argpyrimidine and pentosidine

argpyrimidine has been researched along with pentosidine* in 7 studies

Other Studies

7 other study(ies) available for argpyrimidine and pentosidine

ArticleYear
DAF in diabetic patients is subject to glycation/inactivation at its active site residues.
    Molecular immunology, 2018, Volume: 93

    Decay accelerating factor (DAF or CD55) is a cell associated C3 and C5 convertase regulator originally described in terms of protection of self-cells from systemic complement but now known to modulate adaptive T cell responses. It is expressed on all cell types. We investigated whether nonenzymatic glycation could impair its function and potentially be relevant to complications of diabetes mellitus and other conditions that result in nonenzymatic glycation including cancer, Alzheimer's disease, and aging. Immunoblots of affinity-purified DAF from erythrocytes of patients with diabetes showed pentosidine, glyoxal-AGEs, carboxymethyllysine, and argpyrimidine. HPLC/MS analyses of glucose modified DAF localized the sites of AGE modifications to K

    Topics: Amino Acids; Arginine; Catalytic Domain; CD55 Antigens; Complement Activation; Diabetes Mellitus; Erythrocytes; Glucose; Glycation End Products, Advanced; Humans; Lymphocyte Activation; Lysine; Models, Molecular; Ornithine; Protein Conformation; Pyrimidines; Ribose

2018
Explorative investigation of the anti-glycative effect of a rapeseed by-product extract.
    Food & function, 2018, Nov-14, Volume: 9, Issue:11

    The formation of advanced glycation end-products (AGEs) in biological systems is increased during hyperglycaemia due to higher levels of circulating glucose and carbonyl reactive species. AGEs are causative factors of common chronic diseases. Since synthetic AGE-inhibitors exert unwanted side effects and polyphenols act as potent antiglycative agents, vegetables (fruits, seeds and related by-products) are good candidates when searching for natural inhibitors. The aim of this research is to explore the suitability of a polyphenol-rich rapeseed cake extract (RCext) to decrease the formation of AGEs in an in vitro model. Different phenols, amino acids, carbohydrates, organic acids and fatty acids were identified in the RCext by GC-MS. The results confirm a high concentration of polyphenols (73.85 ± 0.64 and 86.85 ± 2.08 mg of gallic acid equivalents per g of RCext spray dried and freeze dried, respectively) which is correlated with the antioxidant capacity and anti-glycative activity in a dose dependent manner. Rapeseed cake extract (3.7 mg mL-1) significantly reduced the formation of free fluorescent AGEs and pentosidine up to 34.85%. The anti-glycative activity of the extract is likely to be due to the high concentration of sinapinic acid (0.108 ± 0.0043 mg g-1) in its metabolic profile, and the mechanism of action is mediated by methylglyoxal trapping. The results show promising potential for using rapeseed cake extract as a food supplement to ameliorate the formation of AGEs. Rapeseed cake extract should therefore be considered a potential candidate for the prevention of glycation-associated complications of age-related pathologies.

    Topics: Antioxidants; Arginine; Brassica rapa; Fruit; Glycation End Products, Advanced; Glycosylation; Lysine; Ornithine; Plant Extracts; Polyphenols; Pyrimidines; Seeds; Vegetables

2018
Characterization of modified proteins in plasma from a subtype of schizophrenia based on carbonyl stress: Protein carbonyl is a possible biomarker of psychiatric disorders.
    Biochemical and biophysical research communications, 2015, Nov-13, Volume: 467, Issue:2

    Although it's well known that protein carbonyl (PCO) and advanced glycation end-products (AGEs) levels are elevated in plasma from patients with renal dysfunction, we recently identified patients who had no renal dysfunction but possessed high levels of plasma pentosidine (PEN), which is an AGEs, and low vitamin B6 levels in serum. In this study, we investigated the status of carbonyl stress to characterize the subtype of schizophrenia. When plasma samples were subjected to Western blot analysis for various AGEs, clear differences were only observed with the anti-PEN antibody in the plasma from schizophrenic patients. Moreover, we determined the formation of protein carbonyl (PCO), a typical indicator of carbonyl stress, occurred prior to the accumulation of PEN in the plasma of schizophrenic patients. PCO levels in the plasma from schizophrenic patients were significantly higher than that from healthy subjects. Western blots analysis clearly showed that albumin and IgG were markedly carbonylated in the plasma of some patients. Thus, PCOs may be a novel marker of carbonyl stress-type schizophrenia in addition to albumin containing PEN structure.

