Mechanism of formation of the putative advanced glycosylation end product and protein cross-link 2-(2-furoyl)-4(5)-(2-furanyl)-1H-imidazole.

Njoroge, F. George; Fernandes, A.; Monnier, Vincent M.

doi:10.1016/s0021-9258(18)38020-7

Cited by 105 publications

(6 citation statements)

References 20 publications

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“…Native and all glycated HSA samples were reduced with NaBH 4 in 20 mM PBS at pH 7.4, as described previously. 37 Slow addition of 1 N HCl was used to remove excess borohydride.…”

Section: Reduction Of Amadori Adduct By Nabhmentioning

confidence: 99%

Impact of in vitro non-enzymatic glycation on biophysical and biochemical regimes of human serum albumin: relevance in diabetes associated complications

2015

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Early glycation involves attachment of glucose on 3-NH 2 of lysine residues. Human serum albumin (HSA), a lysine rich protein, is highly prone to non-enzymatic glycation. In this study, the effect of different concentrations of glucose on HSA through early glycation was assessed by various physicochemicaltechniques. An early glycation product Amadori HSA was estimated by colorimetric method, nitro blue tetrazolium (NBT) and thiobarbituric acid assay (TBA). The conformational changes were confirmed by UV-visible spectroscopy, tryptophan fluorescence quenching, circular dichroism (CD), and sodium dodecyl sulphate poly acrylamide gel electrophoresis (SDS-PAGE). Biochemical alterations in Amadori-HSA were analyzed by NaBH 4 reduction, increased carbonyl content and decrease in free lysine, arginine and sulfhydryl groups. Most studies have reported the structural changes in protein due to AGEs or Amadori protein at a particular glucose concentration; to the best of our knowledge, no reports have been published comparing the physicochemical changes in HSA due to early glycation within a range of glucose concentrations. In the present study, the investigations confirmed the structural and biochemical alterations in Amadori-HSA which is directly proportional to glucose concentration. This might interfere with the normal function of HSA and can contribute to the progression of diabetes and its associated complications. Amadori modified HSA might be used as a biomarker for early detection of diabetes and be beneficial in preventing the diabetic complications at early stages of diabetes. In this context, this study provides additional information about biochemical and biophysical changes occurring in Amadori-HSA within the glucose range upon early glycation.

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“…Native and all glycated HSA samples were reduced with NaBH 4 in 20 mM PBS at pH 7.4, as described previously. 37 Slow addition of 1 N HCl was used to remove excess borohydride.…”

Section: Reduction Of Amadori Adduct By Nabhmentioning

confidence: 99%

Impact of in vitro non-enzymatic glycation on biophysical and biochemical regimes of human serum albumin: relevance in diabetes associated complications

2015

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mentioning

confidence: 99%

“…However, a role of FFI in protein cross-linking is discounted by results of studies showing that FFI is not a component of glycated proteins but is an artifactual product of the procedures used in its isolation (Horiuchi et al, 1988;Njoroge et al, 1988). A plausible mechanism for the formation of FFI from unlinked glycated proteins has been presented (Njoroge et al, 1988). It is noteworthy that, in addition to glucose, reactions with fructose (Suárez et al, 1989), mannose and frucose (Davis et al, 1989), and glucose 6-phosphate (Beswick & Harding, 1987) have been shown to glycate proteins.…”

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confidence: 99%

Covalent modification reactions are marking steps in protein turnover

Stadtman¹

1990

Biochemistry

203

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“…DDMP Formation from Other Amadori Compounds. Three kinds of Amadori compounds, fructose-3-alanine, fructose-p-toluidine, and fructose-IV"-terf-Boclysine, were prepared by the procedures set out in the literature (Anet, 1957;Lowy and Borsook, 1956;Njoroge et al, 1988). They were heated at 150 °C for 10 min, and the degradation products were analyzed by HPLC.…”

Section: Resultsmentioning

confidence: 99%

“…N"-(tert-Butoxycarbonyl)lysine (N"-t-Boc-lysine) was obtained from Sigma Chemical Co. (St. Louis, MO). l-Deoxy-l-/S-alanino-Dfructose (fructose-/S-alanine), 1-deoxy-l-p-toluidino-D-fructose (fructose-p-toluidine), and l-deoxy-l-Na-(terf-butoxycarbonyl)lysino-D-fructose (fructose-/V"-t-Boc-lysine) were prepared according to the procedures of Anet (1957), Lowy and Borsook (1956), and Njoroge et al (1988), respectively. Other reagents of the best grades were commercially available.…”

Section: Methodsmentioning

confidence: 99%

Formation of 2,3-Dihydro-3,5-dihydroxy-6-methyl-4(H)-pyran-4-one from Fructose and .beta.-Alanine under Conditions Used for Baking

Nishibori¹,

Kawakishi²

1994

J. Agric. Food Chem.

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Mechanism of formation of the putative advanced glycosylation end product and protein cross-link 2-(2-furoyl)-4(5)-(2-furanyl)-1H-imidazole.

Cited by 105 publications

References 20 publications

Impact of in vitro non-enzymatic glycation on biophysical and biochemical regimes of human serum albumin: relevance in diabetes associated complications

Impact of in vitro non-enzymatic glycation on biophysical and biochemical regimes of human serum albumin: relevance in diabetes associated complications

Covalent modification reactions are marking steps in protein turnover

Formation of 2,3-Dihydro-3,5-dihydroxy-6-methyl-4(H)-pyran-4-one from Fructose and .beta.-Alanine under Conditions Used for Baking

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