Modification of glycosylation of renin in sodium-depleted and captopril-treated rats

Concanavalin A (con A) chromatography of rat plasma revealed the presence of three differently glycosylated forms of renin, including the con A unbound form (renin C), the loosely bound form (renin A), and the tightly bound form (renin B). Rat renal cortical slices in vitro secreted all these forms. They had a different half-life in the plasma after ligation of both renal artery and vein (half-life of 21 +/- 1, 14 +/- 3, and 35 +/- 4 min for renin A, B, and C, respectively). Thus differently glycosylated forms of renin are released from the kidney into the blood circulation and disappear, with a different half-life. Rats were sodium-depleted and captopril-treated (40-60 mg.kg-1.day-1) for 2 wk, and the effects of these treatments on relative proportions of renin A, B, and C were investigated. These treatments elevated plasma renin concentration approximately 60-fold (from 24 +/- 3 to 1,406 +/- 128 ng angiotensin I.h-1.ml-1; P less than 0.01), in association with an increase in the relative percent of renin C in the plasma from 22 +/- 2 to 39 +/- 3% (P less than 0.01). Moreover, the relative proportion of renin C released from the renal cortical slices was significantly higher in the treated than in the control rats (42 +/- 9 vs. 16 +/- 3% of secreted renin, respectively; P less than 0.02). These results show that the predominant release of renin C, with the longest half-life (35 min) in the plasma, contributes to the increased plasma renin concentration in sodium-depleted and captopril-treated rats.

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Absence of Activation in Vitro of Renin in Rat Plasma

Clinical Science ◽

10.1042/cs0620435 ◽

1982 ◽

Vol 62 (4) ◽

pp. 435-437 ◽

Cited By ~ 5

Author(s):

M. H. De Keijzer ◽

A. P. Provoost ◽

F. H. M. Derkx

Keyword(s):

Human Plasma ◽

Active Form ◽

Plasma Renin ◽

Rat Plasma ◽

Plasma Renin Concentration ◽

Inactive Form ◽

Inactive Renin

1. Rat plasma was subjected at 4°C to various treatments known to convert inactive renin into its active form in human plasma. 2. No statistical differences in plasma renin concentration were found when the levels after the various treatments were compared with that of untreated rat plasma. 3. It is concluded that, in contrast to human plasma, no inactive form of renin is present in rat plasma.

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EXTRAHEPATIC AND EXTRARENAL RENIN INACTIVATION IN THE DOG

Journal of Endocrinology ◽

10.1677/joe.0.0600217 ◽

1974 ◽

Vol 60 (2) ◽

pp. 217-222

Author(s):

R. FAGARD ◽

E. FOSSION ◽

M. CAMPFORTS ◽

A. AMERY

Keyword(s):

Blood Vessels ◽

Pulmonary Circulation ◽

Plasma Renin ◽

Glass Container ◽

Plasma Renin Concentration ◽

Vascular Beds ◽

Extrarenal Renin

SUMMARY It was demonstrated previously that renin disappears quickly from the circulation after nephrectomy in the hepatectomized dog. In the present study the plasma renin concentration (PRC) was measured in the efferent and afferent blood vessels of several vascular beds (pulmonary circulation, splanchnic region, spleen, both inferior limbs and pelvis, head) in the anhepatic and in the anhepatic and anephric dog in order to investigate extrarenal and extrahepatic renin inactivation. However, no significant arteriovenous differences in PRC could be traced. The blood of these dogs kept in vitro at 37 °C in a glass container showed no decline in PRC within 3 h of removal. Therefore no specific extrahepatic and extrarenal renin-inactivating mechanism was found which could explain the rapid disappearance of renin from the blood in vivo in the anhepatic and anephric dog.

