scholarly journals Age-related accumulation of Maillard reaction products in human articular cartilage collagen

2000 ◽  
Vol 350 (2) ◽  
pp. 381-387 ◽  
Author(s):  
Nicole VERZIJL ◽  
Jeroen DEGROOT ◽  
Esther OLDEHINKEL ◽  
Ruud A. BANK ◽  
Suzanne R. THORPE ◽  
...  

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 substantially 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, Nε-(carboxymethyl)lysine, and Nε-(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.

2000 ◽  
Vol 350 (2) ◽  
pp. 381 ◽  
Author(s):  
Nicole VERZIJL ◽  
Jeroen DEGROOT ◽  
Esther OLDEHINKEL ◽  
Ruud A. BANK ◽  
Suzanne R. THORPE ◽  
...  

1998 ◽  
Vol 330 (1) ◽  
pp. 345-351 ◽  
Author(s):  
Ruud A. BANK ◽  
Michael T. BAYLISS ◽  
Floris P. J. G. LAFEBER ◽  
Alice MAROUDAS ◽  
Johan M. TEKOPPELE

A biomechanical failure of the collagen network is postulated in many hypotheses of the development of osteoarthritis with advancing age. Here we investigate the accumulation of non-enzymatic glycation (NEG) products in healthy human articular cartilage, its relation to tissue remodelling and its role in tissue stiffening. Pentosidine levels were low up to age 20 years, and increased linearly after this age. This indicates extensive tissue remodelling at young age, and slow turnover of collagen after maturity has been reached. The slow remodelling is supported by the finding that enzymatic modifications of collagen (hydroxylysine, hydroxylysylpyridinoline, and lysylpyridinoline) were not related to age. The high remodelling is supported by levels of the crosslink lysylpyridinoline (LP) as a function of distance from the articular surface. LP was highest at the surface in mature cartilage (> 20 years), whereas in young cartilage (< 10 years) the opposite was seen; highest levels were close to the bone. LP levels in cartilage sections at age 14 years are high at the surface and close to the bone, but they are low in the middle region. This indicates that maturation of cartilage in the second decade of life starts in the upper half of the tissue, and occurs last in the tissue close to the bone. The effect of NEG products on instantaneous deformation of cartilage was investigated as a functional of topographical variations in pentosidine levels in vivo and in relation to in vitro induced NEG. Consistently, higher pentosidine levels were associated with a stiffer collagen network. A stiffer and more crosslinked collagen network may become more brittle and more prone to fatigue.


1993 ◽  
Vol 91 (6) ◽  
pp. 2463-2469 ◽  
Author(s):  
D G Dyer ◽  
J A Dunn ◽  
S R Thorpe ◽  
K E Bailie ◽  
T J Lyons ◽  
...  

2016 ◽  
Vol 196 ◽  
pp. 204-210 ◽  
Author(s):  
Mariela Patrignani ◽  
Gustavo Juan Rinaldi ◽  
Cecilia Elena Lupano

2021 ◽  
pp. 112315
Author(s):  
Benyang Wu ◽  
Xiaoyan Chai ◽  
Aiming He ◽  
Zhen Huang ◽  
Sheng Chen ◽  
...  

1985 ◽  
Vol 16 (1) ◽  
pp. 37-47 ◽  
Author(s):  
Rickard Öste ◽  
Per Sjödin ◽  
Margaretha Jägerstad ◽  
Inger Björck ◽  
Arne Dahlqvist

1992 ◽  
Vol 663 (1 Aging and Cel) ◽  
pp. 421-422 ◽  
Author(s):  
D. G. DYER ◽  
J. A. DUNN ◽  
S. R. THORPE ◽  
T. J. LYONS ◽  
D. R. MCCANCE ◽  
...  

1999 ◽  
Vol 82 (6) ◽  
pp. 489-495 ◽  
Author(s):  
Jennifer M. Ames ◽  
Anthony Wynne ◽  
Andrea Hofmann ◽  
Saskia Plos ◽  
Glenn R. Gibson

The Maillard reaction produces coloured, macromolecular materials (melanoidins) in a variety of foods, on heating. Significant quantities may enter the human gut on a daily basis, but there is little information on their metabolism in the human colon. As the large bowel contains a diverse population of bacteria involved in normal bowel function, it is possible that melanoidins are metabolized therein. Depending on the bacteria involved, there may be disease or health implications. The aim of the present study was to usein vitromodels to determine the digestibility of melanoidins and the effect of melanoidins on colonic bacteria in the gastrointestinal tract. Melanoidins were prepared and the effects of simulated upper-gut secretions on their stability determined in a model system. The effects of faecal bacteria were also determined, in batch culture, with a combination of phenotypic and genotypic (probes) criteria being used to identify the microbial diversity involved. Simulation of peptic and pancreatic digestion showed that the melanoidins did not produce detectable amounts of low-molecular-mass degradation products. However, melanoidins affected the growth of gut bacteria during mixed culture growth. The effect was to cause a non-specific increase in the anaerobic bacteria enumerated. Thisin vitrostudy indicates that melanoidins can affect the growth of human large-bowel bacteria and serves to demonstrate possible effects that may occurin vivo. Given the large and varied number of food items that contain Maillard reaction products, this may have relevance for lower-gut health.


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