Identification of the Carboxymethyllysine Residue in the Advanced Stage of Glycated Human Serum Albumin.

Takanashi, Masaya; Sakurai, Tamiko; Tsuchiya, Susumu

doi:10.1248/cpb.40.705

Cited by 10 publications

(8 citation statements)

References 1 publication

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“…A common structure in AGE modified macromolecules that interacts with polyclonal antibodies has been suggested [97]. But, polyclonal antibodies against AGE-BSA or AGERNase failed to recognize CML which is claimed to be a dominant AGE in human serum albumin and in tissue proteins [99]. Another problem may be that factors in human serum interfere with the measurement [100].…”

Section: Markers Of Age and Problems With Current Assaysmentioning

confidence: 99%

The Clinical Relevance of Advanced Glycation Endproducts (AGE) and Recent Developments in Pharmaceutics to Reduce AGE Accumulation

Smit¹,

Lutgers

2004

CMC

116

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Advanced glycation endproducts (AGE) are a class of compounds resulting from glycation and oxidation of proteins, lipids or nucleic acids. Glycation is the non-enzymatic addition or insertion of saccharide derivatives to these molecules. This leads to the formation of intermediary Schiff bases and Amadori products and finally to irreversible AGE. This classical view has been modified in recent years with recognition of the importance of oxidative and carbonyl stress in endogenous AGE formation. AGE may also have exogenous sources, in certain foods and tobacco smoke. A whole class of specific and non-specific receptors binding AGE has been characterized. Apart from cross-linking of proteins by AGE, the effects of receptor stimulation contribute to the development of chronic complications of conditions like diabetes mellitus, renal failure, and atherosclerosis. Possible interventions to reduce the effects of AGE accumulation include AGE formation inhibitors or breakers, or receptor blockers, but possibly also dietary interventions. Some of the problems with current assay or diagnostic techniques, and several unresolved issues on the role of AGE in disease will be discussed. Our review will focus on the clinical and pharmaceutical implications of these developments.

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Section: Markers Of Age and Problems With Current Assaysmentioning

confidence: 99%

The Clinical Relevance of Advanced Glycation Endproducts (AGE) and Recent Developments in Pharmaceutics to Reduce AGE Accumulation

Smit¹,

Lutgers

2004

CMC

116

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“…Polylysine-HBr and human serum albumin (HSA) (fatty acid free) were obtained from Sigma Chemical Co., St. Louis, MO. Authentic CML was prepared as reported previously (13). All chemicals were purchased from Kanto Chemical Co. (Tokyo, Japan) unless otherwise stated.…”

Section: Methodsmentioning

confidence: 99%

“…Blueprint reaction by glycated human serum albumin. Glycated human serum albumin (G-HSA) was prepared as reported elsewhere (13). HSA or G-HSA at 300 L (10 mg/mL in 10 mM Na-phosphate buffer at pH 7.4) was mixed with 200 L of 10 mM Fe(III) nitrate solution, exposed to sunlight for 1 h and 20 mL of 1% potassium hexacyanoferrate(III) solution was added.…”

Section: Methodsmentioning

confidence: 99%

Sunlight Induces Nε-(Carboxymethyl)Lysine Formation from Glycated Polylysine–Iron(III) Complex¶

Sakurai

Fujimori

Ueda

et al. 2001

Photochem Photobiol

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Sunlight was found to strongly induce the formation of N epsilon-(carboxymethyl)lysine (CML) from glycated polylysine in the presence of Fe(III) ion. The initial step of this Fe(III)-catalyzed CML formation was noted to be similar to that of blueprint photography as was confirmed by the production of Turnbull's blue in sunlight-exposed glycated human serum albumin ferricyanide solution in the presence of Fe(III). Based on this, photoinduced oxidative C-C bond cleavage of the Amadori compound was assumed to be initiated by photochemical single electron transfer front ligand to Fe(III) in the Fe(III)-Amadori compound complex affording the Fe(II)-Amadori compound radical intermediate, which eventually yields either CML or active oxygen species. CML is thus a useful oxidative stress marker. The mechanism proposed here would explain the high accumulation of CML in lens protein and skin actinic elastosis.

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“…Above all, the first one is thought to represent a major pathway in vivo [26]. CML formation from Amadori product was accelerated by the addition of Fe 3+ [27]and was inhibited by the presence of chelators, reducing agents, or radical scavengers [28–30]. We recently demonstrated that hydroxyl radical generated by the reaction of Fe 2+ with H 2 O 2 mediates CML formation from Amadori compounds [30].…”

Section: Introductionmentioning

confidence: 99%

Conversion of Amadori product of Maillard reaction to N^ϵ‐(carboxymethyl)lysine in alkaline condition

et al. 1998

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N O -(carboxymethyl)lysine (CML) is known to be formed by oxidative cleavage of Amadori products between C-2 and C-3 of the carbohydrate chain. We report here that CML formation from Amadori compounds is highly accelerated under alkaline conditions. Incubation of glycated human serum albumin (HSA) in 0.1 N NaOH led to the formation of CML whereas glycated HSA reduced by NaCNBH Q or non-glycated HSA did not generate CML., a model compound of Amadori product, was converted to CML under alkaline conditions. CML level of human sera (n = 224) preincubated with 0.1 N NaOH correlated well with glycated albumin value (r = 0.912) and hemoglobin A1c (r = 0.797).z 1998 Federation of European Biochemical Societies.

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Identification of the Carboxymethyllysine Residue in the Advanced Stage of Glycated Human Serum Albumin.

Cited by 10 publications

References 1 publication

The Clinical Relevance of Advanced Glycation Endproducts (AGE) and Recent Developments in Pharmaceutics to Reduce AGE Accumulation

The Clinical Relevance of Advanced Glycation Endproducts (AGE) and Recent Developments in Pharmaceutics to Reduce AGE Accumulation

Sunlight Induces Nε-(Carboxymethyl)Lysine Formation from Glycated Polylysine–Iron(III) Complex¶

Conversion of Amadori product of Maillard reaction to N^ϵ‐(carboxymethyl)lysine in alkaline condition

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Identification of the Carboxymethyllysine Residue in the Advanced Stage of Glycated Human Serum Albumin.

Cited by 10 publications

References 1 publication

The Clinical Relevance of Advanced Glycation Endproducts (AGE) and Recent Developments in Pharmaceutics to Reduce AGE Accumulation

The Clinical Relevance of Advanced Glycation Endproducts (AGE) and Recent Developments in Pharmaceutics to Reduce AGE Accumulation

Sunlight Induces Nε-(Carboxymethyl)Lysine Formation from Glycated Polylysine–Iron(III) Complex¶

Conversion of Amadori product of Maillard reaction to Nϵ‐(carboxymethyl)lysine in alkaline condition

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Conversion of Amadori product of Maillard reaction to N^ϵ‐(carboxymethyl)lysine in alkaline condition