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PubMed1987

The relationship between the rate of glutamate deamination and long-chain acyl-CoA accumulation in kidney cortex mitochondria of rabbit.

The effect of long-chain acyl-CoA on glutamate dehydrogenase activity was studied in uncoupled rabbit kidney cortex mitochondria incubated with glutamate and palmitoylcarnitine in the presence of arsenite. The mitochondrial long-chain acyl-CoA (about 2 nmol/mg of protein) accumulated in the presence of arsenite resulted in an inhibition of ammonia production from 4.1 to 1.2 nmol/min per mg of protein. Leucine and ADP, activators of glutamate dehydrogenase, did not release the inhibitory effect of long-chain acyl-CoA on glutamate deamination. In view of the presented data it seems that inhibitory effect of long-chain acyl-CoA on glutamate dehydrogenase activity may have a physiological significance.

Acyl Coenzyme A↗
PubMed1977

Guanosine triphosphate: 5-hydroxylysine phosphotransferase in rat kidney cortex.

An enzyme which catalyzes the transfer of the gamma-phosphate from GTP onto 5-hydroxylysine was partially purified from rat kidney cortex by means of acid precipitation and DEAE-Sephadex A-50 column chromatography. The enzyme activity was assayed by measuring the transfer of [32P] from gamma-[32P]-GTP to materials not adsorbed by charcoal. This partially purified enzyme showed essentially no GTP phosphohydrolase activity and an optimal pH of 8.0. An apparent Km of about 23.8 mumol/1 was obtained with respect to 5-hydroxylysine. Mg2+ was required for the activity of this enzyme. Ethanolamine, L-lysine, L-ornithine and choline inhibited the enzyme but L-threonine, L-serine and hydroxy-L-proline did not. None of these compounds severed as substrate for this enzyme.

Animals↗
PubMed1979

Sodium-dependence of p-aminohippurate transport by rat kidney cortex slices.

The effect of medium Na+ concentration on p-amino-hippuric acid (PAH) uptake and efflux were investigated in rat kidney cortex slices. The uptake during 10 min incubation was taken as a measure of the initial influx. At a fixed Na+ concentration, the uptake curve (amount of uptake against substrate concentration) consisted of two distinct components; one linear with medium PAH concentration and the other obeying Michaelis-Menten kinetics. Only the latter was dependent on the Na+ concentration. A reduction of medium Na+ concentration resulted in an increase in Kt for PAH, while Vmax for PAH remained unchanged. In the absence of Na+, the component obeying Michaelis-Menten kinetics still existed, and Vmax for PAH was identical with that in the presence of Na+. The reciprocals of Kt were linearly proportional to medium Na+ concentration. Such kinetic properties could be interpreted on the basis of a kinetic model in which PAH was assumed to be transported across the cell membrane by forming both binary (carrier-PAH, SX) and ternary (NaXS) complexes. An elevation or reduction of Na+ concentration in efflux media caused an immediate decrease or increase in the rate constant for PAH efflux, respectively. Addition of a competitive inhibitor (hippurate) to efflux medium also caused an immediate increase in the rate constant. From these observations, it was concluded that PAH transport in rat kidney was mediated through both Na+-dependent and Na+-independent carrier processes at the peritubular membrane.

Aminohippuric Acids↗
PubMed2005

Cd2+-induced swelling-contraction dynamics in isolated kidney cortex mitochondria: role of Ca2+ uniporter, K+ cycling, and protonmotive force.

