Title
Age-related accumulation of Maillard reaction products in human articular cartilage collagen
Author
Verzijl, N.
de Groot, J.
Oldehinkel, E.
Bank, R.A.
Thorpe, S.R.
Baynes, J.W.
Bayliss, M.T.
Bijlsma, J.W.J.
Lafeber, F.P.J.G.
TeKoppele, J.M.
Gaubius Laboratory, Div. Vasc./Connective Tissue Res., TNO Prevention and Health, PO Box 2215, 2301 CE Leiden, Netherlands
Publication year
2000
Abstract
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 < 1 cross-link per 20 collagen molecules, and as such cannot be expected to contribute sub-stantially to the increase in collagen network stiffness. In the present study, we investigated a broad range of Maillard reaction products in cartilage collagen in order to determine whether pentosidine serves as an adequate marker for AGE levels. Not only did the well-characterized AGEs pentosidine, N(ε)-(carboxymethyl)lysine, and N(ε)-(carboxyethyl)lysine increase with age in cartilage collagen (all P < 0.0001), but also general measures of AGE cross-linking, such as browning and fluorescence (both P < 0.0001), increased. The levels of these AGEs are all higher in cartilage collagen than in skin collagen. As a functional measure of glycation the digestibility of articular collagen by bacterial collagenase was investigated; digestibility decreased linearly with age, proportional to the extent of glycation. Furthermore, the arginine content and the sum of the hydroxylysine and lysine content of cartilage collagen decrease significantly with age (P < 0.0001 and P < 0.01 respectively), possibly due to modification by the Maillard reaction. The observed relationship between glycation and amino acid modification has not been reported previously in vivo. Our present results indicate that extensive accumulation of a variety of Maillard reaction products occurs in cartilage collagen with age. Altogether our results support the hypothesis that glycation contributes to stiffer and more brittle cartilage with advancing age.
Subject
Health Biology
Biomedical Research
Advanced glycation end product
Aging
Cross-linking
N(ε)-(carboxymethyl)lysine
Pentosidine
advanced glycation end product
arginine
collagen
collagenase
hydroxylysine
lysine
n carboxyethyllysine
n carxobymethyllysine
pentosidine
unclassified drug
adolescent
adult
age
aged
aging
amino acid composition
article
articular cartilage
bioaccumulation
child
color
controlled study
fluorescence
human
human tissue
priority journal
protein cross linking
protein degradation
protein glycosylation
skin
tensile strength
tissue level
Adolescent
Adult
Age Factors
Aged
Aged, 80 and over
Aging
Arginine
Cartilage, Articular
Child
Child, Preschool
Collagen
Collagenases
Cross-Linking Reagents
Female
Femur
Glycosylation End Products, Advanced
Humans
Lysine
Maillard Reaction
Male
Middle Aged
Skin
Spectrometry, Fluorescence
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http://resolver.tudelft.nl/uuid:a3635b36-47b8-4921-8434-97044eac4394
DOI
https://doi.org/10.1042/0264-6021:3500381
TNO identifier
235646
ISSN
0264-6021
Source
Biochemical Journal, 350 (2), 381-387
Document type
article