ADAMTS proteases: key roles in atherosclerosis?
Summary of "ADAMTS proteases: key roles in atherosclerosis?"
The ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteases are secreted enzymes that regulate extracellular matrix turnover by degrading specific matrix components. Roles for the proteases in inflammation and atherosclerosis have been suggested by a number of recent studies, and the role of ADAMTS-4 and -5 in the breakdown of aggrecan and subsequent degradation of cartilage during osteoarthritis has also been established. The ability of the ADAMTS proteases to degrade versican, the primary proteoglycan in the vasculature, is thought to be central to any hypothesized role for the proteases in atherosclerosis. In this review, we introduce the structure and function of the ADAMTS family of proteases and review the literature that links them with inflammation and atherosclerosis.
Affiliation
School of Biosciences, Cardiff University, Museum Avenue, Cardiff, UK, CF10 3AX, SalterRC@cardiff.ac.uk.
Journal Details
This article was published in the following journal.
Name: Journal of molecular medicine (Berlin, Germany)
ISSN: 1432-1440
Pages:
Links
- PubMed Source: http://www.ncbi.nlm.nih.gov/pubmed/20652528
- DOI: http://dx.doi.org/10.1007/s00109-010-0654-x
Medical and Biotech [MESH] Definitions
Complement C1 Inhibitor Protein
An endogenous 105-kDa plasma glycoprotein produced primarily by the LIVER and MONOCYTES. It inhibits a broad spectrum of proteases, including the COMPLEMENT C1R and the COMPLEMENT C1S proteases of the CLASSICAL COMPLEMENT PATHWAY, and the MANNOSE-BINDING PROTEIN-ASSOCIATED SERINE PROTEASES. C1-INH-deficient individuals suffer from HEREDITARY ANGIOEDEMA TYPES I AND II.
Mannose-binding Protein-associated Serine Proteases
Serum serine proteases which participate in COMPLEMENT ACTIVATION. They are activated when complexed with the MANNOSE-BINDING LECTIN, therefore also known as Mannose-binding protein-Associated Serine Proteases (MASPs). They cleave COMPLEMENT C4 and COMPLEMENT C2 to form C4b2a, the CLASSICAL PATHWAY C3 CONVERTASE.
Atp-dependent Proteases
Proteases that contain proteolytic core domains and ATPase-containing regulatory domains. They are usually comprised of large multi-subunit assemblies. The domains can occur within a single peptide chain or on distinct subunits.
Cathepsins
A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.
Protease Inhibitors
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
PubMed Articles
ADAMTS: Novel Proteases Expressed by Activated Mast Cells.
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ADAMTS (a disintegrin and metalloproteinase with thrombospondin type 1 motifs) proteases are emerging as key participants in the pathogenesis of vascular diseases. We studied the expression of ADAMTS-...
ADAMTS-13 is produced by glial cells and upregulated after spinal cord injury.
ADAMTS-13, a member of the family of disintegrins and metalloproteinases with thrombospondin motifs, is produced primarily in the liver, particularly by hepatic stellate cells. This metalloproteinase...
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We have previously reported that reactive site mutants of the N-terminal inhibitory domain of TIMP-3 (N-TIMP-3) modified at the N-terminus, selectively inhibited ADAM17 (A Disintegrin and Metalloprote...
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