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PubMed1990

Studies on the metabolism of glycolyl-CoA.

Glycolyl-CoA can be formed during the course of the beta-oxidation by rat liver mitochondria of 4-hydroxybutyrate. The existence of this beta-oxidation has been previously supported by the occurrence of 4-hydroxybutyrate and its beta-oxidation catabolites in urine from patients with 4-hydroxybutyric aciduria, an inborn error of gamma-aminobutyric acid metabolism due to the deficiency of succinic semialdehyde dehydrogenase. The characteristics of the mitochondrial beta-oxidation of 4-hydroxybutyrate were, in rat liver, compared with those of the mitochondrial beta-oxidation of butyrate. The inhibition by malonate of the oxidation of 4-hydroxybutyrate was about twofold weaker than that of oxidation of butyrate, whereas both oxidations were abolished by preincubating the mitochondria with 1 mM valproic acid, a known inhibitor of mitochondrial beta-oxidation. Mitochondria from rat kidney cortex were demonstrated to catalyse, as previously shown for hepatic mitochondria, the carnitine-dependent oxidation of 12-hydroxylauroyl-CoA-omega-Hydroxymonocarboxylyl-CoAs are thus concluded to be precursors of glycolyl-CoA also in rat kidney cortex. In addition, 3-hydroxypyruvate was found to be a precursor of glycolyl-CoA, since it was oxidized by bovine heart pyruvate dehydrogenase with a cofactor requirement similar to that of pyruvate oxidation. Glycolyl-CoA was a substrate of carnitine acetyltransferase (pigeon breast muscle). Pig heart citrate synthase was capable of catalyzing the condensation of glycolyl-CoA with oxaloacetate. The product of this reaction induced low NADH production rates dependent on the addition of porcine heart aconitase and isocitrate dehydrogenase.

Acetate-CoA Ligase↗
PubMed1989

Cadmium exposure in Denmark. Based on analyses of liver and kidney tissues.

To determine the cadmium exposure level in the Danish population, tissue samples of kidney and liver were collected over the period 1981 to 1987 at the Institutes of Forensic Medicine in Copenhagen, Odense and Aarhus. A total of 795 samples were collected, of which 143 were selected for analysis using, the criteria sudden violent death (accident, homicide or suicide). Cadmium concentrations in kidney cortex increased by age to a maximum of approximately 22 micrograms/g/g (w/w) in the age group 45-55 years and decreased in the older age group, while liver concentrations tended to increase throughout the entire lifespan. Cadmium concentrations in kidney cortex and liver were found significantly correlated. The findings are in good agreement with internationally published data, but lower than previously reported Danish concentration levels. The reason for this difference is discussed.

Adolescent↗
PubMed2000

Regulation of renal artery smooth muscle tone by alpha1-adrenoceptors: role of voltage-gated calcium channels and intracellular calcium stores.

The ischemia induced vasospasm of the renal arterial blood vessels mediated by alpha1-adrenoceptors is of importance for the loss of kidney function. This is based on reduced perfusion of the kidney cortex occurring in kidney transplant and organ preserving surgery. The present study considered the intracellular mechanism of the norepinephrine (NE) induced renal artery vasospasm by using swine renal artery smooth muscle ring. Norepinephrine and phenylephrine (PE) induced dose-dependent and fully reversible isometric contractions with a threshold concentration of 10 nM (n = 7) and 10 nM (n = 4), and an EC50 of 0.3 microM and 1 microM, respectively. The receptor was identified as alpha1A-subtype. The contraction was completely inhibited by verapamil (IC50 = 1.51 microM; n = 11) and diltiazem (IC50 = 9.49 microM; n = 8) and 85% by nifedipine (IC50 = 0.13 microM; n = 21). Blockade of the intracellular inositol- 1,4,5-trisphosphate (IP3)-sensitive Ca2+ store by thapsigargin (1 microM, n = 7) or suppression of Ca2+ release from the intracellular Ca2+-sensitive Ca2+ store by ryanodine (100 microM, n = 4) inhibited the PE induced contraction by 39.5% and 47.6%, respectively. The results suggest a key role of voltage-dependent Ca2+ channels and intracellular Ca2+ stores in the alpha1A-adrenoceptor induced contraction of the renal artery.

Adrenergic alpha-Agonists↗
PubMed1984

Metabolism of different molecular forms of adenosine deaminase intravenously infused into the rabbit.

