Facilitation by serum albumin of renal tubular secretion of organic anions

Am J Physiol. 1989 Mar;256(3 Pt 2):F475-84. doi: 10.1152/ajprenal.1989.256.3.F475.

Abstract

The role of albumin in tubular secretion of the organic anions p-aminohippurate (PAH, 21% albumin-bound at 1 microM) and methotrexate (MTX, 55% bound at 1 microM), and of the organic cation N1-methylnicotinamide (NMN, not bound), was investigated in isolated rabbit S2 proximal tubules. PAH or MTX secretory rates were low in the absence of colloids or in the presence of 1 g/dl dextran 40, and were reversibly two- to sevenfold stimulated by either 1 g/dl bovine (BSA, either regular, defatted, and/or dialyzed) or rabbit serum albumin, or by dialyzed native rabbit plasma. NMN secretion was not stimulated by either dextran or albumin. Luminal BSA had no effect, but stimulation of PAH secretion was observed when albumin was present in both lumen and bath. This secretion was BSA concentration-dependent up to a 1 g/dl BSA. Saturation experiments suggested that 1 g/dl BSA may increase PAH apparent affinity for secretion, with no change in its maximum velocity. Albumin appears therefore to facilitate organic anion proximal secretion by an effect unrelated to oncotic pressure or to the extent of organic anion binding.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Dextrans / pharmacology
  • In Vitro Techniques
  • Kidney Tubules, Proximal / drug effects
  • Kidney Tubules, Proximal / physiology*
  • Kinetics
  • Methotrexate / metabolism
  • Niacinamide / analogs & derivatives
  • Niacinamide / metabolism
  • Protein Binding
  • Rabbits
  • Serum Albumin, Bovine / metabolism*
  • p-Aminohippuric Acid / metabolism

Substances

  • Dextrans
  • Niacinamide
  • Serum Albumin, Bovine
  • 5-methylnicotinamide
  • p-Aminohippuric Acid
  • Methotrexate