The nephrotoxic metal Cd(2+) causes mitochondrial damage and apoptosis of kidney proximal tubule cells. A K(+) cycle involving a K(+) uniporter and a K(+)/H(+) exchanger in the inner mitochondrial membrane (IMM) is thought to contribute to the maintenance of the structural and functional integrity of mitochondria. In the present study, we have investigated the effect of Cd(2+) on K(+) cycling in rat kidney cortex mitochondria. Cd(2+) (EC(50) approximately 19 microM) induced swelling of nonenergized mitochondria suspended in isotonic salt solutions according to the sequence KCl = NaCl > LiCl >> choline chloride. Cd(2+)-induced swelling of energized mitochondria had a similar EC(50) value and showed the same cation dependence but was followed by a spontaneous contraction. Mitochondrial Ca(2+) uniporter (MCU) blockers, but not permeability transition pore inhibitors, abolished swelling, suggesting the need for Cd(2+) influx through the MCU for swelling to occur. Complete loss of mitochondrial membrane potential (DeltaPsi(m)) induced by K(+) influx did not prevent contraction, but addition of the K(+)/H(+) exchanger blocker, quinine (1 mM), or the electroneutral protonophore nigericin (0.4 microM), abolished contraction, suggesting the mitochondrial pH gradient (DeltapH(m)) driving contraction. Accordingly, a quinine-sensitive partial dissipation of DeltapH(m) was coincident with the swelling-contraction phase. The data indicate that Cd(2+) enters the matrix through the MCU to activate a K(+) cycle. Initial K(+) load via a Cd(2+)-activated K(+) uniporter in the IMM causes osmotic swelling and breakdown of DeltaPsi(m) and triggers quinine-sensitive K(+)/H(+) exchange and contraction. Thus Cd(2+)-induced activation of a K(+) cycle contributes to the dissipation of the mitochondrial protonmotive force.

Animals↗
PubMed1988

Na+ and H+ gradient-dependent transport of p-aminohippurate in membrane vesicles from dog kidney cortex.

The transport of p-aminohippurate (PAH) was studied in basolateral (BLMV) and brush border membrane vesicles (BBMV) isolated from dog kidney cortex. Imposition of an inwardly directed 100 mN Na+ gradient stimulated the uptake of 50 microM [3H]PAH into BLMV, whereas a pH gradient (pHout = 6.0, pHin = 7.4) only slightly enhanced uptake. The Na+ gradient-dependent uptake of PAH was electroneutral, saturable and sensitive to inhibition by probenecid and several anionic drugs, with (apparent) Km = 0.79 +/- 0.16 mM, Vmax = 0.80 +/- 0.05 nmol/mg protein, 15 sec and Ki for probenecid = 0.08 +/- 0.01 mM. Simultaneous imposition of the pH gradient (outward OH- gradient) and inward Na+ gradient stimulated PAH uptake significantly over that with an Na+ gradient alone. These results are consistent with an Na+ gradient-stimulated PAH/OH- exchange mechanism in the basolateral membrane. In BBMV, PAH uptake could be stimulated by an outwardly directed OH- gradient as well as an inward Na+ gradient. Both gradients could drive PAH transport via a mediated probenecid-sensitive pathway. Na+ gradient-stimulated uptake was electrogenic with a (apparent) Km = 4.93 +/- 0.57 mM, Vmax = 6.71 +/- 0.36 nmol/mg protein, 15 sec and Ki,prob = 0.13 +/- 0.01 mM. The kinetic parameters for PAH/OH- exchange were virtually the same, (apparent) Km = 5.72 +/- 0.49 mM, Vmax = 7.87 +/- 0.33 nmol/mg protein, 15 sec and Ki,prob = 0.16 +/- 0.02 mM. When both the Na+ and pH (outward OH-) gradient were simultaneously imposed an almost twofold stimulation in uptake was observed over that with either an Na+ or pH gradient alone. These results suggested that both gradients stimulate PAH transport in BBMV via the same pathway. However, inhibition experiments with various organic anions showed that the specificities of Na+ and pH gradient-stimulated PAH uptake do not entirely overlap. Thus, our results support a simple transport in BBMV, but it cannot be excluded that two separate pathways are involved.

Aminohippuric Acids↗
PubMed1985

Morphological and physiological studies of rat kidney cortex slices undergoing isosmotic swelling and its reversal: a possible mechanism for ouabain-resistant control of cell volume.

Slices of rat kidney cortex were induced to swell by preincubation at 1 degree C in an isotonic Ringer's solution, and their capacity to reverse swelling, by net extrusion of cellular water, was studied during subsequent incubation at 25 degrees C. The recovery from swelling was prevented by the respiratory inhibitor, antimycin A. On the other hand, extrusion of water was little affected by ouabain. The extrusion of water continuing in the presence of ouabain (but not that in its absence) was significantly reduced when furosemide was added or when medium Cl- was replaced by NO-3 or I-. There was substantial variability in the morphological appearance of cells within the cortical slices. Different segments of the nephron showed different structural changes during swelling and its reversal, the proximal tubules being most markedly affected. Proximal tubular cells of swollen slices showed disorganization of brush borders and expansion of their apical surfaces, and contained vesicles in their apical cytoplasm. Upon recovery at 25 degrees C, the apical portions of these cells showed reversal of the expansion, but some apical vesicles remained. These vesicles were much more numerous after recovery in the presence of ouabain, but they were much reduced in numbers, or totally absent, when recovery took place in the presence of furosemide or absence of Cl-, with or without ouabain. The vesicles seen in the presence of ouabain alone appeared to fuse with each other and with infoldings of the basolateral plasma membrane. Rather similar results were obtained with distal tubular cells in the slices. We suggest that volume regulation in the proximal and distal tubular cells proceeds by way of two mechanisms. The first consists of extrusion of water coupled to the ouabain-sensitive transport of Na+ and K+. The other proceeds by way of an ouabain-resistant entry of water into apical cytoplasmic vesicles, following furosemide-sensitive movements of Cl- and Na+; the vesicles then expel their contents by exocytosis at the basolateral cell borders.

