Study of glomerular permselectivity for proteins of the glomerular basement membrane using a dialyzer model.

The glomerular basement membrane (GBM) is considered to regulate glomerular permselectivity for proteins by acting as both size barrier and charge barrier. Since heparan sulfate-proteoglycan (HS-PG), which forms the charge barrier of GBM, contains a sulfonic acid, we made membranes with various degrees of negative charge models of GBM by addition of sulfonic acid to ethylene vinyl alcohol (EVAL) membranes. A high-resolution scanning electron-microscopic study revealed no ultrastructural alterations after adding sulfonic acid to EVAL membranes. Both neutrally and negatively charged membranes had porous structures in the inner surface of the membranes. The interrelation between the two actions of size and charge of GBM was studied using special dialyzers with various degrees of negative charge and different pore sizes. The negatively charged membranes adsorbed proteins with positive charge and repulsed proteins with negative charge. The degrees of adsorption and repulsion were weaker in membranes with larger pores and were stronger for proteins with larger molecular weights. The permselectivity for proteins of a charged membrane depends largely upon the interrelation between the pore size of the membrane and the size of the proteins. It is, therefore, suggested that the presence of a size barrier in GBM is necessary for the charge barrier to effectively exert glomerular permselectivity for proteins. Our study may lead to the development of a dialyzer with higher permselectivity by adding sulfonic acid rather than conventional dialyzers.