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Differential Effects of Cisplatin on the Production of NADH-Dependent Superoxide and the Activity of Antioxidant Enzymes in Rat Renal Cortical Slices in vitro

Pharmacology & Toxicology ◽

10.1111/j.1600-0773.1996.tb02087.x ◽

1996 ◽

Vol 79 (4) ◽

pp. 191-198 ◽

Cited By ~ 12

Author(s):

Jin-Gang Zhang ◽

W. Edward Lindup

Keyword(s):

Antioxidant Enzymes ◽

Differential Effects ◽

Rat Renal Cortical Slices ◽

Cortical Slices

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Effects of lactate and glutamine on palmitate metabolism in rat kindey cortex

American Journal of Physiology-Legacy Content ◽

10.1152/ajplegacy.1976.231.1.14 ◽

1976 ◽

Vol 231 (1) ◽

pp. 14-19 ◽

Cited By ~ 8

Author(s):

M Barac-Nieto

Keyword(s):

Renal Cortex ◽

Palmitate Oxidation ◽

The Media ◽

High Concentrations ◽

Rat Renal Cortical Slices ◽

Very High ◽

Cortical Slices ◽

Palmitate Metabolism ◽

Low Rate

Rat renal cortical slices were incubated with [1-(14)C]palmitate bound to 2.5% albumin. The following effects were found: a)1 mM palmitate utilization or oxidation to CO(2) varied according to the concentration of lactate in the media, it increased at 0.8 and 3.2 mM, was unchanged at 8 mM, and decreased at 16 mM. Esterification was stimulated at 3.2 mM lactate. b) Addition of glutamine (0.1 mM) instead of lactate stimulated incomplete and complete oxidation of palmitate (1 mM), whereas high medium glutamine (10 mM) inhibited palmitate (1 mM) utilization, esterification, and oxidation to CO(2) but increased its incomplete oxidation. The low rate of exogenous palmitate oxidation observed in this study and the finding that exogenous palmitate oxidation is only partially inhibited at very high concentrations of exogenous lactate or glutamine are consistent with the view that these exogenous substrates contribute little to the oxidative metabolism of rat renal cortex in vitro, which probably depends on the supply of substrates endogenous to the tissue.

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The Clearance of Endogenous Renin in the Anhepatic Anephric Dog

Clinical Science ◽

10.1042/cs045225s ◽

1973 ◽

Vol 45 (s1) ◽

pp. 225s-228s

Author(s):

R. Fagard ◽

E. Eyskens ◽

H. Delooz ◽

E. Fossion ◽

A. Amery

Keyword(s):

Plasma Renin ◽

Plasma Renin Concentration ◽

Rapid Fall ◽

Inferior Limb

1. A rapid fall in plasma renin concentration occurs not only in colonectomized but also in hepatectomized dogs after binephrectomy. 2. In the anhepatic anephric dog no renin extraction can be demonstrated across lungs, splanchnic region, spleen, inferior limb and head. 3. No renin inactivation occurs in blood kept in vitro at 37°C for 3 h taken from anaesthetized dogs and from the anhepatic anephric dogs. 4. We suggest that the clearance of renin in the anhepatic anephric dog is due to extraction or inactivation of renin by tissues in general.

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Amelioration of Cisplatin Toxicity in Rat Renal Cortical Slices by Dithiothreitol In vitro

Human & Experimental Toxicology ◽

10.1177/096032719401300205 ◽

1994 ◽

Vol 13 (2) ◽

pp. 89-93 ◽

Cited By ~ 17

Author(s):

J.G. Zhang ◽

L.F. Zhong ◽

M. Zhang ◽

X.L. Ma ◽

Y.X. Xia ◽

...

Keyword(s):

Lactate Dehydrogenase ◽

Protective Effect ◽

Protective Mechanism ◽

Protective Effects ◽

Metal Chelator ◽

Rat Renal Cortical Slices ◽

Antioxidative Action ◽

Cortical Slices ◽

Related Increase

1 The protective effects of dithiothreitol (DTT) on cisplatin-induced nephrotoxicity were investigated with rat renal cortical slices. 2 The nephrotoxic effects of cisplatin (2 mmol l-1) were manifested in several ways: the Na+ and water content were increased while K+ was decreased. The malondiadehyde (MDA) concentration in the slices and the lactate dehydrogenase (LDH) released into the medium were increased. The uptake of p-aminohippurate (PAH), the synthesis of glucose and the glutathione (GSH) concentration in the slices were all decreased. 3 Despite a DTT-related increase in platinum (Pt) uptake by the slices, DTT (0.5-2 mmol I-1 ) ameliorated all these toxic effects of cisplatin in a concentration related manner. 4 The results suggest that the protective mechanism of DTT is its antioxidative action, DTT is also a metal chelator, however, and so a protective effect via chelation of Pt by DTT cannot be excluded.