Animals↗
PubMed1969

Factors affecting the lactate dehydrogenase isoenzyme pattern of cultured kidney-cortex cells.

1. The lactate dehydrogenase isoenzyme pattern of cultured calf kidney-cortex cells was correlated to growth phase, changes in oxygen supply, mean generation time and changes in nutritional supply. 2. During culture of free cells and intact explants the lactate dehydrogenase isoenzyme pattern changed towards a dominance of isoenzymes containing the M subunit. 3. Of the shift in monomer proportion, 58% occurred during the lag phase and 42% during the initial part of the exponential growth phase. During the stationary phase the shift in monomer proportion reversed slightly. It was possible to relate the observed shift in monomer proportion to the glycolytic rate. 4. Factors that depressed glycolysis decreased the shift in monomer proportion. Oxygen was found to limit the decrease in the H subunit/M subunit ratio caused by anaerobic culture in vitro. 5. The results obtained support the view that the altered lactate dehydrogenase isoenzyme pattern of urine in renal ischaemia may be explained by anaerobic changes in the lactate dehydrogenase isoenzyme pattern of cortical tubule cells.

Animals↗
PubMed1967

Control of glycolysis and gluconeogenesis in rat kidney cortex slices.

1. Glucose uptake or glucose formation has been studied in kidney cortex slices to investigate metabolic control of phosphofructokinase and fructose-diphosphatase activities. 2. Glucose uptake is increased and glucose formation is decreased by anoxia, cyanide or an uncoupling agent. Under these conditions the intracellular concentrations of glucose 6-phosphate and ATP decreased whereas that of fructose diphosphate either increased or remained constant, and the concentrations of AMP and ADP increased. 3. Glucose uptake was decreased, and glucose formation from glycerol or dihydroxyacetone was increased, by the presence of ketone bodies or fatty acids, or after starvation of the donor animal. Under these conditions, the concentrations of glucose 6-phosphate and citrate were increased, whereas those of fructose diphosphate and the adenine nucleotides were unchanged (see also Newsholme & Underwood, 1966). 4. It is concluded that anoxia and cell poisons increase glucose uptake and decrease gluconeogenesis by stimulating phosphofructokinase and inhibiting fructose diphosphatase, whereas ketone bodies, fatty acids or starvation increase gluconeogenesis and decrease glucose uptake through the citrate inhibition of phosphofructokinase.

Acetoacetates↗
PubMed1984

Secretion of active and inactive renin by rabbit kidney cortex slices: effects of verapamil, flunarizine and A23187.

Secretion control for active and inactive (acid-activatable) renin was investigated using a rabbit kidney cortex slice preparation. In complete Krebs-Ringer bicarbonate buffer (pH 7.4) the calcium-channel-blocking drugs verapamil (50 microM) and flunarizine (50 microM) had no effect on active renin release but increased inactive renin secretion. In Ca-free or Ca-depleted (+EGTA) buffers secretion of both active and inactive renin was increased. Neither verapamil nor flunarizine under these conditions had any additional effect on active renin secretion but inactive renin release was stimulated by verapamil and inhibited by flunarizine. Although having no effect in the presence of Ca++ ions, the ionophore A23187 (17 microM) selectively abolished the secretion of inactive renin in the absence of calcium. The mechanisms regulating the secretion of the two forms of renin are clearly not identical. Differential release of active and inactive renin by the kidney may contribute to the overall control of the renin-angiotensin system.

