Production of cartilage oligomeric matrix protein (COMP) by cultured human dermal and synovial fibroblasts

Dodge, George R.; Hawkins, David F.; Boesler, Eric; Sakai, Lynn Y.; Jimenez, Sergio A.

doi:10.1053/joca.1998.0147

Cited by 50 publications

(39 citation statements)

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“…First, we have shown that COMP/TSP5 can bind chondrocytes and serves as an adhesive factor for these cells using short-term attachment assays. This is in agreement with the distribution of COMP/TSP5 close to the chondrocytes in early development in cartilage pericellular and territorial matrix (7,8). Through binding to the chondrocytes, COMP/ TSP5 has the potential to influence cellular activities and cellular phenotype.…”

Section: Discussionsupporting

confidence: 87%

Cartilage Oligomeric Matrix Protein/Thrombospondin 5 Supports Chondrocyte Attachment through Interaction with Integrins

Chen

Thomas

Hecht

et al. 2005

Journal of Biological Chemistry

129

122

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Cartilage oligomeric matrix protein/thrombospondin 5 (COMP/ TSP5) is a major component of the extracellular matrix of the musculoskeletal system. Although COMP/TSP5 abnormalities are associated with several pathological conditions, its normal function remains unclear. This study was undertaken to delineate the function(s) of COMP/TSP5 in cartilage, especially regarding its interaction with chondrocytes. We show that COMP/TSP5 can support chondrocyte attachment and that the RGD sequence in COMP/ TSP5 and the integrin receptors ␣5␤1 and ␣V␤3 on the chondrocytes are involved in mediating this attachment. The interactions of COMP/TSP5 with the integrins are dependent on COMP/TSP5 conformation. Chondrocyte attachment to COMP/TSP5 in the calcium-replete conformation was inhibited by function-blocking integrin ␣5 and ␤1 antibodies, suggesting the involvement of the ␣5␤1 integrin. Under this condition, a function-blocking antibody against ␣V␤3 did not have any effect on cell attachment. On the other hand, chondrocyte attachment to reduced COMP/TSP5 was instead sensitive to ␣V␤3 function-blocking antibodies, suggesting that COMP/TSP5 mediates attachment through chondrocyte ␣V␤3 integrin under this condition. Cell attachment to reduced COMP/TSP5 was not inhibited by ␤1 antibodies. These data indicate that COMP/TSP5 in different conformations can utilize different integrin receptors. These results are the first to demonstrate that COMP/TSP5 can mediate chondrocyte attachment through interactions with integrins. Through these interactions, COMP/ TSP5 may be able to regulate cellular activities and respond to environment in the surrounding cartilage matrix.Cartilage oligomeric matrix protein (COMP), 2 also known as thrombospondin 5 (TSP5), is an abundant extracellular matrix protein that has been shown to exist in tissues of the musculoskeletal system including cartilage, tendon, ligament, and synovium (1-7). Immunohistochemistry studies of COMP/TSP5 distribution in cartilage have revealed specific temporal and spatial patterns, and COMP/TSP5 can be found in cartilage at sites both in proximity to chondrocytes in the pericellular matrix and away from the cells in the territorial and interterritorial matrix (8 -10). In fetal cartilage, COMP/TSP5 exists in the pericellular matrix, especially in the growth cartilage adjacent to the primary ossification center. In adult articular cartilage, COMP/TSP5 is found at higher levels in the interterritorial matrix, with stronger staining in the deeper zone (8 -10).The importance of COMP/TSP5 is suggested by its association with several pathological conditions. Compared with normal cartilage, the levels and patterns of COMP/TSP5 expression were found to change in cartilage of osteoarthritis and rheumatoid arthritis patients, and COMP/TSP5 in serum and synovial fluid has been suggested as a biomarker for these conditions (11-13). The importance of COMP/ TSP5 to cartilage structure and function is further underscored by findings that COMP/TSP5 mutations lead to human skeletal dysplasias, p...

