Current Rheumatology Reports

, Volume 5, Issue 1, pp 33–40 | Cite as

Advanced glycation endproducts and osteoarthritis

  • Deborah M. Saudek
  • Jonathan Kay


Non-enzymatic glycation of proteins, such as collagen, results in the formation of advanced glycation endproducts (AGE). Advanced glycation endproducts result in pathologic stiffening of cartilage and extracellular matrix and accumulate with age. Pentosidine, an AGE, is present in serum, synovial fluid, and articular cartilage from patients with osteoarthritis (OA). However, AGE levels are not always increased, and may be decreased locally, in association with osteoarthritic pathology. The finding of pentosidine in articular cartilage of individuals with OA may not be specific for that disease, independent of chronologic age. Advanced glycation endproduct modification of normal articular cartilage increases its stiffness, increases chondrocyte-mediated proteoglycan degradation, reduces its susceptibility to matrix metalloproteinase-mediated degradation, and decreases proteoglycan synthesis by chondrocytes. These observations parallel findings in osteoarthritic cartilage, which suggests that AGE modification could contribute to the pathogenesis of OA. However, a causative link between AGEs and OA has not yet been established.


Articular Cartilage Synovial Fluid Pentosidine Proteoglycan Synthesis Human Articular Cartilage 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Current Science Inc 2003

Authors and Affiliations

  • Deborah M. Saudek
  • Jonathan Kay
    • 1
  1. 1.Rheumatology UnitMassachusetts General HospitalBostonUSA

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