Effects of Tamm-Horsfall protein and albumin on calcium oxalate crystallization and importance of sialic acids.

BACKGROUND Tamm-Horsfall protein and human serum albumin are common urinary proteins that show uncertain inhibitory action on the crystallization of calcium oxalate monohydrate. MATERIALS AND METHODS Batch experiments on crystal nucleation, growth, and aggregation were performed using purified Tamm-Horsfall protein and albumin before and after enzymatic removal of sialic acids from the proteins. RESULTS At a concentration of 100 nM, both Tamm-Horsfall protein and albumin promoted the time of crystal nucleation by 18.4% and 8.9%, respectively, relative to the control. However, both of the proteins exerted an inhibitory effect on crystal growth, with the IC(50) being 7.27 nM for Tamm-Horsfall protein and 37.5 nM for albumin. The inhibition of crystal aggregation was 81.82% by Tamm-Horsfall protein 100 nM but only 54.55% at 50 nM after enzymatic removal of the sialic acid. Instead of increasing the inhibition, the effect was changed to promotion after an increase in the concentration of Tamm-Horsfall protein to more than 500 nM for native protein and to more than 100 nM for the enzymatic digest. Albumin showed little change after enzymatic treatment and maintained a maximal inhibitory effect of 72.73% on crystal aggregation when the concentration reached to 100 nM. CONCLUSION Because the promotion of nucleation could lessen the subsequent saturation of a calcium oxalate solution, it is concluded that Tamm-Horsfall protein and albumin show an overall effect of inhibition on crystallization in vitro. The inhibitory effect of Tamm-Horsfall protein is partly related to sialic acid.