Animals↗
PubMed1995

Identification of drugs subtype-selective for alpha 2A-, alpha 2B-, and alpha 2C-adrenoceptors in the pig cerebellum and kidney cortex.

The radioligands [3H]MK912 and [3H]RX821002 were used to label alpha2A-, alpha2B-, and alpha2C-adrenoceptors of the pig cerebellum and kidney cortex. By inclusion of the alpha2A-adrenoceptor-selective drug, BRL44408, and using a 'multi-curve' experimental design all the three porcine alpha2-adrenoceptor subtypes could be characterized pharmacologically. The data indicate that the pig alpha2-adrenoceptor subtypes are pharmacologically more related to human alpha2-adrenoceptor subtypes than to the rodent alpha2-adrenoceptors. We suggest a set of drugs that are useful for the delineation of the pig alpha2-adrenoceptor subtypes.

Animals↗
PubMed1980

Kininogenase activity in plasma membranes and cell organelles from rabbit kidney cortex: subcellular localization of renal kallikrein by free-flow electrophoresis and density-gradient fractionation.

Subcellular fractions were prepared from a rabbit kidney cortex homogenate by density gradient and free-flow electrophoresis techniques. After enzymatic and morphologic characterization, we determined the kininogenase activity in the different fractions. This activity was present in those plasma membranes that also contained high specific activities Na-K-ATPase and in lysosomal-like particles. No activity was found in the lumen, that is, the microvillous part of the proximal tubule cell. The kallikrein-like nature of this kininogenase activity was established by several methods.

Animals↗
PubMed1986

Analytical study on Na-K-ATPase (and cysteine insensitive p-nitrophenylphosphatase) in rat kidney-cortex microsomes subfractioned by zonal centrifugation.

The common use of Na-K-ATPase as a marker enzyme for basolateral membranes in the kidney is based on the microscopic localization of the enzyme by the cytochemical assay of Na-K-ATPase as cysteine insensitive p-nitrophenylphosphatase (Ernst S.A., J. Cell Biol. 66, 586-606, 1975). Rat kidney cortex plasma membranes were therefore fractionated by differential pelleting in isotonic sucrose, followed by equilibrium banding in linear sucrose gradients, to compare the distribution of "biochemical" and "cytochemical" assayed Na-K-ATPase. In all fractions, the distribution of Na-K-stimulated Mg-dependent ATPase differed from the distribution of cysteine insensitive p-nitrophenylphosphatase (alkaline phosphatase). Evidence is presented that this difference is not only due to the separation of plasma membranes from different cell types, but simply reflects different membrane location of the enzymic activities.

4-Nitrophenylphosphatase↗
PubMed1993

Effect of 13-hydroperoxyoctadecadienoic acid on 15-hydroxy prostaglandin dehydrogenase activity in rabbit kidney cortex.

The effect of a hydroperoxy adduct of linoleic acid, 13-hydroperoxyoctadecadienoic acid (13-HPODE), on 15-hydroxy prostaglandin dehydrogenase activity in rabbit kidney cortex was examined. 13-HPODE inhibited the 15-hydroxy prostaglandin dehydrogenase activity at concentrations ranging from 1 to 10 microM. The effect was concentration-dependent and the concentration required for 50% inhibition was approximately 3 microM. Linoleic acid and 13-hydroxyoctadecadienoic acid (13-HODE) exhibited weaker inhibition of the enzyme activity than did 13-HPODE (linoleic acid, 30% inhibition at 10 microM; 13-HODE, 45% inhibition at 10 microM). Studies utilizing Fe2+ (a catalyst of peroxide decomposition), and mannitol or dimethylsulfoxide (a hydroxy radical scavenger) revealed that the inhibitory effect of 13-HPODE on the 15-hydroxy prostaglandin dehydrogenase activity is not due to the hydroxy radicals which are expected to be formed from 13-HPODE and that the hydroperoxy functional group is a prerequisite. The inhibition by 13-HPODE was uncompetitive and non-competitive with regard to NAD+ and prostaglandin E2, respectively. These results suggest that 13-HPODE has the potential to modulate the prostaglandin catabolism by affecting the 15-hydroxy prostaglandin dehydrogenase activity.

Animals↗
PubMed1990

Microsomal hexose-6-phosphate and 6-phosphogluconate dehydrogenases in extrahepatic tissues: human placenta and pig kidney cortex.

