Skip to main content
Annals of the Rheumatic Diseases logoLink to Annals of the Rheumatic Diseases
. 1987 May;46(5):363–369. doi: 10.1136/ard.46.5.363

Neutral metalloproteases and age related changes in human articular cartilage.

J Martel-Pelletier, J P Pelletier
PMCID: PMC1002142  PMID: 3296969

Abstract

A decrease in proteoglycan (Pg) content and disturbances in the collagen network have been reported in aging cartilage. This study aims to determine whether these changes are associated with proteolytic enzymes such as neutral metalloproteases. Eighty lateral tibial plateaus were collected from subjects after death. The age, topographical area, and lesion severity (macroscopic grading) of each specimen were noted and the effects of neutral metallo-Pg-degrading and collagenolytic enzymes on these specimens were compared. The specimens were divided into two age groups: 20-50 years (group 1) and greater than 50 years (group 2). They were selected from both weight bearing and non-weight bearing areas. In some cartilage tissues the superficial layer was separated from the deep zone. Our data for the two neutral metalloenzymes examined showed: no correlation between enzyme activity and age when the specimens were of the same grade and a statistically significant rise in the enzyme levels of the older specimens, which increased as the lesions progressed. Neutral metallo-Pg-degrading enzyme activity was higher in non-weight bearing areas than in weight bearing areas, and this reached a statistical difference in the older cartilage with advanced lesions. The Pg-degrading enzyme activity was raised in the superficial layers of damaged cartilage tissue. Our data suggest that neutral metalloproteases are closely associated with the appearance and progression of the changes seen in aging cartilage.

