Age-related accumulation of Maillard reaction products in human articular cartilage collagen
| Autor: | Verzijl, N., Degroot, J., Oldehinkel, E., Bank, R. A., Thorpe, S. R., Baynes, J. W., Bayliss, M. T., Bijlsma, J. W., Lafeber, F. P., TeKoppele, J. M. |
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| Přispěvatelé: | Gaubius Laboratory, Div. Vasc./Connective Tissue Res., TNO Prevention and Health, PO Box 2215, 2301 CE Leiden, Netherlands, Other departments |
| Jazyk: | angličtina |
| Rok vydání: | 2000 |
| Předmět: |
collagen
Cartilage Articular Male Aging Biomedical Research tissue level arginine advanced glycation end product protein glycosylation protein cross linking Femur amino acid composition Child n carboxyethyllysine Skin Aged 80 and over adult article Age Factors Middle Aged n carxobymethyllysine unclassified drug aged bioaccumulation Cross-Linking Reagents priority journal Child Preschool protein degradation Female fluorescence Health Biology Pentosidine Adolescent Glycosylation End Products Advanced hydroxylysine Humans articular cartilage controlled study N(ε)-(carboxymethyl)lysine human Collagenases lysine human tissue color Maillard Reaction collagenase Spectrometry Fluorescence age tensile strength Cross-linking |
| Zdroj: | Biochemical Journal, 2, 350, 381-387 Biochemical journal, 350 Pt 2, 381-387. Portland Press Ltd. |
| ISSN: | 0264-6021 |
| Popis: | Non-enzymic modification of tissue proteins by reducing sugars, the so-called Maillard reaction, is a prominent feature of aging. In articular cartilage, relatively high levels of the advanced glycation end product (AGE) pentosidine accumulate with age. Higher pentosidine levels have been associated with a stiffer collagen network in cartilage. However, even in cartilage, pentosidine levels themselves represent |
| Databáze: | OpenAIRE |
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