High-Mr and monomeric adenosine deaminase were injected intravenously into the rabbit. The rates of clearance and sites of uptake of the enzymes were compared. Calf intestinal mucosa served as the source of monomeric adenosine deaminase. High-Mr enzymes were assembled in vitro from the calf enzyme and adenosine deaminase-complexing proteins isolated from rabbit plasma or kidney. An immunoassay specific for calf adenosine deaminase was used to determine which organs took up the injected enzyme. The enzymes were cleared from circulation in the following order: monomeric adenosine deaminase greater than high-Mr enzyme prepared with kidney complexing protein greater than high-Mr enzyme prepared with plasma complexing protein. High-Mr enzyme assembled with kidney complexing protein was taken up primarily by the liver. Complexing protein and adenosine deaminating activity were cleared from circulation at similar rates. This and other evidence indicate that kidney complexing protein and calf adenosine deaminase are taken up as a unit by the liver. In contrast, adenosine-deaminating activity was cleared more quickly from circulation than complexing protein in rabbits injected with enzyme prepared with plasma complexing protein. Immunoassay results indicated that calf adenosine deaminase was taken up principally by the kidney cortex and liver. Kidney was the major site of uptake of monomeric adenosine deaminase. Indirect immunoperoxidase staining was used to localize the calf enzyme in glomeruli and proximal renal tubules, the same areas in which rabbit complexing protein is localized. These results support the hypothesis that complexing proteins play a role in the clearance of adenosine deaminase from plasma [W.P. Schrader and P.J. Bryer (1982) Arch. Biochem. Biophys. 215, 107-115].

Adenosine Deaminase↗
PubMed1986

Heterogeneity of mammalian alpha 2-adrenoceptors delineated by [3H]yohimbine binding.

[3H]Yohimbine binding to membrane preparations of human colon, cerebral cortex, kidney, spleen and platelets was compared with binding to preparations of animal tissues (rabbit spleen, kidney and cerebral cortex; rat cerebral cortex; guinea-pig and cat spleen). Specific binding to all preparations was saturable and indicative of binding to a uniform population of sites. The equilibrium dissociation constants (KD) of [3H]yohimbine ranged from 1.6 to 2.6 nM for human tissue and from 5.1 to 9.4 nM for the animal tissues. Binding to all tissues was displaced by drugs with an order of potency yohimbine greater than phentolamine greater than prazosin, indicating an alpha 2-adrenoceptor classification of the labelled sites. Whilst certain drugs (phentolamine, corynanthine) possessed similar affinities for all alpha 2-adrenoceptors, others (prazosin, idazoxan, WY 26392) exhibited differential potencies for alpha 2-adrenoceptors in certain species. The pharmacological characteristics of human alpha 2-adrenoceptors were conserved within the tissues examined. These results suggest that human alpha 2-adrenoceptors differ in a number of ways from those present in tissues from the other mammalian species examined. The possible existence of a spectrum of alpha 2-adrenoceptors is discussed in the light of these findings.

Animals↗
PubMed1998

Experimental evaluation of two simple thermal models using transient temperature analysis.

Thermal models are used to predict temperature distributions of heated tissues during thermal therapies. Recent interest in short duration high temperature therapeutic procedures necessitates the accurate modelling of transient temperature profiles in heated tissues. Blood flow plays an important role in tissue heat transfer and the resultant temperature distribution. This work examines the transient predictions of two simple mathematical models of heat transfer by blood flow (the bioheat transfer equation model and the effective thermal conductivity equation model) and compares their predictions to measured transient temperature data. Large differences between the two models are predicted in the tissue temperature distribution as a function of blood flow for a short heat pulse. In the experiments a hot water needle, approximately 30 degrees C above ambient, delivered a 20 s heating pulse to an excised fixed porcine kidney that was used as a flow model. Temperature profiles of a thermocouple that primarily traversed the kidney cortex were examined. Kidney locations with large vessels were avoided in the temperature profile analysis by examination of the vessel geometry using high resolution computed tomography angiography and the detection of the characteristic large vessel localized cooling or heating patterns in steady-state temperature profiles. It was found that for regions without large vessels, predictions of the Pennes bioheat transfer equation were in much better agreement with the experimental data when compared to predictions of the scalar effective thermal conductivity equation model. For example, at a location r approximately 2 mm away from the source, the measured delay time was 10.6 +/- 0.5 s compared to predictions of 9.4 s and 5.4 s of the BHTE and ETCE models, respectively. However, for the majority of measured locations, localized cooling and heating effects were detected close to large vessels when the kidney was perfused. Finally, it is shown that increasing flow in regions without large vessels minimally perturbs temperature profiles for short exposure times; regions with large vessels still have a significant effect.

