(Q44353029)

English

Increased level of glycoxidation product N(epsilon)-(carboxymethyl)lysine in rat serum and urine proteins with aging: link with glycoxidative damage accumulation in kidney

scientific article published in March 2003

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scholarly article

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Europe PubMed Central

PubMed publication ID

2 December 2017

Increased level of glycoxidation product N(epsilon)-(carboxymethyl)lysine in rat serum and urine proteins with aging: link with glycoxidative damage accumulation in kidney (English)

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

Bertrand Friguet

3

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

author name string

Maud Hamelin

1

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Europe PubMed Central

PubMed publication ID

2 December 2017

Caroline Borot-Laloi

2

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Europe PubMed Central

PubMed publication ID

2 December 2017

Hilaire Bakala

4

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Europe PubMed Central

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2 December 2017

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publication date

1 March 2003

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2 December 2017

number of pages

8

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based on heuristic

inferred from page(s)

Archives of Biochemistry and Biophysics

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Europe PubMed Central

PubMed publication ID

2 December 2017

411

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Europe PubMed Central

PubMed publication ID

2 December 2017

2

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Europe PubMed Central

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2 December 2017

215-222

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Europe PubMed Central

PubMed publication ID

2 December 2017

The Maillard reaction in vivo

1 reference

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Role of oxidative stress in development of complications in diabetes

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Oxidation conspires with glycation to generate noxious advanced glycation end products in renal failure

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Mechanism of the degradation of non-enzymatically glycated proteins under physiological conditions. Studies with the model fructosamine, N epsilon-(1-deoxy-D-fructos-1-yl)hippuryl-lysine.

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Mechanism of protein modification by glyoxal and glycolaldehyde, reactive intermediates of the Maillard reaction

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The advanced glycation end product, Nepsilon-(carboxymethyl)lysine, is a product of both lipid peroxidation and glycoxidation reactions

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N (epsilon)-(carboxymethyl)lysine protein adduct is a major immunological epitope in proteins modified with advanced glycation end products of the Maillard reaction

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N epsilon-(carboxymethyl)lysine is a dominant advanced glycation end product (AGE) antigen in tissue proteins

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Early light microscopic changes in chronic progressive nephrosis in several strains of aging laboratory rats

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A simple, versatile, nondisruptive method for the isolation of morphologically and chemically pure basement membranes from several tissues

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Mechanisms for the formation of glycoxidation products in end-stage renal disease

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Macrophage scavenger receptor mediates the endocytic uptake and degradation of advanced glycation end products of the Maillard reaction

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Novel macrophage receptor for glucose-modified proteins is distinct from previously described scavenger receptors

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Immunocytochemical detection of advanced glycated end products in rat renal tissue as a function of age and diabetes

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N(epsilon)-(carboxymethyl)lysine adducts of proteins are ligands for receptor for advanced glycation end products that activate cell signaling pathways and modulate gene expression

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Age-dependent accumulation of N epsilon-(carboxymethyl)lysine and N epsilon-(carboxymethyl)hydroxylysine in human skin collagen

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Accumulation of Maillard reaction products in skin collagen in diabetes and aging

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Oxidative alterations in the experimental glycation model of diabetes mellitus are due to protein-glucose adduct oxidation. Some fundamental differences in proposed mechanisms of glucose oxidation and oxidant production

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Protein glycation and oxidative stress in diabetes mellitus and ageing

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Oxidation-reduction properties of methylglyoxal-modified protein in relation to free radical generation

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Specificity of age-related carbonylation of plasma proteins in the mouse and rat.

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Metal ion-catalyzed oxidation of proteins: biochemical mechanism and biological consequences

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Glycation of albumin with aging and diabetes in rats: changes in its renal handling

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Multi-metal binding site of serum albumin

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Identifiers

10.1016/S0003-9861(02)00735-X

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

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