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Adenine nucleotide and calpain inhibitor I protect against atractyloside-induced toxicity in rat renal cortical slices in vitro

Archives of Toxicology ◽

10.1007/s002040100272 ◽

2001 ◽

Vol 75 (8) ◽

pp. 487-496 ◽

Cited By ~ 4

Author(s):

David Obatomi ◽

Richard Blackburn ◽

Peter Bach

Keyword(s):

Adenine Nucleotide ◽

Calpain Inhibitor ◽

Rat Renal Cortical Slices ◽

Cortical Slices

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Effect of tolbutamide on plasma renin activity.

AJP Endocrinology and Metabolism ◽

10.1152/ajpendo.1979.236.1.e1 ◽

1979 ◽

Vol 236 (1) ◽

pp. E1

Author(s):

N K Sherma ◽

V V Gossain ◽

A M Michelakis ◽

D R Rovner

Keyword(s):

Cyclic Amp ◽

Plasma Renin Activity ◽

Biological Significance ◽

Plasma Renin ◽

Renin Activity ◽

Control Group ◽

Cortical Slices ◽

Intact Rats

The effect of tolbutamide on renin secretion in rats was studied in vivo, and in vitro. Administration of tolbutamide in doses of 12.5 and 25 mg/kg body wt ip to two groups of rats produced no significant change in plasma renin activity compared to the control group. In the in vitro experiments renal cortical slices were incubated with increasing concentrations of tolbutamide (0--4 mg/ml). No significant increase in the net renin production was observed, whereas the concentration of cyclic AMP increased significantly in the incubation medium. These findings suggest that in the intact rats tolbutamide does not increase plasma renin activity. In the renal cortical experiments although tolbutamide increased cyclic AMP production, the increase may not have been sufficient to stimulate the net renin production. These results are of biological significance because of the possible effects of tolbutamide and increased plasma renin activity on the cardiovascular system.

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Mouse and rat plasma renin concentration and gene expression in (mRen2)27 transgenic rats

AJP Heart and Circulatory Physiology ◽

10.1152/ajpheart.1998.274.5.h1450 ◽

1998 ◽

Vol 274 (5) ◽

pp. H1450-H1456 ◽

Cited By ~ 4

Author(s):

Jürgen Bohlender ◽

Joel Ménard ◽

Oliver Edling ◽

Detlev Ganten ◽

Friedrich C. Luft

Keyword(s):

Gene Expression ◽

Rat Kidney ◽

Plasma Renin ◽

Rat Plasma ◽

Transgenic Rat ◽

Ribonuclease Protection Assay ◽

Kinetic Assay ◽

Ph Optimum ◽

Plasma Renin Concentration ◽

The Relationship

The (mRen2)27 transgenic rat [TGR(mRen2)27] is said to have low plasma levels of active renin. We used a direct radioimmunoassay (RIA) for mouse submaxillary renin, as well as an indirect enzyme-kinetic assay based on the generation of angiotensin I with modification of the pH optimum, to measure rat and mouse plasma renin activity (PRA), plasma renin concentration (PRC), and plasma prorenin in TGR before and after lisinopril. The relationship between rat PRC and %rat kidney extract was steepest at pH 6.0 and flat at pH 8.5, whereas the relationship between mouse PRC and purified mouse renin was steepest at pH 8.5 and flat at pH 6.0. Mouse PRC was highly correlated with direct RIA measurements ( r = 0.93). PRA before lisinopril was little influenced by pH, whereas the increase with lisinopril was greatest at pH 6.5. PRC before lisinopril was fourfold higher at pH 8.5 compared with that at pH 6.0. Lisinopril increased both PRC values but reversed the pH dependency. Prorenin was fourfold higher at pH 8.5 compared with that at pH 6.0 and decreased slightly with lisinopril. Renal renin concentration was higher at pH 6.0 than at pH 8.5. With lisinopril, renal renin concentration increased at both pH values. Mouse PRC was not changed by lisinopril. Ribonuclease protection assay showed both rat and mouse renin gene expression in the kidney, which increased with lisinopril. Thus TGR have circulating active rat and mouse renin and prorenin. The notion that TGR are a “low renin” model should be revised.

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