Characteristics of ionic binding by rat renal tissue in vitro.

A study has been made of Na+ and Cl- binding in metabolically inhibited slices of rat renal cortex and outer medulla incubated in modified Krebs phosphate-bicarbonate Ringer solution. At pH 7.35 in control media (cortex, 147 mmol Na+/l, 105 mmol Cl-/l; outer medulla, 187 mmol Na+/l, 145 mmol Cl-/l) cortical slices bound (mean) 171 nmol Na+ and 56.7 nmol Cl-/mg solute-free dry weight; outer medullary slices bound 188 nmol Na+/mg and negligible amounts of Cl-. In both regions, Na+ was exchangeable on a 1:1 basis for K+ or Li+ in media containing equal concentrations of each cation: Na+ was completely displaced by La3+. In cortical slices in media containing equimolar Cl- and other monovalent anions, binding occurred according to the sequence acetate less than or equal to salicylate less than or equal to Cl- less than SCN-; Cl- was completely displaced by PO4(3-). When medium pH was lowered, Na+ binding was markedly reduced in both regions, whereas Cl- binding increased (and became significant in outer medulla). In NaCl solutions, Na+ binding capacity was saturated at control Na+ concentrations. When [Na+] was progressively reduced (iso-osmolality being maintained by addition of urea), bound Na+ in both regions was nearly linearly related to log medium [Na+]. Raising medium osmolality with urea caused decreased Na+ binding and increased Cl- binding in both regions. Na+ binding in both regions was significantly reduced by pre-treatment with chondroitinase ABC. Binding of both ions was independent of temperature within the range 2-37 degrees C. The possibility is raised that renal ionic binding might influence vectorial ion transport by affecting free ion activity in the region of the transporting cells.