Literature DB >> 16293224

Interactions between collagen IX and biglycan measured by atomic force microscopy.

Chia-Hsin Chen1, Ming-Long Yeh, Mark Geyer, Gwo-Jaw Wang, Mao-Hsiung Huang, Michael H Heggeness, Magnus Höök, Zong-Ping Luo.   

Abstract

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 15pN, 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.

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Year:  2005        PMID: 16293224     DOI: 10.1016/j.bbrc.2005.10.205

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  8 in total

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6.  Sexual Dimorphism in the Extracellular and Pericellular Matrix of Articular Cartilage.

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  8 in total

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