Interactions between collagen IX and biglycan measured by atomic force microscopy
- Department of Orthopedic Surgery, Baylor College of Medicine, Houston, TX (United States)
- Department of Orthopedics, Kaohsiung Medical University School of Medicine, Kaohsiung, Taiwan (China)
- Department of Physical Medicine and Rehabilitation, Kaohsiung Medical University Hospital, Taiwan (China)
- Institute of Biosciences and Technology, Texas A and M University, Houston, TX (United States)
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.
- OSTI ID:
- 20795854
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 339, Issue 1; Other Information: DOI: 10.1016/j.bbrc.2005.10.205; PII: S0006-291X(05)02520-9; Copyright (c) 2005 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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