Interactions between collagen IX and biglycan measured by atomic force microscopy

被引:15
作者
Chen, CH
Yeh, ML
Geyer, M
Wang, GJ
Huang, MH
Heggeness, MH
Höök, M
Luo, ZP [1 ]
机构
[1] Baylor Coll Med, Dept Orthoped Surg, Houston, TX 77030 USA
[2] Kaohsiung Med Hosp Univ, Dept Phys Med & Rehabil, Kaohsiung, Taiwan
[3] Kaohsiung Med Univ, Sch Med, Dept Orthoped, Kaohsiung, Taiwan
[4] Texas A&M Univ, Inst Biosci & Technol, Houston, TX USA
关键词
collagen IX; biglycan; atomic force microscopy; binding force;
D O I
10.1016/j.bbrc.2005.10.205
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要
The stability of the lattice-like type 11 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. (c) 2005 Elsevier Inc. All rights reserved.
引用
收藏
页码:204 / 208
页数:5
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