Angiography↗
PubMed1999

Characterization of Na+/HCO-3 cotransporter isoform NBC-3.

Na+-HCO-3 cotransporters mediate the transport of HCO-3 into or out of the cell. Two Na+-HCO-3 cotransporters (NBC) have been identified previously, which are referred to as NBC-1 and NBC-2. A cDNA library from uninduced human NT-2 cells was screened with an NBC-2 cDNA probe. Several clones were identified and isolated. Sequence analysis of these clones identified a partial coding region (2 kb) of a novel NBC (called here NBC-3), which showed 53% and 72% identity with NBC-1 and NBC-2, respectively. Northern blot analysis revealed that NBC-3 encodes a 4.4-kb mRNA with a tissue distribution pattern distinct from NBC-1 and NBC-2. NBC-3 is highly expressed in brain and spinal column, with moderate levels in trachea, thyroid, and kidney. In contrast with NBC-1, NBC-3 shows low levels of expression in pancreas and kidney cortex. In the kidney, NBC-3 expression is predominantly limited to the medulla. Cultured mouse inner medullary collecting duct (mIMCD-3) cells showed high levels of NBC-1 and low levels of NBC-3 mRNA expression. Subjecting the mutagenized mIMCD-3 cells to sublethal acid stress decreased the mRNA expression of NBC-1 by approximately 90% but increased the Na+-dependent HCO-3 cotransport activity by approximately 7-fold (as assayed by DIDS-sensitive, Na+-dependent, HCO-3-mediated intracellular pH recovery). This increase was associated with approximately 5.5-fold enhancement of NBC-3 mRNA levels. NBC showed significant affinity for Li+ in the mutant but not the parent mIMCD-3 cells. On the basis of the widespread distribution of NBC-3, we propose that this isoform is likely involved in cell pH regulation by transporting HCO-3 from blood to the cell. We further propose that enhanced expression of NBC-3 in severe acid stress could play an important role in cell survival by mediating the influx of HCO-3 into the cells.

Acids↗
PubMed1989

The fate and uptake of murine epidermal growth factor in the sheep.

125I-Labelled murine epidermal growth factor (EGF) was injected or infused into conscious ewes through the jugular vein. Its disappearance from the circulation and the pattern of its distribution in other body tissues and compartments were observed. Single bolus injections of 125I-labelled EGF resulted in a transient peak of radioactive EGF in the circulation which occurred within 1 min of the injection. This was followed by a very rapid fall in radioactivity in the plasma (t1/2 approximately 1 min) and the gradual appearance of 125I-labelled EGF in the urine. Immunoprecipitable 125I-labelled EGF could be detected in urine within 5 min of the start of the experiment. 125I-Labelled EGF accumulated in the urine for several hours following the injection, although with increasing time a substantial amount of non-immunoprecipitable iodide was also found. The rate of disappearance of the 125I-labelled EGF from the plasma of the ewe was found to be faster than the rate of disappearance of free [125I]iodide that had been injected into the ewe. 125I-Labelled EGF was also administered by a continuous infusion following an initial bolus injection. This again resulted in a rapid initial fall in radioactivity in blood, followed by a slow rise throughout the period of the infusion. When the infusion was stopped, there was a 15-min period of rapid readjustment, after which the radioactivity in the blood fell at a much slower rate (t1/2 approximately 70 min) than was seen initially. Again, intact 125I-labelled EGF was transferred to urine throughout the experiment. At autopsy, 125I-labelled EGF was increased in bile, liver, thyroid and kidney. Although most of the 125I found in the thyroid was free iodide, some EGF-like material was also present. There was also EGF-like material found in both the kidney cortex and the kidney medulla. These results indicate that complex multi-compartment pathways for the uptake, distribution and clearance of 125I-labelled EGF exist in the sheep.

Animals↗
PubMed2001

Reconstruction of dynamic renal tomographic data acquired by slow rotation.