Full text

PDF
363

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bayliss M. T., Ali S. Y. Age-related changes in the composition and structure of human articular-cartilage proteoglycans. Biochem J. 1978 Dec 15;176(3):683–693. doi: 10.1042/bj1760683. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. COLLINS D. H., McELLIGOTT T. F. Sulphate (35SO4) uptake by chondrocytes in relation to histological changes in osteoarthritic human articular cartilage. Ann Rheum Dis. 1960 Dec;19:318–330. doi: 10.1136/ard.19.4.318. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Inerot S., Heinegård D., Audell L., Olsson S. E. Articular-cartilage proteoglycans in aging and osteoarthritis. Biochem J. 1978 Jan 1;169(1):143–156. doi: 10.1042/bj1690143. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Jones I. L., Lemperg R. The glycosaminoglycans of human articular cartilage: molecular weight distribution of chondroitin sulphate in different layers in the adult individual. Clin Orthop Relat Res. 1978 Jul-Aug;(134):364–370. [PubMed] [Google Scholar]
  5. Mankin H. J., Lippiello L. Biochemical and metabolic abnormalities in articular cartilage from osteo-arthritic human hips. J Bone Joint Surg Am. 1970 Apr;52(3):424–434. [PubMed] [Google Scholar]
  6. Martel-Pelletier J., Pelletier J. P., Cloutier J. M., Howell D. S., Ghandur-Mnaymneh L., Woessner J. F., Jr Neutral proteases capable of proteoglycan digesting activity in osteoarthritic and normal human articular cartilage. Arthritis Rheum. 1984 Mar;27(3):305–312. doi: 10.1002/art.1780270310. [DOI] [PubMed] [Google Scholar]
  7. Martel-Pelletier J., Pelletier J. P. Degradative changes in human articular cartilage induced by chemotherapeutic agents. J Rheumatol. 1986 Feb;13(1):164–174. [PubMed] [Google Scholar]
  8. Meachim G. Light microscopy of Indian ink preparations of fibrillated cartilage. Ann Rheum Dis. 1972 Nov;31(6):457–464. doi: 10.1136/ard.31.6.457. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Mort J. S., Poole A. R., Roughley P. J. Age-related changes in the structure of proteoglycan link proteins present in normal human articular cartilage. Biochem J. 1983 Jul 15;214(1):269–272. doi: 10.1042/bj2140269. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Muir H., Bullough P., Maroudas A. The distribution of collagen in human articular cartilage with some of its physiological implications. J Bone Joint Surg Br. 1970 Aug;52(3):554–563. [PubMed] [Google Scholar]
  11. Nojima T., Towle C. A., Mankin H. J., Treadwell B. V. Secretion of higher levels of active proteoglycanases from human osteoarthritic chondrocytes. Arthritis Rheum. 1986 Feb;29(2):292–295. doi: 10.1002/art.1780290219. [DOI] [PubMed] [Google Scholar]
  12. Pelletier J. P., Martel-Pelletier J., Altman R. D., Ghandur-Mnaymneh L., Howell D. S., Woessner J. F., Jr Collagenolytic activity and collagen matrix breakdown of the articular cartilage in the Pond-Nuki dog model of osteoarthritis. Arthritis Rheum. 1983 Jul;26(7):866–874. doi: 10.1002/art.1780260708. [DOI] [PubMed] [Google Scholar]
  13. Pelletier J. P., Martel-Pelletier J. Cartilage degradation by neutral proteoglycanases in experimental osteoarthritis. Suppression by steroids. Arthritis Rheum. 1985 Dec;28(12):1393–1401. doi: 10.1002/art.1780281212. [DOI] [PubMed] [Google Scholar]
  14. Pelletier J. P., Martel-Pelletier J., Howell D. S., Ghandur-Mnaymneh L., Enis J. E., Woessner J. F., Jr Collagenase and collagenolytic activity in human osteoarthritic cartilage. Arthritis Rheum. 1983 Jan;26(1):63–68. doi: 10.1002/art.1780260110. [DOI] [PubMed] [Google Scholar]
  15. Plaas A. H., Sandy J. D. Age-related decrease in the link-stability of proteoglycan aggregates formed by articular chondrocytes. Biochem J. 1984 May 15;220(1):337–340. doi: 10.1042/bj2200337. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Roughley P. J., White R. J. Age-related changes in the structure of the proteoglycan subunits from human articular cartilage. J Biol Chem. 1980 Jan 10;255(1):217–224. [PubMed] [Google Scholar]
  17. Roughley P. J., White R. J., Poole A. R. Identification of a hyaluronic acid-binding protein that interferes with the preparation of high-buoyant-density proteoglycan aggregates from adult human articular cartilage. Biochem J. 1985 Oct 1;231(1):129–138. doi: 10.1042/bj2310129. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Roughley P. J., White R. J., Santer V. Comparison of proteoglycans extracted from high and low weight-bearing human articular cartilage, with particular reference to sialic acid content. J Biol Chem. 1981 Dec 25;256(24):12699–12704. [PubMed] [Google Scholar]
  19. SILBERBERG R., SILBERBERG M., VOGEL A., WETTSTEIN W. Ultrastructure of articular cartilage of mice of various ages. Am J Anat. 1961 Nov;109:251–275. doi: 10.1002/aja.1001090304. [DOI] [PubMed] [Google Scholar]
  20. Santer V., White R. J., Roughley P. J. Proteoglycans from normal and degenerate cartilage of the adult human tibial plateau. Arthritis Rheum. 1981 May;24(5):691–700. doi: 10.1002/art.1780240510. [DOI] [PubMed] [Google Scholar]
  21. Venn M. F. Variation of chemical composition with age in human femoral head cartilage. Ann Rheum Dis. 1978 Apr;37(2):168–174. doi: 10.1136/ard.37.2.168. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. WOESSNER J. F., Jr The determination of hydroxyproline in tissue and protein samples containing small proportions of this imino acid. Arch Biochem Biophys. 1961 May;93:440–447. doi: 10.1016/0003-9861(61)90291-0. [DOI] [PubMed] [Google Scholar]

Articles from Annals of the Rheumatic Diseases are provided here courtesy of BMJ Publishing Group

RESOURCES