    Topics: Adult; Antibodies, Monoclonal; Arginine; Biomarkers; Blood Proteins; Case-Control Studies; Female; Glycation End Products, Advanced; Humans; Immunoglobulin G; Lysine; Male; Middle Aged; Ornithine; Protein Carbonylation; Pyrimidines; Schizophrenia; Serum Albumin; Vitamin B 6; Vitamin B 6 Deficiency

2015
Pyridoxamine inhibits maillard reactions in diabetic rat lenses.
    Ophthalmic research, 2006, Volume: 38, Issue:5

    Advanced glycation end products (AGEs) play an important role in protein modification during cataract formation. Along with sugars, alpha-dicarbonyl compounds, such as methylglyoxal (MGO), have been implicated in AGE formation. Here we report the effect of pyridoxamine (PM) on AGEs and AGE-precursor-metabolizing enzymes in diabetic rat lenses and organ-cultured rat lenses.. Diabetes was induced in rats by injecting streptozotocin. Diabetic and nondiabetic control rats were treated with PM in drinking water for 20 weeks. Rat lenses were organ cultured with normal or high glucose. We measured lens glutathione (GSH), MGO, AGEs and activities of aldose reductase and glyoxalase I.. Treatment of diabetic rats with PM inhibited both argpyrimidine and pentosidine formation when compared to untreated diabetic animals and nondiabetic control animals. Incubation of lenses with 30 mMD-glucose caused an elevation of these AGEs. Addition of 250 muM PM along with glucose resulted in inhibition of AGE formation in organ-cultured lenses. The glyoxalase I activity was significantly reduced in diabetic rats; PM treatment inhibited such a reduction. The activity of aldose reductase was elevated in diabetic lenses; PM treatment further enhanced its activity.. Our results suggest that PM can inhibit AGE formation in the diabetic lens by enhancing the activity of aldose reductase and reacting with precursors of AGEs.

    Topics: Aldehyde Reductase; Animals; Arginine; Chromatography, High Pressure Liquid; Diabetes Complications; Diabetes Mellitus, Experimental; Glucose; Glutathione; Glycation End Products, Advanced; Lactoylglutathione Lyase; Lens Diseases; Lens, Crystalline; Lysine; Maillard Reaction; Male; Organ Culture Techniques; Ornithine; Pyridoxamine; Pyrimidines; Pyruvaldehyde; Rats; Rats, Sprague-Dawley

2006
Advanced glycation end products and oxidative stress are increased in chronic allograft nephropathy.
    American journal of kidney diseases : the official journal of the National Kidney Foundation, 2004, Volume: 43, Issue:1

    The histologic picture of chronic allograft nephropathy (CAN) resembles early arteriosclerotic lesion. Oxidative stress and advanced glycation end products (AGES) have been implicated in the pathogenesis of atherosclerosis and progression of renal disease.. The authors serially measured the plasma malonyldialdehyde (MDA), carbonyl protein (CP), pentosidine, and argpyramidine levels in 11 postrenal transplant patients with normal renal function (KPT) and 10 patients with biopsy proven CAN at 1, 3, 6, 9 through 12, and 18 through 24 months posttransplant. Data were also obtained in 16 controls and 13 patients with chronic renal failure (CRF).. Although serum creatinine, MDA, CP, pentosidine, and argpyrimidine levels decreased during follow-up in KPT, it progressively increased in patients with CAN. The mean serum creatinine level was higher in patients with CRF (3.3 +/- 0.8 mg/dL [291.7 +/- 70.7 micromol/L]) and CAN (2.4 +/- 1.1 mg/dL [212.1 +/- 96.6 micromol/L]) than in controls (1.2 +/- 0.3 mg/dL [105.8 +/- 26.7 micromol/L]) and KPT patients (1.2 +/- 0.2 mg/dL [109.7 +/- 17.7 micromol/L]; P < 0.001). Markers of oxidative stress and AGEs measured at 18 to 24 months posttransplant in patients with CAN were higher than in KPT, controls, and CRF patients. MDA (nmol/mL) was significantly higher in patients with CAN (1.30 +/- 0.30) compared with controls (0.53 +/- 0.12), KPT (0.52 +/- 0.15), and CRF (0.74 +/- 0.27) groups (P < 0.001). Plasma CP (nmol/mg protein) in patients with CAN (4.3 +/- 1.00) was higher than in controls (1.90 +/- 0.69) and KPT (2.62 +/- 1.00) groups at the same time-point (P < 0.001), but comparable with CRF (2.69 +/- 1.20). Plasma pentosidine (pmol/micromol protein) level in patients with CAN (19.69 +/- 5.05) was higher compared with controls (2.49 +/- 0.86), CRF (13.10 +/- 3.68), and KPT (14.32 +/- 6.28) groups (P < 0.001). Plasma argpyrimidine (pmol/10 micromol protein) was higher in patients with CAN (123.8 +/- 17.9) compared with controls (4.81 +/- 1.91), CRF (56.92 +/- 29.67), and KPT (31.1 +/- 11.1; P < 0.001) groups.. Oxidative stress and AGEs are increased in patients with CAN, which cannot be explained by the decline in renal function alone. Oxidative stress and AGEs may be one among the nonimmune mediators of CAN.

