Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2007;9(5):221.
doi: 10.1186/ar2304.

Proteinases in the joint: clinical relevance of proteinases in joint destruction

Yvonne Rengel  1 , Caroline Ospelt, Steffen Gay
Affiliations
Review

Proteinases in the joint: clinical relevance of proteinases in joint destruction

Yvonne Rengel et al. Arthritis Res Ther. 2007.

Abstract

Proteinases are involved in essential steps in cartilage and bone homeostasis. Consequently, efforts have been made to establish their potential role in the pathology of rheumatic conditions such as rheumatoid arthritis, osteoarthritis and spondyloarthritis. Matrix metalloproteinases (MMPs) are sensitive markers of disease severity and response to treatment, and therefore they have potential in the assessment of rheumatic diseases. Despite disappointing early results with synthetic inhibitors of MMPs, there is still much scope for developing effective and safe MMPs inhibitors, and consequently to deliver new options to inhibit joint destruction.

PubMed Disclaimer

Figures

Figure 1
Figure 1
Summary of proteases. MMP, matrix metalloproteinase; MT, membrane-type; tPA, tissue-type plasminogen activator; uPA, urokinase-type plasminogen activator.
Figure 2
Figure 2
Proteinases in joint destruction. Shown are the proteinases that are involved in the joint destruction that occurs in (a) osteoarthritis and (b) rheumatoid arthritis. ADAM, a disintegrin and metalloproteinase-like; ADAMTS, ADAM-thrombospondin; IL, interleukin; MMP, matrix metalloproteinase; MT, membrane-type; RANKL, receptor activator of nuclear factor-κB ligand; TNF, tumour necrosis factor; tPA, tissue-type plasminogen activator; uPA, urokinase-type plasminogen activator.
See this image and copyright information in PMC

References

    1. Turk B. Targeting proteases: successes, failures and future prospects. Nat Rev Drug Discov. 2006;5:785–799. doi: 10.1038/nrd2092. - DOI - PubMed
    1. Lah TT, Duran Alonso MB, Van Noorden CJ. Antiprotease therapy in cancer: hot or not? Expert Opin Biol Ther. 2006;6:257–79. doi: 10.1517/14712598.6.3.257. - DOI - PubMed
    1. Dickinson DP. Cysteine peptidases of mammals: their biological roles and potential effects in the oral cavity and other tissues in health and disease. Crit Rev Oral Biol Med. 2002;13:238–275. - PubMed
    1. Turk D, Guncar G. Lysosomal cysteine proteases (cathepsins): promising drug targets. Acta Crystallogr D Biol Crystal-logr. 2003;59:203–213. doi: 10.1107/S0907444902021479. - DOI - PubMed
    1. Barrett AJ. The many forms and functions of cellular proteinases. Fed Proc. 1980;39:9–14. - PubMed

Substances