Renal selectivity properties towards endogenous albumin in minimal change nephropathy.

It is well accepted that the molecular charge and conformation of serum proteins are major determinants of their glomerular filtration, but few studies characterizing the molecular features of circulating proteins in renal diseases are currently available. In 11 children affected by minimal change nephropathy (MCN) we determined the electrical charge and the fluorescence quantum yield of Tyrosine (Tyr) and Tryptophan (Trp) (taken as index of conformation) of serum and urinary albumin before and after steroid-induced remission of proteinuria. In all proteinuric children at the onset of the disease, urinary albumin was formed by one band with an isoelectric point (pI) of 4.7 (pI of the native protein), and by numerous other, less anionic bands with pIs between 4.8 and 5.5 accounting for about 50% of the total amount of this protein. The normalization of proteinuria which followed steroid therapy was characterized by the disappearance in urines of the less anionic fraction and by the appearance of numerous isoforms with a pI still more anionic (pI less than 4.7) than normal. At the same time, in the proteinuric phase, the fluorescence quantum yield of Trp of urinary albumin was markedly quenched, returning to near normal levels after steroid-induced remission of proteinuria. These data indicate that in MCN the charge-dependent renal selectivity properties are partially maintained and that the less anionic isoforms of albumin are a main component of urinary albumin. Together with the electrical charge, the conformation of albumin as a major determinant of its urinary excretion in MCN must also be considered.