An oxidative pathway of glucose-6-phosphate was found in the microsomal fraction of two extra-hepatic tissues: human placenta and pig kidney cortex. Oxidation activity in microsomes, measured by the formation of 14CO2 from [1-14C] glucose-6-phosphate, was observed only after Triton X-100 treatment and in the presence of methylene blue and NADP. Hexose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase were present in a latent form and required treatment with detergent for full activation. Our results suggest that these enzymes are located in the luminal space of placental and kidney microsomes, and that, as in the liver, they generate NADPH on the inner side of the endoplasmic reticulum when G6P and NADP are available.

Animals↗
PubMed1987

Cadmium in kidney cortex of inhabitants of North-West Germany: its relationship to age, sex, smoking and environmental pollution by cadmium.

The cadmium concentration in kidney cortex (CdKc) was determined in 388 deceased persons, who at the time of death had lived in the cities of Düsseldorf and Duisburg, Federal Republic of Germany (FRG), and surrounding areas. The average CdKc concentration was found to be 17.1 micrograms/g wet weight. Individual values range from less than 0.4 to 94.3 micrograms/g wet weight. The CdKc levels rapidly increase during the first decades of life. At the age of about 40 years, a plateau phase is reached. At high ages (greater than 70 years), the CdKc levels tend to decrease. Cigarette smokers have significantly higher CdKc concentrations than non-smokers. The increase of CdKc depends on the number of cigarettes smoked. Cigar and pipe smokers have slightly increased CdKc levels compared to non-smokers. Non-smokers who had spent the major part of their life in the area of Duisburg, a cadmium-polluted area, have, on the average, significantly higher CdKc levels than non-smokers from the less-polluted surrounding areas. In smokers the residential factor is masked by the effect of cigarette smoking.

Adult↗
PubMed1990

The effect of selenium ions on the catabolism of prostaglandin E2 in rabbit kidney cortex.

The effect of selenium ions on the catabolism of prostaglandin E2 by 15-hydroxy prostaglandin dehydrogenase and prostaglandin delta 13 reductase in rabbit kidney cortex was examined. Selenium ions had no effect on the 15-hydroxy prostaglandin dehydrogenase activity. On the other hand, selenium ions inhibited the prostaglandin delta 13 reductase activity at concentrations ranging from 0.05 to 0.5 mM. The effect was concentration-dependent. The inhibition by selenium ions was non-competitive with regard to NADH and 15-keto PGE2, respectively. These results suggest that selenium ions have the potential to increase 15-keto PG levels in the kidney by inhibiting the prostaglandin delta 13 reductase activity and that such action of selenium ions may participate in renal damage of selenium poisoning.

Animals↗
PubMed1988

Urodilatin (CDD/ANP-95-126) is not biologically inactivated by a peptidase from dog kidney cortex membranes in contrast to atrial natriuretic peptide/cardiodilatin (alpha-hANP/CDD-99-126).

Atrial natriuretic peptide (CDD/ANP-99-126) is rapidly inactivated by a membrane preparations from dog kidney cortex. Inactivation occurs by cleavage of the ring structure in the position between Cys-105 and Phe-106. A unique proteolytic product separated by HPLC on reverse-phase column appears as a single peak which elutes prior the intact peptide. In contrast, CDD/ANP-95-126 (urodilatin) which is released from the kidney is not destroyed by proteolysis using an identical membrane preparation.

Animals↗
PubMed1987

Degradation of atrial natriuretic factor by kidney cortex membranes. Isolation and characterization of the primary proteolytic product.

Synthetic rat atrial natriuretic factor (r-ANF, 1-28) was incubated with rat kidney cortex membranes, and a predominant degradation product was identified by reverse-phase high performance liquid chromatography. The degradation product was subjected to amino acid analyses and found to have a composition identical to r-ANF. Amino-terminal sequence analyses identified two distinct amino-terminal residues and suggested that cleavage had occurred between the cysteine-phenylalanine bond (residues 7 and 8) of r-ANF. This degradative process could be inhibited by 1,10-phenanthroline and EDTA, suggesting that the enzyme responsible for proteolysis is a metalloendoprotease. The enzyme exhibits a Michaelis-Menten constant of approximately 10 microM for the metabolism of r-ANF and has a broad pH optimum between 8.5 and 9.5. These findings suggest that ANF may be initially degraded in the kidney at a single cleavage site within the 17-residue ring structure.

Amino Acid Sequence↗