Inhibition of interleukin-1α-induced cartilage oligomeric matrix protein degradation in bovine articular cartilage by matrix metalloproteinase inhibitors: Potential role for matrix metalloproteinases in the generation of cartilage oligomeric matrix protein fragments in arthritic synovial fluid

Ganu, Vishwas; Goldberg, Ronald; Peppard, Jane; Rediske, John; Melton, Richard; Hu, S; Wang, Weigwang; Duvander, Charlotte

doi:10.1002/1529-0131(199812)41:12<2143::aid-art9>3.3.co;2-g

Cited by 8 publications

(11 citation statements)

References 7 publications

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“…These enzymes degrade matrix constituents, thereby affecting tissue integrity. To study the release of cartilage components, particularly chondroadherin, under the influence of activated endogenous proteinases, we treated cartilage with APMA to activate matrix metalloproteinases (26). Chondroadherin was indeed among the molecules released to the medium in buffers that show little extraction on their own.…”

Section: Discussionmentioning

confidence: 99%

Association of Chondroadherin with Collagen Type II

Månsson¹,

Wenglén²,

Mörgelin³

et al. 2001

Journal of Biological Chemistry

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Chondroadherin is a cell binding, leucine-rich repeat protein found in the territorial matrix of articular cartilage. Several members of the leucine-rich repeat protein family present in the extracellular matrix of e.g. cartilage have been shown to interact with collagen and influence collagen fibrillogenesis. We show that complexes of monomeric collagen type II and chondroadherin can be released under non-denaturing conditions from articular cartilage treated with p-aminophenylmercuric acetate to activate resident matrix metalloproteinases. Purified complexes as well as complexes formed in vitro between recombinant chondroadherin and collagen type II were studied by electron microscopy. Chondroadherin was shown to bind to two sites on collagen type II.

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Section: Discussionmentioning

confidence: 99%

Association of Chondroadherin with Collagen Type II

Månsson¹,

Wenglén²,

Mörgelin³

et al. 2001

Journal of Biological Chemistry

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“…65,66 A member of the ADAMTS family, ADAMTS-4, has also been reported to cleave COMP in vitro. 67 Despite these findings, the exact role of MMPs in COMP degradation has yet to be confirmed by in vivo animal studies.…”

Section: Interaction With Compmentioning

confidence: 99%

The emerging roles of ADAMTS-7 and ADAMTS-12 matrix metalloproteinases

Lin¹,

Liu

2009

OARRR

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Abstract:The a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS) comprise a family of secreted zinc metalloproteinases with a precisely ordered modular organization. These enzymes play an important role in the turnover of extracellular matrix proteins in various tissues and their dysregulation has been implicated in disease-related processes such as arthritis, atherosclerosis, cancer, and inflammation. ADAMTS-7 and ADAMTS-12 share a similar domain organization to each other and form a subgroup within the ADAMTS family. Emerging evidence suggests that ADAMTS-7 and ADAMTS-12 may play an important role in the development and pathogenesis of various kinds of diseases. In this review, we summarize what is currently known about the roles of these two metalloproteinases, with a special focus on their involvement in chondrogenesis, endochondral ossification, and the pathogenesis of arthritis, atherosclerosis, and cancer. The future study of ADAMTS-7 and ADAMTS-12, as well as the molecules with which they interact, will help us to better understand a variety of human diseases from both a biological and therapeutic standpoint.

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“…cartilage, contains pro-MMPs, which can be activated (6,31). In view of the findings in the present work it is possible that anionic domains with tyrosine sulfate residues may serve to sequester these proenzymes to specific structures in the tissue.…”

Section: Discussionmentioning

confidence: 59%

The Tyrosine Sulfate-rich Domains of the LRR Proteins Fibromodulin and Osteoadherin Bind Motifs of Basic Clusters in a Variety of Heparin-binding Proteins, Including Bioactive Factors

Tillgren

Önnerfjord

Haglund³

et al. 2009

Journal of Biological Chemistry

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The small leucine-rich repeat proteins, fibromodulin and osteoadherin, have N-terminal extensions with a variable number of O-sulfated tyrosine residues. This modification combined with a number of aspartic and glutamic acid residues results in a highly negatively charged domain of less than 30 amino acids. We hypothesized that this domain shares functional properties with heparin regarding binding to proteins and polypeptides containing clusters of basic amino acids. Two other family members, PRELP and chondroadherin, have distinctly different clusters of basic amino acids in their N and C termini, respectively, and PRELP is known to bind to heparin via this domain. Another heparin-binding protein is the cytokine Oncostatin M, with a different cluster of basic amino acids in its C terminus. We used polypeptides representing these basic domains in solid phase assays and demonstrate interactions with the negatively charged N-terminal domain of fibromodulin and full-length osteoadherin. The tyrosine sulfate domains also bound heparin-binding proteins such as basic fibroblast growth factor-2, thrombospondin I, MMP13, the NC4 domain of collagen IX, and interleukin-10. Fibronectin with large heparin-binding domains did not bind, neither did CILP containing a heparin-binding thrombospondin type I motif without clustered basic amino acids. Affinity depends on the number and position of the sulfated tyrosine residues shown by different binding properties of 10-kDa fragments subfractionated by ion-exchange chromatography. These interactions may sequester growth factors, cytokines, and matrix metalloproteinases in the extracellular matrix as well as contribute to its organization.The integrity of the extracellular matrix depends on a multitude of interactions between molecular constituents leading to the formation of major macromolecular assemblies important for tissue functions. A major component in most types of extracellular matrix is the network of fibrillar structures primarily composed of collagen I in fibrous tissues and bone, whereas cartilage contains the similar collagen II.These collagen fibrils contain a number of associated molecules, often bound to their surface. One such molecule is the distinct collagen IX, containing three triple helical domains each surrounded by non-triple helical domains. Another set of molecules binding to triple helical collagen is the members of the small leucine-rich repeat protein family, such as fibromodulin (1), lumican (2), decorin (3), biglycan (4), PRELP (5), chondroadherin (6), and possibly osteoadherin. The typical LRR 3 protein contains 10 -11 repeats of some 25 amino acids with leucine residues at conserved locations. This domain represents a common denominator for the family and contains structures providing for interaction with, e.g. triple helical collagen (7-9). The LRR proteins contain an extension at either the N-or C-terminal end or, in a few cases, at both ends. These extensions may contribute to a second function exemplified by PRELP, where the N-terminal with a ...

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Inhibition of interleukin-1α-induced cartilage oligomeric matrix protein degradation in bovine articular cartilage by matrix metalloproteinase inhibitors: Potential role for matrix metalloproteinases in the generation of cartilage oligomeric matrix protein fragments in arthritic synovial fluid

Cited by 8 publications

References 7 publications

Association of Chondroadherin with Collagen Type II

Association of Chondroadherin with Collagen Type II

The emerging roles of ADAMTS-7 and ADAMTS-12 matrix metalloproteinases

The Tyrosine Sulfate-rich Domains of the LRR Proteins Fibromodulin and Osteoadherin Bind Motifs of Basic Clusters in a Variety of Heparin-binding Proteins, Including Bioactive Factors

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