    Topics: Adult; Arginine; Case-Control Studies; Creatinine; Female; Glycation End Products, Advanced; Humans; Immunosuppressive Agents; Kidney Failure, Chronic; Kidney Transplantation; Lysine; Male; Malondialdehyde; Middle Aged; Ornithine; Oxidative Stress; Pyrimidines; Transplantation, Homologous

2004
Time-resolved and steady-state fluorescence spectroscopic studies of the human lens with comparison to argpyrimidine, pentosidine and 3-OH-kynurenine.
    Photochemistry and photobiology, 2002, Volume: 76, Issue:5

    The intrinsic fluorescence from the human lens on excitation in the UV region, referred to as blue lens autofluorescence, increases with age or in the presence of diabetes. The present study reveals that the relative contribution of compounds responsible for the blue autofluorescence appears to be a constant with age. Three potential candidates for the blue fluorescence were also studied with respect to fluorescence spectroscopic properties. These were argpyrimidine and pentosidine, both advanced glycation end products, and 3-hydroxykynurenine (3-OH-kynurenine), a photooxidative derivative of tryptophan. It was shown that the spectral properties of argpyrimidine and pentosidine are compatible with the observed blue fluorescence of the human lens, whereas the fluorescence from 3-OH-kynurenine is negligible.

    Topics: Adult; Aged; Arginine; Female; Fluorescence; Humans; Kynurenine; Lens, Crystalline; Lysine; Male; Middle Aged; Molecular Structure; Ornithine; Photochemistry; Pyrimidines; Spectrometry, Fluorescence; Time Factors

2002
Chromatographic quantification of argpyrimidine, a methylglyoxal-derived product in tissue proteins: comparison with pentosidine.
    Analytical biochemistry, 2001, Volume: 290, Issue:2

    Methylglyoxal (MG), an alpha-dicarbonyl compound, can be produced in vivo by several metabolic pathways and the Maillard reaction. It reacts rapidly with proteins to form advanced glycation end products or AGEs. We previously isolated and characterized a blue fluorescent product of the reaction between MG and arginine, which we named argpyrimidine. We found that argpyrimidine was stable to acid hydrolysis, which allowed us to hydrolyze tissue proteins with 6 N HCl and quantify argpyrimidine by high-performance liquid chromatography. Here we report argpyrimidine concentrations in human lens and serum proteins as determined by HPLC. We have also measured pentosidine, a fluorescent AGE derived from pentose sugars, and compared the concentrations of pentosidine and argpyrimidine. We found two- to threefold higher argpyrimidine concentrations in diabetic serum proteins than in nondiabetic controls (9.3 +/- 6.7 vs 4.4 +/- 3.4 pmol/mg). We found a significant correlation (P = 0.0001) between serum protein argpyrimidine and glycosylated hemoglobin. Argpyrimidine concentrations were approximately seven times greater in brunescent cataractous lenses than in aged noncataractous lenses. Pentosidine concentrations in serum and lens proteins were much lower than argpyrimidine concentrations; in general, argpyrimidine levels were 10--25 times higher than pentosidine. Results from our study confirm that MG-mediated arginine modifications occur in vivo and provide a method for assessing protein-arginine modification by MG in aging and diabetes.

    Topics: Adolescent; Adult; Aged; Analysis of Variance; Arginine; Blood Proteins; Diabetes Mellitus; Humans; Lens, Crystalline; Lysine; Middle Aged; Ornithine; Pyrimidines; Pyruvaldehyde

2001