Chromatographic evidence for amadori product formation in rat liver aminophospholipids

Pamplona, Reinald; Bellmunt, Marı́a Josep; Portero, Manuel Aguilar; Riba, D.; Prat, Joan

doi:10.1016/0024-3205(95)02020-j

Cited by 44 publications

(27 citation statements)

References 15 publications

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“…Recent studies reported the detection of Amadori-PE in biological samples (i.e., blood plasma, red blood cells, and human atherosclerotic plaques) using LC-MS (25)(26)(27)(28). During LC-MS analysis, chromatographic peaks that showed mass increments of 162 Da (most likely C 6 H 10 O 5 ) relative to the molecular masses of nonglycated PE were tentatively ascribed to Amadori-PE.…”

Section: Discussionmentioning

confidence: 99%

Ion-trap tandem mass spectrometric analysis of Amadori-glycated phosphatidylethanolamine in human plasma with or without diabetes

Nakagawa

Oak

Higuchi

et al. 2005

Journal of Lipid Research

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Section: Discussionmentioning

confidence: 99%

Ion-trap tandem mass spectrometric analysis of Amadori-glycated phosphatidylethanolamine in human plasma with or without diabetes

Nakagawa

Oak

Higuchi

et al. 2005

Journal of Lipid Research

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“…Furthermore, using ELISA, these authors concluded that the bulk of the AGE in LDL isolated from normal and diabetic subjects was located in the lipid phase. 27 Pamplona et al 28 had obtained evidence for glycated aminophospholipids in rat liver and for their increase in animals with streptozotocin-induced diabetes. With Amadori-product formation from glucose and PtdEtn now clearly established, we undertook further investigations on the effect of Glc PtdEtn on LDL lipid oxidation.…”

Section: February 2000mentioning

confidence: 99%

Glucosylated Glycerophosphoethanolamines are the Major LDL Glycation Products and Increase LDL Susceptibility to Oxidation

Ravandi

Kuksis²,

Shaikh³

2000

ATVB

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Abstract-Glycation of both protein and lipid components is believed to be involved in LDL oxidation. However, the relative importance of lipid and protein glycation in the oxidation process has not been established, and products of lipid glycation have not been isolated. Using glucosylated phosphatidylethanolamine (Glc PtdEtn) prepared synthetically, we have identified glycated diacyl and alkenylacyl species among the ethanolamine phospholipids in LDL. Accumulation of these glycation products in LDL incubated with glucose showed a time-and glucose concentration-dependent increase. LDL specifically enriched with Glc PtdEtn (25 nmol/mg protein) showed increased susceptibility to lipid oxidation when dialyzed against a 5-mol/L Cu 2ϩ solution. The presence of this glucosylated lipid resulted in a 5-fold increase in production of phospholipid-bound hydroperoxides and 4-fold increase in phospholipid-bound aldehydes. Inclusion of glucosylated phosphatidylethanolamine in the surface lipid monolayer of the LDL resulted in rapid loss of polyunsaturated cholesteryl esters from the interior of the particle during oxidation. Glycated ethanolamine phospholipids were also isolated and identified from atherosclerotic plaques collected from both diabetic and nondiabetic subjects. The present findings provide direct evidence for the previously proposed causative effect of lipid glycation on LDL oxidation.

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“…Pamplona et al (13) first showed evidence for the presence of glycated phospholipids in rat liver and found their levels increased in animals with streptozotocin-induced diabetes. Ravandi et al (14) further documented the existence of glycated aminophospholipids in human red blood cells and plasma, although their analytical technique did not distinguish between Schiff base and Amadori compounds, both of which are formed during the initial stage of the reaction of glucose with amino groups (1).…”

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confidence: 99%

Carboxymethylethanolamine, a Biomarker of Phospholipid Modification during the Maillard Reaction in Vivo

Requena

Ahmed

Fountain

et al. 1997

Journal of Biological Chemistry

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N⑀ -(Carboxymethyl)lysine (CML) is a stable chemical modification of proteins formed from both carbohydrates and lipids during autoxidation reactions. We hypothesized that carboxymethyl lipids such as (carboxymethyl)phosphatidylethanolamine (carboxymethyl-PE) would also be formed in these reactions, and we therefore developed a gas chromatography-mass spectrometry assay for quantification of carboxymethylethanolamine (CME) following hydrolysis of phospholipids. In vitro, CME was formed during glycation of dioleoyl-PE under air and from linoleoylpalmitoyl-PE, but not from dioleoyl-PE, in the absence of glucose. In vivo, CME was detected in lipid extracts of red blood cell membranes, ϳ0.14 mmol of CME/mol of ethanolamine, from control and diabetic subjects, (n ‫؍‬ 22, p > 0.5). Levels of CML in erythrocyte membrane proteins were ϳ0.2 mmol/mol of lysine for both control and diabetic subjects (p > 0.5). For this group of diabetic subjects there was no indication of increased oxidative modification of either lipid or protein components of red cell membranes. CME was also detected in fasting urine at 2-3 nmol/mg of creatinine in control and diabetic subjects (p ‫؍‬ 0.085). CME inhibited detection of advanced glycation end product (AGE)-modified protein in a competitive enzyme-linked immunosorbent assay using an anti-AGE antibody previously shown to recognize CML, suggesting that carboxymethyl-PE may be a component of AGE lipids detected in AGE low density lipoprotein. Measurement of levels of CME in blood, tissues, and urine should be useful for assessing oxidative damage to membrane lipids during aging and in disease.The nonenzymatic reaction of blood glucose with body proteins (glycation) followed by browning and oxidation reactions of glycated proteins leads to cumulative chemical modifications of tissue proteins throughout the body. These chemical changes, collectively termed the Maillard reaction, are considered to cause a gradual deterioration in the structure and function of tissue proteins and to contribute to the pathophysiology of normal aging (1-3). Further, the Maillard reaction is accelerated during hyperglycemia in diabetes, yielding advanced glycation end products (AGEs) 1 thought to be involved in the pathogenesis of diabetic complications (4 -6). Among Maillard reaction products identified thus far in tissue proteins, concentrations of pentosidine (3, 7) and N ⑀ -(carboxymethyl)lysine (CML) (7) are known to increase in human skin collagen with age, and age-adjusted concentrations of both are increased in skin collagen in diabetes (7). Moreover, there is a strong relationship between levels of these products in collagen and the status of diabetic complications (8 -10). Both CML and pentosidine require oxidative conditions for their formation, hence their description as glycoxidation products (11). Recently we showed that CML can also be formed during the reaction of autoxidizing polyunsaturated fatty acids (PUFA) with proteins (12), so that its precise biochemical origin is uncertain. The formation of ...

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Chromatographic evidence for amadori product formation in rat liver aminophospholipids

Cited by 44 publications

References 15 publications

Ion-trap tandem mass spectrometric analysis of Amadori-glycated phosphatidylethanolamine in human plasma with or without diabetes

Ion-trap tandem mass spectrometric analysis of Amadori-glycated phosphatidylethanolamine in human plasma with or without diabetes

Glucosylated Glycerophosphoethanolamines are the Major LDL Glycation Products and Increase LDL Susceptibility to Oxidation

Carboxymethylethanolamine, a Biomarker of Phospholipid Modification during the Maillard Reaction in Vivo

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