Matrix Metalloproteinases in Arthritic Disease

Overview

Journal Arthritis Res

Specialty Rheumatology

Date 2002 Jul 12

PMID 12110122

Citations 110

Authors

Gillian Murphy

Vera Knauper

Susan Atkinson

George Butler

William English

Mike Hutton

Jan Stracke

Ian Clark

Affiliations

Soon will be listed here.

Abstract

The role of matrix metalloproteinases in the degradative events invoked in the cartilage and bone of arthritic joints has long been appreciated and attempts at the development of proteinase inhibitors as potential therapeutic agents have been made. However, the spectrum of these enzymes orchestrating connective tissue turnover and general biology is much larger than anticipated. Biochemical studies of the individual members of the matrix metalloproteinase family are now underway, ultimately leading to a more detailed understanding of the function of their domain structures and to defining their specific role in cellular systems and the way that they are regulated. Coupled with a more comprehensive and detailed study of proteinase expression in different cells of joint tissues during the progress of arthritic diseases, it will be possible for the future development and application of highly specific proteinase inhibitors to be directed at specific key cellular events.

Citing Articles

Effect of the novel anti-NGF monoclonal antibody DS002 on the metabolomics of pain mediators, cartilage and bone.

Jin D, Yang H, Chen Z, Hong Y, Ma H, Xu Z Front Pharmacol. 2024; 15:1396790.

PMID: 39188953 PMC: 11345146. DOI: 10.3389/fphar.2024.1396790.

Unveiling the bioinformatic genes and their involved regulatory mechanisms in type 2 diabetes combined with osteoarthritis.

Mao G, Xu W, Wan L, Wang H, Xu S, Zhang L Front Immunol. 2024; 15:1353915.

PMID: 39176085 PMC: 11338775. DOI: 10.3389/fimmu.2024.1353915.

The role of inflammatory mediators and matrix metalloproteinases (MMPs) in the progression of osteoarthritis.

Mukherjee A, Das B Biomater Biosyst. 2024; 13:100090.

PMID: 38440290 PMC: 10910010. DOI: 10.1016/j.bbiosy.2024.100090.

Poly-beta-amino-ester licofelone conjugates development for osteoarthritis treatment.

Alghamdi R, Pertusati F, Prokopovich P RSC Adv. 2024; 14(1):15-28.

PMID: 38173598 PMC: 10758810. DOI: 10.1039/d3ra04967a.

Translation of cell therapies to treat autoimmune disorders.

Mehta J, Hiremath S, Chilimba C, Ghasemi A, Weaver J Adv Drug Deliv Rev. 2023; 205:115161.

PMID: 38142739 PMC: 10843859. DOI: 10.1016/j.addr.2023.115161.

References

Lindy O, Konttinen Y, Sorsa T, Ding Y, Santavirta S, Ceponis A . Matrix metalloproteinase 13 (collagenase 3) in human rheumatoid synovium. Arthritis Rheum. 1997; 40(8):1391-9. DOI: 10.1002/art.1780400806. View

Konttinen Y, Ceponis A, Takagi M, Ainola M, Sorsa T, Sutinen M . New collagenolytic enzymes/cascade identified at the pannus-hard tissue junction in rheumatoid arthritis: destruction from above. Matrix Biol. 1999; 17(8-9):585-601. DOI: 10.1016/s0945-053x(98)90110-x. View

Moldovan F, Pelletier J, Hambor J, Cloutier J, Martel-Pelletier J . Collagenase-3 (matrix metalloprotease 13) is preferentially localized in the deep layer of human arthritic cartilage in situ: in vitro mimicking effect by transforming growth factor beta. Arthritis Rheum. 1997; 40(9):1653-61. DOI: 10.1002/art.1780400915. View

Hanemaaijer R, Sorsa T, Konttinen Y, Ding Y, Sutinen M, Visser H . Matrix metalloproteinase-8 is expressed in rheumatoid synovial fibroblasts and endothelial cells. Regulation by tumor necrosis factor-alpha and doxycycline. J Biol Chem. 1998; 272(50):31504-9. DOI: 10.1074/jbc.272.50.31504. View

