Quantitative Screening of Protein Glycation, Oxidation, and Nitration Adducts by LC‐MS/MS: Protein Damage in Diabetes, Uremia, Cirrhosis, and Alzheimer's Disease

Thornalley, Paul J.

doi:10.1002/0471973122.ch22

Cited by 22 publications

(18 citation statements)

References 138 publications

(196 reference statements)

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“…Activated leukocytes have also been associated with increased concentrations of plasma AGEs (Fig. 1D), and several studies have shown elevated levels of these AOPPs in hemodialysis patients (Thornalley and Rabbani 2011; Agalou et al 2005; Thornalley et al 2003; Thornalley 2006). Complement proteins themselves are glycated and may contain AGEs, which are suspected to influence complement activity (Cheng and Gao 2005; Acosta et al 2000; Davies et al 2005; Zhang et al 2011; Austin et al 1987; Hair et al 2012; Niemann et al 1991; Thornalley et al 1999).…”

Section: Introductionmentioning

confidence: 94%

Targeted complement inhibition as a promising strategy for preventing inflammatory complications in hemodialysis

et al. 2012

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Hemodialysis is the most common method used to remove waste and hazardous products of metabolism in patients suffering from renal failure. Hundreds of thousands of people with end-stage renal disease undergo hemodialysis treatment in the United States each year. Strikingly, the 5-year survival rate for all dialysis patients is only 35%. Most of the patients succumb to cardiovascular disease that is exacerbated by the chronic induction of inflammation caused by contact of the blood with the dialysis membrane. The complement system, a strong mediator of pro-inflammatory networks, is a key contributor to such biomaterial-induced inflammation. Though only evaluated in experimental ex vivo settings, specific targeting of complement activation during hemodialysis has uncovered valuable information that points towards the therapeutic use of complement inhibitors as means to control the unwelcomed inflammatory responses and consequent pathologies in hemodialysis patients.

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Section: Introductionmentioning

confidence: 94%

Targeted complement inhibition as a promising strategy for preventing inflammatory complications in hemodialysis

et al. 2012

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“…This is best achieved by enzymatic hydrolysis as the alternative acid or basic hydrolysis changes glycation adduct contents. Glycation free adducts are quantified by direct analysis of ultrafiltrate of plasma, urine, or dialysate (4).…”

Section: Clearance Of Glycation Adducts and Consequences Of The Clearmentioning

confidence: 99%

PROGRESS IN UREMIC TOXIN RESEARCH: Highlights and Hotspots of Protein Glycation in End‐Stage Renal Disease

Thornalley

Rabbani

2009

Seminars in Dialysis

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Analysis of tissues, plasma, urine, other body fluids, and dialysate for glycation adducts has revealed the presence of two major forms: glycation adduct residues of proteins and related glycated amino acids--called glycation free adducts. The major effect on protein glycation in uremia is loss of clearance of glycation free adducts and their marked increase in plasma. Changes in glycation adduct residue content of plasma protein in uremia is, in contrast, relatively modest. There is now doubt as to whether the concept of interaction of advanced glycation endproduct (AGE)-modified proteins with putative AGE receptors can be sustained in vivo. A residual important feature of the receptor for AGEs may be decrease in expression of glyoxalase 1 of the antiglycation defence by S100A12 protein leaving the vasculature vulnerable to dicarbonyl stress and related AGE formation. The dicarbonyl proteome, proteins susceptible to dicarbonyl glycation at functional sites, is the likely mediator of glycation damage in uremia. Glycation of type IV collagen with shedding of endothelial cells and glycation of apolipoprotein B100 with increased atherogenicity of low density lipoprotein are two examples which may link protein glycation to increased risk of cardiovascular disease in end-stage renal disease.

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“…Dicarbonyl compounds react with amino acid residues (lysine and arginine) in proteins to produce glycated proteins [advanced glycation end products (AGEs)].AGEs dimerize by cross-linking through GLY-derived lysine dimers (GOLD), MG-derived lysine dimers (MOLD) and 3-DG-derived lysine dimers (DOLD; Ahmed & Thornalley 2007). The accumulation of reactive oxygen species (ROS) and AGEs stimulates the oxidation of cell components and the inactivation of proteins (Thornalley 2006). In other words, biochemicals originating from sugars are among the causal agents of diabetes (Rabbani & Thornalley 2008).…”

Section: Introductionmentioning

confidence: 99%

Methylglyoxal functions as Hill oxidant and stimulates the photoreduction of O₂ at photosystem I: a symptom of plant diabetes

Saito

Yamamoto

Makino

et al. 2011

Plant Cell & Environment

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We elucidated the metabolism of methylglyoxal (MG) in chloroplasts of higher plants. Spinach chloroplasts showed MG-dependent NADPH oxidation because of aldo-keto reductase (AKR) activity. Km for MG and Vmax of AKR activity were 6.5 mM and 3.3 mmol NADPH (mg Chl) , respectively. MG-dependent O2 uptake was inhibited by 3-(3,4-dichlorophenyl)-1, 1-dimethylurea (DCMU) and 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone (DBMIB). Under anaerobic conditions, the Qp of Chl fluorescence was suppressed. These results indicate that MG was reduced as a Hill oxidant by the photosystem I (PSI), and that O2 was reduced to O2 -by the reduced MG. In other words, MG produced in chloroplasts is preferentially reduced by PSI rather than through AKR. This triggers a type of oxidative stress that may be referred to as 'plant diabetes', because it ultimately originates from a common metabolite of the primary pathways of sugar anabolism and catabolism.

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Quantitative Screening of Protein Glycation, Oxidation, and Nitration Adducts by LC‐MS/MS: Protein Damage in Diabetes, Uremia, Cirrhosis, and Alzheimer's Disease

Cited by 22 publications

References 138 publications

Targeted complement inhibition as a promising strategy for preventing inflammatory complications in hemodialysis

Targeted complement inhibition as a promising strategy for preventing inflammatory complications in hemodialysis

PROGRESS IN UREMIC TOXIN RESEARCH: Highlights and Hotspots of Protein Glycation in End‐Stage Renal Disease

Methylglyoxal functions as Hill oxidant and stimulates the photoreduction of O₂ at photosystem I: a symptom of plant diabetes

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Quantitative Screening of Protein Glycation, Oxidation, and Nitration Adducts by LC‐MS/MS: Protein Damage in Diabetes, Uremia, Cirrhosis, and Alzheimer's Disease

Cited by 22 publications

References 138 publications

Targeted complement inhibition as a promising strategy for preventing inflammatory complications in hemodialysis

Targeted complement inhibition as a promising strategy for preventing inflammatory complications in hemodialysis

PROGRESS IN UREMIC TOXIN RESEARCH: Highlights and Hotspots of Protein Glycation in End‐Stage Renal Disease

Methylglyoxal functions as Hill oxidant and stimulates the photoreduction of O2 at photosystem I: a symptom of plant diabetes

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Methylglyoxal functions as Hill oxidant and stimulates the photoreduction of O₂ at photosystem I: a symptom of plant diabetes