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Characterization of hyaluronic acid interaction with calcium oxalate crystals: implication of crystals faces, pH and citrate
Author(s) -
Lamontagne CharlesAntoine,
Plante Gérard E.,
Grandbois Michel
Publication year - 2011
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.1110
Subject(s) - calcium oxalate , adhesion , crystal (programming language) , kidney stones , hyaluronic acid , chemistry , biophysics , force spectroscopy , atomic force microscopy , glycosaminoglycan , molecule , calcium , oxalate , crystallography , biochemistry , materials science , nanotechnology , inorganic chemistry , anatomy , organic chemistry , biology , medicine , computer science , programming language , urology
Interaction between hyaluronic acid (HA) present at the surface of tubular epithelial cells and calcium oxalate monohydrate (COM) crystals is thought to play an important role in kidney stone formation. AFM‐based force spectroscopy, where HA is covalently attached to AFM‐probes, was used to quantify the interaction between HA and the surfaces of COM crystals. The work of adhesion of the HA‐probe as well as the rupture force of single HA molecules were quantified in order to understand the molecular regulation of HA binding to COM crystals. Our results reveal that HA adsorbs to the crystal surface in physiological conditions. We also observed increased adhesion when the pH is lowered to a value that increases the risk of kidney stone formation. HA adhesion to the COM crystal surface can be suppressed by citrate, a physiological inhibitor of stone retention currently used in the treatment and prevention of kidney stone formation. Interestingly, we also observed preferential binding of HA onto the [100] face versus the [010] face, suggesting a major contribution of the [100] faces in the crystal retention process at the surface of tubular epithelial cells and the promotion of stone formation. Our results clearly establish a direct role for the glycosaminoglycan HA present at the surface of kidney tubular epithelium in the process of COM crystal retention. Copyright © 2011 John Wiley & Sons, Ltd.