Advanced glycation endproducts and osteoarthritis

UMMS Affiliation

Department of Medicine, Division of Rheumatology

Publication Date


Document Type



Aging; Glycosylation End Products, Advanced; Humans; Osteoarthritis; Receptors, Immunologic


Musculoskeletal Diseases | Rheumatology | Skin and Connective Tissue Diseases


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.

DOI of Published Version



Curr Rheumatol Rep. 2003 Feb;5(1):33-40. 10.1007/s11926-003-0081-x Link to article on publisher's site

Journal/Book/Conference Title

Current rheumatology reports


At the time of publication, Jonathan Kay was not yet affiliated with the University of Massachusetts Medical School.

Related Resources

Link to Article in PubMed

PubMed ID