Renal Proximal Cells Research Articles

Secretion of lipoprotein particles by the cells of the kidney proximal segment in the migrating arctic lamprey, Lampetra japonica.

The cells of the kidney proximal segment of the migrating arctic lamprey, Lampetra japonica, contain particles of the same size, electron-density and intracellular location as particles identified by others as very low-density lipoproteins (VLDL) in the liver and intestine of teleost fishes and lampreys. These particles are synthesized within the cisternae of the smooth endoplasmic reticulum and elements of the Golgi complex. They are transferred to the lateral intercellular space and lamina propria by way of the Golgi vesicles and an intracellular channel system. Some particles are discharged into the lumina of the sinusoidal capillaries of the lamina propria. Although the physiological role of lipoprotein secretion in the renal proximal segment cells is unknown, the present observations provide morphological evidence that the kidney of the arctic lampreys synthesizes lipoproteins and releases them into the circulation at the time when they are undertaking their anadromous migration.

Quantitative requirement for ATP for active transport in isolated renal cells

We investigated the quantitative relationship between cellular ATP concentration and Na+-K+-ATPase activity as measured by ouabain-sensitive 86Rb influx in rabbit proximal renal cells. Cellular ATP was reduced in a stepwise manner by rotenone (10(-7) to 10(-5) M) and was increased by 10 mM adenosine. During these maneuvers, ouabain-sensitive 86Rb influx was linearly related to cellular ATP and did not saturate up to 9.9 mM ATP. In contrast, Na+-K+-ATPase activity in membranes prepared from these cells saturated at 2.0 mM ATP at various sodium (10-100 mM) and potassium (4-100 mM) concentrations. Sodium-dependent phosphate uptake and alpha-methylglucoside (alpha-MG) uptake were both inhibited to a similar degree when cellular ATP was reduced. We conclude that 1) the ATP requirement for saturation of Na+-K+-ATPase is higher in intact renal cells than in the membranes, and 2) the uptake of phosphate and alpha-MG are similarly influenced by reduction in ATP. This effect of ATP on phosphate and AMG uptake is most likely an indirect one and is secondary to changes in the sodium gradient across the cell.

Effect of calcium on transport characteristics of cultured proximal renal cells.

We examined the effects of acute changes in extracellular and intracellular calcium on transport processes in primary culture of proximal rabbit renal cells. A change in extracellular calcium from 0 to 3 mM inhibited amiloride-sensitive sodium uptake by 30%, and this effect was maximal at 1 mM calcium. Other polyvalent cations (Mn2+, Mg2+, La3+, and Ba2+) produced quantitatively similar inhibition of amiloride-sensitive sodium uptake compared with calcium. An increase in cytosolic calcium produced by calcium loading (20 mM) or by A23187 (20 microM) resulted in an inhibition of 25-40% of amiloride-sensitive sodium uptake. Moreover, quinidine (10(-4)M) and ruthenium red (3 microM), agents presumed to increase cytosolic calcium, inhibited amiloride-sensitive sodium uptake by 20-60%. Both these agents also inhibited sodium-dependent phosphate uptake by 20% but had no effect on ouabain-sensitive 86Rb+ uptake or on sodium-dependent alpha-methylglucoside uptake. Our data indicate that increases in extracellular calcium inhibit amiloride-sensitive sodium uptake and increases in cytosolic calcium inhibit sodium-dependent phosphate and amiloride-sensitive sodium uptakes. The effect of extracellular calcium may be due to charge screening and/or binding to the negatively charged plasma membrane or due to alterations in membrane fluidity.

Effect of phloretin on transport processes in guinea-pig kidney cortex slices

1. 1. Phloretin inhibits the transport processes in the basolateral membrane of the renal proximal cell at a lower concentration than that which affects brush-border transport mechanisms. 2. 2. It is proposed that phloretin interacts with membrane lipid components to alter membrane permeability.