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Interaction of lubricin with type II collagen surfaces: adsorption, friction, and normal forces.

Publication ,  Journal Article
Chang, DP; Guilak, F; Jay, GD; Zauscher, S
Published in: Journal of biomechanics
February 2014

One of the major constituents of the synovial fluid that is thought to be responsible for chondroprotection and boundary lubrication is the glycoprotein lubricin (PRG4); however, the molecular mechanisms by which lubricin carries out its critical functions still remain largely unknown. We hypothesized that the interaction of lubricin with type II collagen, the main component of the cartilage extracellular matrix, results in enhanced tribological and wear properties. In this study, we examined: (i) the molecular details by which lubricin interacts with type II collagen and how binding is related to boundary lubrication and adhesive interactions; and (ii) whether collagen structure can affect lubricin adsorption and its chondroprotective properties. We found that lubricin adsorbs strongly onto denatured, amorphous, and fibrillar collagen surfaces. Furthermore, we found large repulsive interactions between the collagen surfaces in presence of lubricin, which increased with increasing lubricin concentration. Lubricin attenuated the large friction and also the long-range adhesion between fibrillar collagen surfaces. Interestingly, lubricin adsorbed onto and mediated the frictional response between the denatured and native amorphous collagen surfaces equally and showed no preference on the supramolecular architecture of collagen. However, the coefficient of friction was lowest on fibrillar collagen in the presence of lubricin. We speculate that an important role of lubricin in mediating interactions at the cartilage surface is to attach to the cartilage surface and provide a protective coating that maintains the contacting surfaces in a sterically repulsive state.

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Published In

Journal of biomechanics

DOI

EISSN

1873-2380

ISSN

0021-9290

Publication Date

February 2014

Volume

47

Issue

3

Start / End Page

659 / 666

Related Subject Headings

  • Synovial Fluid
  • Surface Properties
  • Protein Structure, Secondary
  • Protein Denaturation
  • Protein Binding
  • Microscopy, Atomic Force
  • Lubrication
  • Humans
  • Glycoproteins
  • Friction
 

Citation

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Chicago
ICMJE
MLA
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Chang, D. P., Guilak, F., Jay, G. D., & Zauscher, S. (2014). Interaction of lubricin with type II collagen surfaces: adsorption, friction, and normal forces. Journal of Biomechanics, 47(3), 659–666. https://doi.org/10.1016/j.jbiomech.2013.11.048
Chang, Debby P., Farshid Guilak, Gregory D. Jay, and Stefan Zauscher. “Interaction of lubricin with type II collagen surfaces: adsorption, friction, and normal forces.Journal of Biomechanics 47, no. 3 (February 2014): 659–66. https://doi.org/10.1016/j.jbiomech.2013.11.048.
Chang DP, Guilak F, Jay GD, Zauscher S. Interaction of lubricin with type II collagen surfaces: adsorption, friction, and normal forces. Journal of biomechanics. 2014 Feb;47(3):659–66.
Chang, Debby P., et al. “Interaction of lubricin with type II collagen surfaces: adsorption, friction, and normal forces.Journal of Biomechanics, vol. 47, no. 3, Feb. 2014, pp. 659–66. Epmc, doi:10.1016/j.jbiomech.2013.11.048.
Chang DP, Guilak F, Jay GD, Zauscher S. Interaction of lubricin with type II collagen surfaces: adsorption, friction, and normal forces. Journal of biomechanics. 2014 Feb;47(3):659–666.
Journal cover image

Published In

Journal of biomechanics

DOI

EISSN

1873-2380

ISSN

0021-9290

Publication Date

February 2014

Volume

47

Issue

3

Start / End Page

659 / 666

Related Subject Headings

  • Synovial Fluid
  • Surface Properties
  • Protein Structure, Secondary
  • Protein Denaturation
  • Protein Binding
  • Microscopy, Atomic Force
  • Lubrication
  • Humans
  • Glycoproteins
  • Friction