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Structure elucidation of a senescence cross-link from human extracellular matrix. Implication of pentoses in the aging process.
  • D. Sell, V. Monnier
  • Chemistry, Medicine
  • The Journal of biological chemistry
  • 25 December 1989
The unexpected discovery of pentose-mediated protein cross-linking raises new questions concerning the aging process and suggests ribose or ribonucleotide metabolites as precursors. Expand
Relation between complications of type I diabetes mellitus and collagen-linked fluorescence.
The data suggest that there is an overall correlation between the severity of diabetic complications and cumulative glycemia over many years. Expand
Nonenzymatic browning in vivo: possible process for aging of long-lived proteins.
Although most proteins in living systems turn over with sufficient rapidity to avoid nonenzymatic browning, some, such as lens crystallins and skin collagen, are exceptionally long-lived and may be vulnerable. Expand
Advanced Maillard reaction end products are associated with Alzheimer disease pathology.
Evidence is presented that antibodies against two Maillard end products, pyrraline and pentosidine, immunocytochemically label neurofibrillary tangles and senile plaques in brain tissue from patients with Alzheimer disease contain modifications typical of advanced Maillard reaction end products. Expand
Glycation of mitochondrial proteins from diabetic rat kidney is associated with excess superoxide formation.
Posttranslational modifications of mitochondrial proteins by MGO may represent pathogenic events leading to mitochondria-induced oxidative stress in the kidney in chronic diabetes. Expand
Accelerated age-related browning of human collagen in diabetes mellitus.
Collagen adducts from aged and diabetic individuals had absorption and fluorescence spectra identical to those of collagen samples that underwent nonenzymatic browning with glucose in vitro, suggesting their likely occurrence throughout the body could explain the correlation between arterial stiffening, decreased joint mobility, and the severity of microvascular complications in type I diabetics. Expand
Nonenzymatic glycosylation, the Maillard reaction and the aging process.
  • V. Monnier
  • Chemistry, Medicine
  • Journal of gerontology
  • 1 July 1990
Mechanism of Protein Modification by Glyoxal and Glycolaldehyde, Reactive Intermediates of the Maillard Reaction (*)
It can be estimated that approximately 50% of the CML forming in a glucose/lysine system originates from oxidation of Amadori product, and 40-50% originizes from a pre-Amadori stage largely independent from glucose autoxidation. Expand
Cross‐Linking of the Extracellular Matrix by the Maillard Reaction in Aging and Diabetes: An Update on “a Puzzle Nearing Resolution”
It is concluded that, while oxidation might be important for Maillard reaction‐mediated cross‐linking via Strecker degradation and allysine formation, the single most important collagen cross-link known to date in diabetes and aging is glucosepane, a lysyl‐arginine cross‐link that forms under nonoxidative conditions. Expand
Radical AGEing in Alzheimer's disease
Findings suggest that age-related increases in oxidative stress and protein glycation either individually, or more probably in a synergistic manner, could, exclusive of the other theories or in concert with them, account for all aspects of Alzheimer's disease. Expand