Cartilage aggrecan can undergo self-adhesion

Biophys J. 2008 Nov 15;95(10):4862-70. doi: 10.1529/biophysj.107.128389. Epub 2008 Aug 1.

Abstract

Here it is reported that aggrecan, the highly negatively charged macromolecule in the cartilage extracellular matrix, undergoes Ca(2+)-mediated self-adhesion after static compression even in the presence of strong electrostatic repulsion in physiological-like solution conditions. Aggrecan was chemically end-attached onto gold-coated planar silicon substrates and gold-coated microspherical atomic force microscope probe tips (end radius R approximately 2.5 mum) at a density ( approximately 40 mg/mL) that simulates physiological conditions in the tissue ( approximately 20-80 mg/mL). Colloidal force spectroscopy was employed to measure the adhesion between opposing aggrecan monolayers in NaCl (0.001-1.0 M) and NaCl + CaCl(2) ([Cl(-)] = 0.15 M, [Ca(2+)] = 0 - 75 mM) aqueous electrolyte solutions. Aggrecan self-adhesion was found to increase with increasing surface equilibration time upon compression (0-30 s). Hydrogen bonding and physical entanglements between the chondroitin sulfate-glycosaminoglycan side chains are proposed as important factors contributing to aggrecan self-adhesion. Self-adhesion was found to significantly increase with decreasing bath ionic strength (and hence, electrostatic double-layer repulsion), as well as increasing Ca(2+) concentration due to the additional ion-bridging effects. It is hypothesized that aggrecan self-adhesion, and the macromolecular energy dissipation that results from this self-adhesion, could be important factors contributing to the self-assembled architecture and integrity of the cartilage extracellular matrix in vivo.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adhesiveness
  • Aggrecans / chemistry*
  • Animals
  • Binding Sites
  • Cartilage, Articular / chemistry*
  • Cattle
  • Computer Simulation
  • Models, Chemical*
  • Multiprotein Complexes / chemistry
  • Protein Binding
  • Stress, Mechanical

Substances

  • Aggrecans
  • Multiprotein Complexes