Literature DB >> 1858425

[The significance of the Maillard reaction in human physiology].

E Schleicher1.   

Abstract

More than 50 years after Maillard's original paper describing the reaction of amino acids with glucose it was found that this reaction also occurs under physiological conditions in the human body. Initially, it was discovered that human hemoglobin contains protein-bound Amadori-products that are increased in diabetic patients with elevated blood glucose levels. Measurements of fructosylated hemoglobin are now widely used as an index of glycemia in diabetes. It was soon recognized that this postribosomal modification is common to other proteins in vivo like albumin, lens crystallins, proteins of the clotting cascade, collagens, lipoproteins, proteins of the cell membrane, and others. This may lead to alterations in structure and function of the respective protein. Later, the realization that long-lived proteins become browned, fluorescent, and insoluble with age, and at an accelerated rate in diabetes, suggested that later stages of the Maillard reaction might proceed in vivo and contribute to some of the pathophysiology associated with both aging and diabetes. Although the contribution of the Maillard products to the development of diabetic late complications is not fully understood, attempts are being made to prevent formation of late Maillard product with aminoguanidine, a drug currently under clinical testing.

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Year:  1991        PMID: 1858425     DOI: 10.1007/bf01910729

Source DB:  PubMed          Journal:  Z Ernahrungswiss        ISSN: 0044-264X


  39 in total

1.  Quantitation of lysine-bound glucose of normal and diabetic erythrocyte membranes by HPLC analysis of furosine [ epsilon-N(L-furoylmethyl)-L-lysine].

Authors:  E Schleicher; L Scheller; O H Wieland
Journal:  Biochem Biophys Res Commun       Date:  1981-04-15       Impact factor: 3.575

2.  Glucosylation of low-density lipoproteins to an extent comparable to that seen in diabetes slows their catabolism.

Authors:  U P Steinbrecher; J L Witztum
Journal:  Diabetes       Date:  1984-02       Impact factor: 9.461

3.  Kinetic analysis of glycation as a tool for assessing the half-life of proteins.

Authors:  E Schleicher; O H Wieland
Journal:  Biochim Biophys Acta       Date:  1986-10-29

4.  Fructosamine: a new approach to the estimation of serum glycosylprotein. An index of diabetic control.

Authors:  R N Johnson; P A Metcalf; J R Baker
Journal:  Clin Chim Acta       Date:  1983-01-07       Impact factor: 3.786

5.  Accelerated age-related browning of human collagen in diabetes mellitus.

Authors:  V M Monnier; R R Kohn; A Cerami
Journal:  Proc Natl Acad Sci U S A       Date:  1984-01       Impact factor: 11.205

6.  Limited nonenzymatic glucosylation of low-density lipoprotein does not alter its catabolism in tissue culture.

Authors:  E Schleicher; B Olgemöller; J Schön; T Dürst; O H Wieland
Journal:  Biochim Biophys Acta       Date:  1985-08-30

7.  Glycosylation of human fibrinogen in vivo.

Authors:  A Lütjens; A A te Velde; E A vd Veen; J vd Meer
Journal:  Diabetologia       Date:  1985-02       Impact factor: 10.122

8.  Nonenzymatic glycosylation of bovine lens crystallins. Effect of aging.

Authors:  S H Chiou; L T Chylack; W H Tung; H F Bunn
Journal:  J Biol Chem       Date:  1981-05-25       Impact factor: 5.157

9.  Measurement of glycosylated amino acids and peptides from urine of diabetic patients using affinity chromatography.

Authors:  M Brownlee; H Vlassara; A Cerami
Journal:  Diabetes       Date:  1980-12       Impact factor: 9.461

10.  Nonenzymatic glycation of fibronectin and alterations in the molecular association of cell matrix and basement membrane components in diabetes mellitus.

Authors:  J F Tarsio; B Wigness; T D Rhode; W M Rupp; H Buchwald; L T Furcht
Journal:  Diabetes       Date:  1985-05       Impact factor: 9.461

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  1 in total

Review 1.  [The effect of Maillard reaction products on enzyme reactions].

Authors:  D Schumacher; L W Kroh
Journal:  Z Ernahrungswiss       Date:  1996-09
  1 in total

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