UNLABELLED: Nuclear medicine renal studies can be performed using slow-rotation SPECT, but reconstruction of such data is largely underdetermined. METHODS: A new method of reconstruction of data acquired using slow camera rotations was developed. In this method we used a factor model of the data in which the factors and factor coefficients were determined by modeling their relationship directly with the projection measurements. This was done by solving a least-squares problem that fits the projections of factors and factor coefficients to the projection data with nonnegativity constraints imposed on the solution. The method was tested on computer simulations and applied to experimental renal (99m)Tc-mercaptoacetyltriglycine canine and patient studies. RESULTS: Computer simulations showed that the extracted time-activity curves of kidneys agreed well with the simulated curves for data with noise levels similar to those in the experimental studies. In the canine study, the method showed that >2 factors were necessary to adequately reproduce the kinetics of the kidney. In the patient study, the method was able to extract separate factors that correspond to the kidney cortex and the kidney pelvis. CONCLUSION: The computer simulation, the canine study, and the patient study all show that reconstructions of the data obtained with 1 detector displayed artifacts, whereas reconstructions of the data obtained with 2 and 3 detectors were free of artifacts. Computer simulations showed that the method gives accurate results that allow quantitation.

Algorithms↗
PubMed1992

Laminin B1 is preferentially expressed in the cortex of rat kidney and is not affected by cyclosporine administration.

Cyclosporine has proven beneficial as an immunosuppressive agent for organ rejection in kidney transplants as well as in heart and liver transplants. Cyclosporine administration, however, is associated with certain adverse effects, one of the most important being chronic nephrotoxicity characterized by focal cortical scarring. Recent experimental data show involvement of type I and possibly type IV collagens in this process. Because laminin represents another potential extracellular matrix target, we examined the effects of cyclosporine administration in rats on the expression of laminin at the messenger ribonucleic acid (mRNA) and protein levels. In untreated normal rats, laminin B1 mRNA is preferentially expressed in the renal cortices, as demonstrated by northern blots. Daily administration of cyclosporine leads to focal cortical interstitial fibrosis and tubular atrophy by 4 weeks with, as shown previously, elevated procollagen alpha-1 (type I) mRNA levels at 1 and 4 weeks. In contrast, the amounts of message for laminin B1 remain identical after 1 week and 4 weeks of cyclosporine administration, despite the development of fibrosis at 4 weeks. Similar results were obtained with antilaminin antibody. We conclude that laminin is abundant in renal cortical tissues as compared with its medullary contents and is not altered in the process of renal cortical fibrosis induced by cyclosporine.

Animals↗
PubMed1997

Metabolism of dexamethasone in the human kidney: nicotinamide adenine dinucleotide-dependent 11beta-reduction.

Recently, two distinct isoenzymes of 11beta-hydroxysteroid-dehydrogenase (11beta-HSD) have been cloned and characterized in several species: The isoenzyme 11beta-HSD-I is widely distributed, bidirectional, prefers NADP(H) and has a low substrate affinity. The isoenzyme 11beta-HSD-II seems to exclusively oxidize physiological glucocorticoids, uses NAD as cosubstrate, has high substrate affinity, and is only found in mineralocorticoid target tissues and the placenta. Synthetic steroids fluorinated in position 9, however, are rapidly reduced by human kidney cortex slices. We attempted to find out which isoenzyme is responsible for this unexpected reductase activity. We studied the 11beta-HSD activity towards cortisol (F)/cortisone (E) and dexamethasone (D)/11-dehydro-dexamethasone (DH-D) in microsomes prepared from human kidney cortex. For the reaction E to F (not for DH-D to D!), glucose-6-phosphate and glucose-6-phosphate-dehydrogenase had to be added as a NADH/NADPH-regenerating system. Oxidation of F to E: NAD was the exclusively used cosubstrate; the affinity [Michael's constant (Km) for F = 25.5 nmol/L] and the maximum velocity (Vmax = 22.9 nmol/mg/min) were high. Reduction of E to F: Without the NADH/NADPH-regenerating system, this reaction was very slow. With this system, the Km value for E was in the nanomolar range (80.6 nmol/L) and the Vmax value was very low (0.88 nmol/mg/min). The reaction was clearly NADH-preferring. For the steroid pair F/E, the quotient Vmax(oxidation)/Vmax(reduction) (=26) demonstrates an equilibrium far on the 11-keto side. Oxidation of D to DH-D: With NAD as the only used cosubstrate, the kinetic analysis is compatible with the existence of two different NAD-dependent isoenzymes: Km for D = 327 nmol/L, Vmax = 53.5 nmol/mg/min and Km for D = 81.2 nmol/L; Vmax = 20.4 nmol/mg/min. Reduction of DH-D to D: The maximum velocity was higher than that of all other reactions tested: Vmax = 226.0 nmol/mg/min. The reaction was exclusively NADH-dependent; the Km value for DH-D was 68.4 nmol/L. For D/DH-D, the ratio Vmax(oxidation)/Vmax(reduction) was 0.24, demonstrating a shift to reductase activity with the reaction equilibrium far on the 11-hydroxy side. The reaction F to E was inhibited by E, DH-D, and D in a concentration-dependent manner. In conclusion, the cosubstrate dependence, the Km value of the oxidation of F and the product inhibition are in good correspondence with data for the cloned human 11beta-HSD-II. The NADH-dependent 11beta-reduction of E and especially of DH-D are inconsistent with the dogma of an unidirectional 11beta-HSD-II. The preference of D for the reductase reaction in human kidney slices is probably caused by the fluor atom in position 9, is catalyzed by 11beta-HSD-II, and leads to an activation of 11-DH-D to D in the human kidney.

