Interactions between collagen IX and biglycan measured by atomic force microscopy

The stability of the lattice-like type II collagen architecture of articular cartilage is paramount to its optimal function. Such stability not only depends on the rigidity of collagen fibrils themselves, but more importantly, on their interconnections. One known interconnection is through type IX a...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2006-01, Vol.339 (1), p.204-208
Main Authors: Chen, Chia-Hsin, Yeh, Ming-Long, Geyer, Mark, Wang, Gwo-Jaw, Huang, Mao-Hsiung, Heggeness, Michael H., Höök, Magnus, Luo, Zong-Ping
Format: Article
Language:English
Subjects:
Atomic force microscopy
Biglycan
Binding force
Biomechanical Phenomena
Collagen IX
Collagen Type IX - chemistry
Extracellular Matrix Proteins
Microscopy, Atomic Force
Protein Binding
Proteoglycans - chemistry
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Summary:The stability of the lattice-like type II collagen architecture of articular cartilage is paramount to its optimal function. Such stability not only depends on the rigidity of collagen fibrils themselves, but more importantly, on their interconnections. One known interconnection is through type IX and biglycan molecules. However, the mechanical properties of this interaction and its role in the overall stability remain unrevealed. Using atomic force microscopy, this study directly measured the mechanical strength (or the rupture force) of a single bond between collagen IX and biglycan. The results demonstrated that the rupture force of this single bond was 15 pN, which was significantly smaller than those of other known molecule interactions to date. This result suggested that type IX collagen and biglycan interaction may be the weak link in the cartilage collagen architecture, vulnerable to abnormal joint force and associated with disorders such as osteoarthritis.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2005.10.205