An investigation of the proteoglycan metabolism of mature equine articular cartilage and its regulation by interleukin-1.
The effect of human recombinant interleukin-1 beta (rhIL-1 beta) on proteoglycan metabolism was investigated in cultures of full thickness explants of articular cartilage from horses 3-21 years of age. Proteoglycan synthesis was inhibited at all ages but no alteration in the hydrodynamic size or electrophoretic heterogeneity was observed in proteoglycan isolated from rhIL-1 beta stimulated cartilage. The sulphation pattern of the newly synthesised proteoglycan molecules was, however, significantly affected by the presence of the peptide regulatory factor. Interleukin-1 had no effect on the rate of turnover of newly synthesised or endogenous proteoglycans in mature equine articular cartilage and did not influence the structure of proteoglycan fragments released into the culture medium. These observations suggest that IL-1, released into synovial fluid during inflammation, may modify the proteoglycan composition of normal equine cartilage not by stimulating catabolic enzymes capable of degrading the resident proteoglycans but by promoting the deposition of a reduced number of newly synthesised proteoglycan molecules of abnormal composition.
Platt
D
D
Kennedy Institute of Rheumatology, Hammersmith, London, UK.
Bayliss
M T
MT
D000818:Animals; D002358:Cartilage, Articular / Q000737:chemistry / Q000166:cytology / Q000378:metabolism*; D002478:Cells, Cultured; D004305:Dose-Response Relationship, Drug; D004591:Electrophoresis, Polyacrylamide Gel / Q000662:veterinary; D006736:Horses / Q000378:metabolism*; D006801:Humans; D007375:Interleukin-1 / Q000494:pharmacology* / Q000502:physiology; D011509:Proteoglycans / Q000032:analysis / Q000378:metabolism*; D011994:Recombinant Proteins / Q000494:pharmacology
D007375:Interleukin-1; D011509:Proteoglycans; D011994:Recombinant Proteins