11-beta-Hydroxysteroid Dehydrogenases↗
PubMed1993

Molecular cloning and characterization of p64, a chloride channel protein from kidney microsomes.

Chloride channels were previously purified from bovine kidney cortex membranes using a drug affinity column. Reconstitution of the purified proteins into artificial liposomes and planar bilayers yielded chloride channels. A 64-kDa protein, p64, identified as a component of this chloride channel was used to generate antibodies which depleted solubilized kidney membranes of all chloride channel activity. This antibody has now been used to identify a clone, H2B, from a kidney cDNA library. Antibodies, affinity-purified against the fusion protein of H2B also depleted solubilized kidney cortex from all chloride channel activity. The predicted amino acid sequence of p64 shows that it contains two and possibly four putative transmembrane domains and potential phosphorylation sites by protein kinase A, protein kinase C, and casein kinase II. There was no significant homology to other protein (or DNA) sequences in the data base. The protein is expressed in all cells tested. Expression of its mRNA in Xenopus laevis oocytes led to the insertion of a protein with the appropriate molecular mass in microsomes but not in the plasma membrane. It is likely that p64 represents the chloride channel of intracellular organelles.

Amino Acid Sequence↗
PubMed1975

Influence of chronic exposure to cadmium on hepatic and renal cyclic AMP-protein kinase system.

Daily intraperitoneal injection of cadmium chloride (0.25 or 1 mg/kg) to rats for 45 days significantly elevated the endogenous levels of cyclic AMP (cAMP) in hepatic tissue. However, the cAMP binding to hepatic protein kinase was decreased following cadmium administration, as was the kinase activity ratio. Although both doses of cadmium produced slight alterations in the cAMP-independent form of hepatic protein kinase, only the 1.0 mg/kg dose significantly depressed (24%) the activity of the cAMP-dependent enzyme. In contrast to liver, chronic exposure to cadmium significantly reduced the endogenous cAMP levels in kidney cortex. Although treatment with the lower dose (0.25 mg/kg) failed to alter either the cAMP-binding capacity of the renal enzyme or the kinase activity ratio, the higher dose (1 mg/kg) of cadmium did cause a significant increase in both parameters. In addition, cadmium treatment produced a significant decrease in both the cAMP-dependent and the independent forms of protein kinase in kidney cortex. Data suggest that the concentration of cAMP as well as its interaction with cAMP-dependent and independent forms of protein kinase, are altered in both kidney and liver following the prolonged exposure to cadmium.

Animals↗
PubMed1984

Enzymatic adaptations to asphyxia in the harbor seal and dog.

The activities of the glycolytic enzymes were determined in heart, liver, kidney cortex and cerebrum from the harbor seal (Phoca vitulina ) and the adult and newborn dog. Activities were similar in the four dog tissues as well as myocardium and brain tissue from both the newborn dog and seal. Most of the enzyme activities were markedly lower in kidney cortex and liver of the seal and the newborn dog, suggesting that the organs which are rendered ischemic in the diving seal or asphyxiated newborn dog have a lowered demand for glycolytic metabolism. This is perceived as an adaptation to prolong the time tissues can rely on anaerobic metabolism. Expression of the enzyme data in a 'similarity criterion' by dividing activity from an organ likely to be perfused during long diving or asphyxia (e.g., heart), by that from one rendered ischemic (e.g., kidney), yields a quotient which provides a convenient indicator of anaerobic potential. Such a treatment would reflect the contribution of a discrete tissue to the total anaerobic demand of the whole animal. The values thus generated for the glycolytic enzymes are generally higher in the seal and the newborn dog than in the adult dog, and suggest an index for determining the capacity of an animal to withstand repeated and variable asphyxia.

