Title
Accumulation of advanced glycation end products decreases collagen turnover by bovine chondrocytes
Author
de Groot, J.
Verzijl, N.
Budde, M.
Bijlsma, J.W.J.
Lafeber, F.P.J.G.
TeKoppele, J.M.
Gaubius Instituut
Publication year
2001
Abstract
The integrity of the collagen network is essential for articular cartilage to fulfill its function in load support and distribution. Damage to the collagen network is one of the first characteristics of osteoarthritis. Since extensive collagen damage is considered irreversible, it is crucial that chondrocytes maintain a functional collagen network. We investigated the effects of advanced glycation end products (AGEs) on the turnover of collagen by articular cartilage chondrocytes. Increased AGE levels (by culturing in the presence of ribose) resulted in decreased collagen synthesis (P < 0.05) and decreased MMP-mediated collagen degradation (P < 0.02). The latter could be attributed to increased resistance of the collagen network to MMPs (P < 0.05) as well as the decreased production of MMPs by chondrocytes (P < 0.02). Turnover of a protein is determined by its synthesis and degradation rates and therefore these data indicate that collagen turnover is decreased at enhanced AGE levels. Since AGE levels in human cartilage increase ∼50 fold between age 20 and 80, cartilage collagen turnover likely decreases with increasing age. Impaired collagen turnover adversely affects the capacity of chondrocytes to remodel and/or repair its extracellular matrix. Consequently, age-related accumulation of AGE (via decreased collagen turnover) may contribute to the development of cartilage damage in osteoarthritis. © 2001 Academic Press.
Subject
Biology
Biomedical Research
Advanced glycation end product
Alginate culture
Cartilage
Chondrocyte
Collagen
Matrix metalloproteinase
Turnover
advanced glycation end product
alginic acid
collagen
matrix metalloproteinase
ribose
animal cell
article
articular cartilage
cartilage cell
cattle
cell culture
collagen defect
collagen degradation
collagen synthesis
controlled study
culture medium
enzyme activity
extracellular matrix
nonhuman
osteoarthritis
priority journal
reaction time
Animals
Cattle
Cells, Cultured
Chondrocytes
Collagen
Enzyme Precursors
Extracellular Matrix
Glycosylation End Products, Advanced
Matrix Metalloproteinases
Osteoarthritis
Ribose
Bovinae
To reference this document use:
http://resolver.tudelft.nl/uuid:037622e8-fc46-4dd5-96c3-e3a68c77bdb2
DOI
https://doi.org/10.1006/excr.2001.5224
TNO identifier
236132
ISSN
0014-4827
Source
Experimental Cell Research, 266 (2), 303-310
Document type
article