Abstract | OBJECTIVE: METHODS: RESULTS: In cartilage lacking both type IX collagen and COMP, matrilin 3 showed decreased matrix anchorage. Less matrilin 3 was deposited in the matrix of double-deficient chondrocytes, while larger amounts were secreted into the medium. Proteoglycans were less well retained in the matrix formed in alginate cultures, while collagen deposition was not significantly affected. Electron microscopy revealed similar cartilage collagen fibril diameters in the cultures of double-deficient and wild-type chondrocytes. In contrast, a larger fibril diameter was observed in the matrix of chondrocytes deficient in only type IX collagen. CONCLUSION: Our results show that type IX collagen and COMP are involved in matrix assembly by mediating the anchorage and regulating the distribution of other matrix macromolecules such as proteoglycans and matrilins and have counteracting effects on collagen fibril growth. Loss of type IX collagen and COMP leads to matrix aberrations that may make cartilage more susceptible to degeneration.
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Authors | K Blumbach, Y M Bastiaansen-Jenniskens, J DeGroot, M Paulsson, G J V M van Osch, F Zaucke |
Journal | Arthritis and rheumatism
(Arthritis Rheum)
Vol. 60
Issue 12
Pg. 3676-85
(Dec 2009)
ISSN: 0004-3591 [Print] United States |
PMID | 19950300
(Publication Type: Journal Article)
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Chemical References |
- Collagen Type IX
- Extracellular Matrix Proteins
- Glycoproteins
- Matn1 protein, mouse
- Matn3 protein, mouse
- Matrilin Proteins
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Topics |
- Animals
- Cells, Cultured
- Chondrocytes
(metabolism, ultrastructure)
- Collagen Type IX
(metabolism, ultrastructure)
- Elastic Modulus
- Extracellular Matrix
(metabolism, ultrastructure)
- Extracellular Matrix Proteins
(metabolism)
- Female
- Fluorescent Antibody Technique, Indirect
- Glycoproteins
(metabolism)
- Male
- Matrilin Proteins
- Mice
- Mice, Inbred C57BL
- Mice, Knockout
- Stress, Mechanical
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