at 60°C for 30, 60, 120, 180 or 240 min was assessed and the glycated products studied in order to establish their biological recognition by lectins. BSA glycation was monitored using gel electrophoresis, determination of available amino groups and lectin binding assays. The BSA molecular mass increase and glycation sites were investigated by mass spectrometry and through digestion with trypsin and chymotrypsin. Depending on time and type of sugar, differences in BSA conjugation were achieved. Modified BSA revealed reduction of amino groups’ availability and slower migration through SDS/PAGE. d-Galactose was more reactive than d-glucose or d-lactose, leading to the coupling of 10, 3 and 1 sugar residues, respectively, after 120 minutes of reaction. BSA lysines (K) were the preferred modified amino acids; both K256 and K420 appeared the most available for conjugation. Only BSA-lactose showed biological recognition by specific lectins.
8

Advanced glycation end-products prepared in solution under high pressure contain epitopes distinct from those formed in the dry reaction at high temperature

63%
Staniszewska M., Jarosz S., Jon M., Gamian A.
Archivum Immunologiae et Therapiae Experimentalis
|
2005
|
tom 53
|
nr 1
9
Content available remote

Fluidising effect of resorcylidene aminoguanidine on sarcolemmal membranes in streptozotocin-diabetic rats: blunted adaptation of diabetic myocardium to Ca2plus overload

63%
Waczulikova I., Ziegelhoffer A., Orszaghova Z., Carsky J.
Journal of Physiology and Pharmacology
|
2002
|
tom 53
|
nr 4,2
The "remodelling" of cardiac sarcolemma in diabetes is believed to underlie the reduced sensitivity of diabetic hearts due to their overload with extracellular calcium. Along with a non-enzymatic glycosylation and the free radical-derived glycoxidation of sarcolemmal proteins there is ongoing reduction in cardiomyocyte membrane fluidity, the modulator of cardiac sarcolemmal functioning. Aminoguanidine derivatives, that inhibit glycation and glycoxidation, might suppress myocardium "remodelling" occurring in diabetic heart. To verify this hypothesis, we studied physical parameters of cardiac sarcolemma from the streptozotocin-induced diabetic rats (45 mg.kg-1 i.m.) treated with resorcylidene aminoguanidine (RAG, 4 or 8 mg.kg-1 i.m.). The treatment with RAG not only completely abolished protein glycation and a generation of free oxygen species (p<0.001) in treated diabetic animals, but also considerably attenuated the decrease in sarcolemmal membrane fluidity (p<0.001). In diabetic animals the "normalizatio". of the sarcolemmal membrane fluidity was accompanied by the vastly increased susceptibility of diabetic hearts to be overload with external calcium. We concluded that the decreased fluidity of the sarcolemmal membrane, apparently linked to the excessive glycation of sarcolemmal membrane proteins, might be intimately connected with the adaptation mechanism(s) that are likely to develop in diabetic heart to protect it against the overload with external calcium.
10

Evaluation of high temperature glycation of proteins and peptides by electrospray ionization mass spectrometry

63%
Stefanowicz P., Boratynski J., Kanska U., Petry I., Szewczuk Z.
Acta Biochimica Polonica
|
2001
|
tom 48
|
nr 4
Recently Boratyński & Roy (Glycoconjugate J., 1998, 15, 131) described a fast and convenient procedure for the synthesis of glycoconjugates. In the present study we used ESI-MS and circular dichroism as tools to analyze non-enzymatic glycation prod­ucts of proteins and peptides. We discuss influence of reaction conditions on the rate of glycation of lysozyme. We analyze for the first time collision induced dissociation spectra of the obtained peptide conjugates.
11

Bacterial recognition of thermal glycation products derived from porcine serum albumin with lactose

51%
Sarabia-Sainz A., Ramos-Clamont G., Winzerling J., Vazquez-Moreno L.
Acta Biochimica Polonica
|
2011
|
tom 58
|
nr 1
 Recently, glyco-therapy is proposed to prevent the interaction of bacterial lectins with host ligands (glycoconjugates). This interaction represents the first step in infection. Neoglycans referred to as PSA-Lac (PSA-Glu (β1-4) Gal) were obtained by conjugation of porcine serum albumin (PSA) with lactose at 80 °C, 100 °C and 120 ºC. Characterization studies of the products showed that PSA could contain 1, 38 or 41 added lactoses, depending on the reaction temperature. These neoglycans were approximately 10 times more glycated than PSA-Lac obtained in previous work. Lactose conjugation occurred only at lysines and PSA-Lac contained terminal galactoses as confirmed by Ricinus communis lectin recognition. Furthermore, Escherichia coli K88+, K88ab, K88ac and K88ad adhesins showed affinity toward all PSA-Lac neoglycans, and the most effective was the PSA-Lac obtained after 100 ºC treatment. In vitro, this neoglycan partially inhibited the adhesion of E. coli K88+ to piglet mucin (its natural ligand). These results provide support for the hypothesis that glycated proteins can be used as an alternative for bioactive compounds for disease prevention.
12
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Faba bean albumins glycation

51%
Kostyra H., Darewicz M., Smyk B.
Polish Journal of Food and Nutrition Sciences
|
1992
|
tom 01
|
nr 4
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