Advanced glycation: implications in tissue damage and disease

Gasser, Anna and Forbes, Josephine M. (2008) Advanced glycation: implications in tissue damage and disease. Protein and Peptide Letters, 15 4: 385-391. doi:10.2174/092986608784246515


Author Gasser, Anna
Forbes, Josephine M.
Title Advanced glycation: implications in tissue damage and disease
Journal name Protein and Peptide Letters   Check publisher's open access policy
ISSN 0929-8665
1875-5305
Publication date 2008
Sub-type Critical review of research, literature review, critical commentary
DOI 10.2174/092986608784246515
Open Access Status Not yet assessed
Volume 15
Issue 4
Start page 385
End page 391
Total pages 7
Place of publication Bussum, Netherlands
Publisher Bentham Science Publishers
Language eng
Abstract Advanced glycation end products (AGEs) are formed from the non-enzymatic reaction between reducing sugars and amine residues on proteins, lipoproteins or nucleic acids. AGEs are found on long-lived proteins and their tissue accumulation is associated with normal ageing. The formation of AGEs can be accelerated in certain pathological conditions such as diabetes where hyperglycaemia is present. AGE modification of proteins can lead to alterations of normal function by binding to intracellular or extracellular cell components, or through receptor binding. This consequently can initiate a cascade of events, which includes the activation of signal transduction pathways, which activate inflammatory responses causing tissue damage. Such tissue injury contributes to the development of microvascular complications and is of particular relevance in diabetes where interventions to reduce the accumulation of AGEs is desirable.
Keyword Superoxide dismutase
Hyperglycaemia
Reactive oxygen species
Type 2 diabetes
AGE receptors
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Critical review of research, literature review, critical commentary
Collection: School of Medicine Publications
 
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