Adaptation, Physiological↗
PubMed1976

Effects of anti-inflammatory agents and some other drugs on prostaglandin biotransport.

The inhibitory effects of drugs on prostaglandin biotransport were studied by measuring the concentrative accumulation of 3H by rabbit choroid plexuses, segments of anterior uvea and kidney cortex slices after incubation in tissue culture medium containing 3H-prostaglandin F2 alpha. After 10 minutes of incubation in the absence of an inhibitor, the choroid plexus showed a tissue/medium 3H accumulation ratio of 14 +/- 0.7; after 30 minutes of incubation, the anterior uvea and the kidney cortex slices showed accumulation ratios of 6.4 +/- 0.5 and 5.6 +/- 0.1, respectively. The I50 values for inhibition of 3H accumulation by indomethacin were 10, 8 and 12 muM for the three tissues, respectively. Some related drugs-oxyphenbutazone, D-naproxen, l-naproxen, ibuprofen, phenylbutazone and pirprofen-were also found to be effective inhibitors of 3H accumulation (I50 for anterior uvea, 6-28 muM) whereas aspirin, dexamethasone phosphate and penicillin had an inhibitory effect only at much higher concentrations (I50 0.1-2.0 mM). Papaverine, fursemide and probenecid were approximately as effective as the anti-inflammatory organic acids (I50 0.01-0.1 mM), whereas bromcresol green was at least 10-fold more effective. Diphenhydramine and the nonacidic prostaglandin synthesis inhibitors, phenelzine and paracetamol, showed little (I50 greater than 1 mM) or no inhibitory effect. The inhibition of this transport system by some drugs, most notably nonsteroidal anti-inflammatory organic acids, and consequent alterations in the distribution and disposition of prostaglandins must be taken into account in the development of new anti-inflammatory agents and in the interpretation of the mechansim of action and side effects of such drugs.

Animals↗
PubMedDate not supplied

Cloning of rabbit Cct6 and the distribution of the Cct complex in mammalian tissues.

Cct6 protein is one of the subunits of the Cct complex involved in ATP-dependent folding of cellular proteins. We used the cDNA of the human CCT6 subunit to obtain a full-length cDNA from a rabbit kidney cortex library. Two transcripts of 2 and 2.5 kb were detected in rabbit kidney and liver by Northern analysis. The rabbit CCT6 was 93% identical to the human gene; the deduced amino acid sequence was 97% identical. A phylogenetic analysis of Cct6 proteins from mouse, rabbit, human, and yeast showed greater similarities of Cct6 protein among the species than among other Cct subunits. The ATP-binding sites were perfectly conserved among mammals and yeast, supporting the role of Cct complex in ATP-dependent protein folding. Using a polyclonal antibody to human Cct6 protein and Western analysis, we found expression of this subunit in a variety of rabbit organs and tissues, as well as in bovine testes, human lymphocytes, human and rabbit reticulocytes, and in two cultured kidney cell lines. We also found Cct1 protein by Western analysis in several rabbit organs as well as in bovine testes. These data characterize the rabbit Cct6 subunit and compare it to its homologues. The Western analyses support the concept that Cct complex is widely distributed among tissues and highly conserved among eukaryotes.

Amino Acid Sequence↗
PubMed1976

Effects of stimulation and inhibition of the renal prostaglandin synthetase system on renin release in vivo and in vitro.

1. The prostaglandin precursor arachidonic acid (C20:4) increases plasma renin activity in the rabbit and rat when it is infused into the renal arteries. 2. The increase in plasma renin activity after C20:4 in rats is not changed by volume expansion. 3. The inhibitor of prostaglandin synthesis indomethacin decreases plasma renin activity in the rabbit. 4. The increase plasma in renin activity after total renal ischaemia is abolished by pretreatment with indomethacin. 5. C20:4 increases dose- and time-dependent renin release from slices of rabbit kidney cortex. 6. Indomethacin or 5,8,11,14-eicosatetraynoic acid pretreatment in vivo, and addition to the incubation medium, reduces basal as well as C20:4-stimulated renin release in vitro. 7. The stimulating effect of C20:4 on renin release is assumed to be caused directly by formation of prostaglandin endoperoxides in the kidney cortex and not by prostaglandins since in vitro a natural prostaglandin endoperoxide (PGG2) and two stable synthetic prostaglandin endoperoxide analogues (EPA I and EPA II) do increase the release of renin, but PGE2 has no effect and PGF2alpha inhibits renin release.

Animals↗