Butler G, Butler M, Atkinson S, Will H, Tamura T, Schade van Westrum S . The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study. J Biol Chem. 1998; 273(2):871-80. DOI: 10.1074/jbc.273.2.871. View

dOrtho M, Will H, Atkinson S, Butler G, Messent A, Gavrilovic J . Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases. Eur J Biochem. 1998; 250(3):751-7. DOI: 10.1111/j.1432-1033.1997.00751.x. View

Tetlow L, Woolley D . Comparative immunolocalization studies of collagenase 1 and collagenase 3 production in the rheumatoid lesion, and by human chondrocytes and synoviocytes in vitro. Br J Rheumatol. 1998; 37(1):64-70. DOI: 10.1093/rheumatology/37.1.64. View

Nordstrom D, Lindy O, Lauhio A, Sorsa T, Santavirta S, Konttinen Y . Anti-collagenolytic mechanism of action of doxycycline treatment in rheumatoid arthritis. Rheumatol Int. 1998; 17(5):175-80. DOI: 10.1007/s002960050030. View

Bottomley K, Johnson W, Walter D . Matrix metalloproteinase inhibitors in arthritis. J Enzyme Inhib. 1998; 13(2):79-101. DOI: 10.3109/14756369809035829. View

10.

ODell J . Is there a role for antibiotics in the treatment of patients with rheumatoid arthritis?. Drugs. 1999; 57(3):279-82. DOI: 10.2165/00003495-199957030-00001. View

11.

Kozaci L, Brown C, Adcocks C, Galloway A, Hollander A, Buttle D . Stromelysin 1, neutrophil collagenase, and collagenase 3 do not play major roles in a model of chondrocyte mediated cartilage breakdown. Mol Pathol. 1999; 51(5):282-6. PMC: 395653. DOI: 10.1136/mp.51.5.282. View

12.

Skotnicki J, Zask A, Nelson F, Albright J, Levin J . Design and synthetic considerations of matrix metalloproteinase inhibitors. Ann N Y Acad Sci. 1999; 878:61-72. DOI: 10.1111/j.1749-6632.1999.tb07674.x. View

13.

Nagase H, Woessner Jr J . Matrix metalloproteinases. J Biol Chem. 1999; 274(31):21491-4. DOI: 10.1074/jbc.274.31.21491. View

14.

Holmbeck K, Bianco P, Caterina J, Yamada S, Kromer M, Kuznetsov S . MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover. Cell. 1999; 99(1):81-92. DOI: 10.1016/s0092-8674(00)80064-1. View

15.

van Meurs J, van Lent P, Stoop R, Holthuysen A, Singer I, Bayne E . Cleavage of aggrecan at the Asn341-Phe342 site coincides with the initiation of collagen damage in murine antigen-induced arthritis: a pivotal role for stromelysin 1 in matrix metalloproteinase activity. Arthritis Rheum. 1999; 42(10):2074-84. DOI: 10.1002/1529-0131(199910)42:10<2074::AID-ANR7>3.0.CO;2-5. View

16.

Malemud C, Goldberg V . Future directions for research and treatment of osteoarthritis. Front Biosci. 1999; 4:D762-71. DOI: 10.2741/malemud. View

17.

Vu T, Werb Z . Matrix metalloproteinases: effectors of development and normal physiology. Genes Dev. 2000; 14(17):2123-33. DOI: 10.1101/gad.815400. View

18.

Gomis-Ruth F, Maskos K, Betz M, Bergner A, Huber R, Suzuki K . Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1. Nature. 1997; 389(6646):77-81. DOI: 10.1038/37995. View

19.

Konttinen Y, Ainola M, Valleala H, Ma J, Ida H, Mandelin J . Analysis of 16 different matrix metalloproteinases (MMP-1 to MMP-20) in the synovial membrane: different profiles in trauma and rheumatoid arthritis. Ann Rheum Dis. 1999; 58(11):691-7. PMC: 1752794. DOI: 10.1136/ard.58.11.691. View

20.

van Meurs J, van Lent P, Holthuysen A, Lambrou D, Bayne E, Singer I . Active matrix metalloproteinases are present in cartilage during immune complex-mediated arthritis: a pivotal role for stromelysin-1 in cartilage destruction. J Immunol. 1999; 163(10):5633-9. View