Advanced glycation end-product pentosidine accumulates in various tissues of rats with high fructose intake
Language English Country Czech Republic Media print-electronic
Document type Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
PubMed
17298207
DOI
10.33549/physiolres.931093
PII: 1093
Knihovny.cz E-resources
- MeSH
- Aorta metabolism MeSH
- Arginine analogs & derivatives metabolism MeSH
- Endothelium, Vascular metabolism MeSH
- Dietary Carbohydrates metabolism MeSH
- Species Specificity MeSH
- Extracellular Matrix metabolism MeSH
- Fructose metabolism MeSH
- Hyperglycemia complications metabolism MeSH
- Hypertriglyceridemia complications metabolism MeSH
- Rats MeSH
- Skin metabolism MeSH
- Lysine analogs & derivatives metabolism MeSH
- Statistics, Nonparametric MeSH
- Protein Processing, Post-Translational physiology MeSH
- Rats, Inbred Lew MeSH
- Rats, Wistar MeSH
- Glycation End Products, Advanced metabolism MeSH
- Tendons metabolism MeSH
- Tissue Distribution MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Male MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Comparative Study MeSH
- Names of Substances
- Arginine MeSH
- Dietary Carbohydrates MeSH
- Fructose MeSH
- Lysine MeSH
- pentosidine MeSH Browser
- Glycation End Products, Advanced MeSH
The slowly metabolized proteins of the extracellular matrix, typically collagen and elastin, accumulate reactive metabolites through uncontrolled non-enzymatic reactions such as glycation or the products arising from the reaction of unsaturated long chain fatty acid metabolites (possessing aldehydic groups). A typical example of these non-enzymatic changes is the formation of advanced glycation end-products (AGEs), resulting from the reaction of carbohydrates with the free amino group of proteins. The accumulation of AGEs and the resulting structural alterations cause altered tissue properties (increased stiffness, reduced elasticity) that contribute to their reduced catabolism and to their aging. Posttranslational nonenzymatic modifications of the proteins of the extracellular matrix (the formation of a typical AGE product--pentosidine) were studied in three types of tissue of three rat strains subjected to a high-fructose diet. Chronic (three-week) hyperglycemia (resulting from fructose loading) caused a significant increase in pentosidine concentration mainly in the aorta and skin of the three rat strains (Lewis, Wistar and hereditary hypertriglyceridemic rats).
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