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Section: Discussionsupporting

confidence: 87%

Cartilage Oligomeric Matrix Protein/Thrombospondin 5 Supports Chondrocyte Attachment through Interaction with Integrins

Chen

Thomas

Hecht

et al. 2005

Journal of Biological Chemistry

129

122

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“…It has also been identified in the vitreous membrane of the eye (40), tendons (41), vascular smooth muscle cells (42), and the synovium (43,44). In the present study, mRNA for COMP was detected in native synovial explants, but the expression level decreased with culturing time in the absence of a growth factor.…”

Section: Discussionsupporting

confidence: 38%

Chondrogenic differentiation of bovine synovium: Bone morphogenetic proteins 2 and 7 and transforming growth factor β1 induce the formation of different types of cartilaginous tissue

Shintani¹,

Hunziker²

2007

Arthritis & Rheumatism

102

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Objective. To compare the potential of bone morphogenetic proteins 2 and 7 (BMP-2 and BMP-7) and transforming growth factor ␤1 (TGF␤1) to effect the chondrogenic differentiation of synovial explants by analyzing the histologic, biochemical, and gene expression characteristics of the cartilaginous tissues formed.Methods. Synovial explants derived from the metacarpal joints of calves were cultured in agarose. Initially, BMP-2 was used to evaluate the chondrogenic potential of the synovial explants under different culturing conditions. Under appropriate conditions, the chondrogenic effects of BMP-2, BMP-7, and TGF␤1 were then compared. The differentiated tissue was characterized histologically, histomorphometrically, immunohistochemically, biochemically, and at the gene expression level.Results. BMP-2 induced the chondrogenic differentiation of synovial explants in a dose-and timedependent manner under serum-and dexamethasonefree conditions. The expression levels of cartilagerelated genes increased in a time-dependent manner. BMP-7 was more potent than BMP-2 in inducing chondrogenesis, but the properties of the differentiated tissue were similar in each case. The type of cartilaginous tissue formed under the influence of TGF␤1 differed in terms of both cell phenotype and gene expression profiles. Conclusion

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“…And in patients with rheumatoid arthritis, the COMP gene is expressed in the fibroblast-like cells but not in the macrophages of the synovial connective-tissue layer. 26 COMP is a pentameric noncollagenous glycoprotein which is present not only in synovial [26][27][28] and cartilage tissue, 29 but also in the ocular vitreous, 30 in tendons, 31 and in vascular smooth muscle cells. 32 In the present study, the mRNA for COMP was likewise expressed in bovine synovial tissue.…”

Section: Discussionmentioning

confidence: 99%

Expression of cartilage‐related genes in bovine synovial tissue

Shintani

Kurth

Hunziker

2007

Journal Orthopaedic Research

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The synovium contains mesenchymal stem cells with chondrogenic potential. Although synovial and articular cartilage tissue develop from a common pool of mesenchymal cells, little is known about their genetic commonalities. In the present study, the mRNA levels for several cartilage-related proteins, namely, cartilage oligomeric matrix protein (COMP), Sox9, aggrecan, and collagen types I, II, IX, X, and XI, were measured using the real-time polymerase chain reaction. Our data reveal the synovium of calf metacarpal joints to physiologically express not only type I collagen but also COMP, Sox9, aggrecan, and collagen types X and XI. The mRNA levels for the latter five proteins lie between 2% and 15% of those in articular cartilage. We speculate that these genes are being expressed by chondroprogenitor cells, whose presence in the synovium reflects a common ontogenetic phase in the fetal development of this tissue and of articular cartilage. ß

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Production of cartilage oligomeric matrix protein (COMP) by cultured human dermal and synovial fibroblasts

Cited by 50 publications

References 0 publications

Cartilage Oligomeric Matrix Protein/Thrombospondin 5 Supports Chondrocyte Attachment through Interaction with Integrins

Cartilage Oligomeric Matrix Protein/Thrombospondin 5 Supports Chondrocyte Attachment through Interaction with Integrins

Chondrogenic differentiation of bovine synovium: Bone morphogenetic proteins 2 and 7 and transforming growth factor β1 induce the formation of different types of cartilaginous tissue

Expression of cartilage‐related genes in bovine synovial tissue

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