Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.23.15 (renin)
35,795 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Presynaptic receptors have recently been identified on nerves supplying vascular smooth muscle. Renin is stored in juxtaglomerular cells in the wall of the afferent glomerular arteriole and the JG cell is probably derived from vascular smooth muscle. Nervous stimuli exert an important influence on release of renin, but the nature of the receptors involved is not agreed. We propose that there are presynaptic receptors associated with the JG apparatus as with vascular muscle and that a mechanism of this sort gives a better account of data on renin release.
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PMID:Hypothesis:presynaptic receptors controlling renin release. 22 46

The present study was carried out to procure detailed information on the relationship between chronic sodium restriction and renin content of kidneys at a subcellular level in the rat. Renin granules (RG) were separated by a discontinuous sucrose-density gradient (from 1.2 to 1.7 M) centrifugation. In control rats, RG were mainly recovered in the fractions corresponding to 1.5 M sucrose, whereas most of the mitochondria, lysosomes, and microsomes equilibrated in upper fractions. The RG fraction contained approximately 60% of total granular renin activity. Low sodium intake for 4 wk resulted in a 12.4-fold increase in plasma renin activity and led to a 2.6-fold increase in renin activity of the RG fraction. But in sodium-restricted rats there was no alteration in the distribution pattern of renin activity on sucrose-density gradients, indicating that there was no change in the density of RG. These results provide evidence for increased renin activity in storage granules following chronic sodium restriction.
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PMID:Effect of sodium restriction on plasma renin activity and renin granules in rat kidney. 22 78

Inactive renin in human plasma is converted to active renin in vitro by acid activation or by cryoactivation. Renin activity was measured at pH 5.5 and renin concentration at pH 7.4. The plasma renin activity before and after cryo-treatment is termed active (APRA) and total (TPRA) plasma renin activity; the plasma renin concentration before and after acid treatment active (APRC) and total (TPRC) plasma renin concentration. In this study we demonstrated that in normal subjects the proportion of active to total renin after cryo-treatment averaged 61%, which was significantly (p less than 0.001) higher than the mean percentage active renin of 34 found with the acid activation procedure. Plasma angiotensin II correlated significantly with APRA, TPRA, TPRC and plasma angiotensin I (PA I), but not with inactive renin, which suggests that inactive renin does not produce angiotensin II in vivo. Cold treatment after acid activation and acid treatment after cryoactivation did not provoke a significant change in the measured renin concentration. Our data support the view that acidification of the plasma activates more than does cryo-treatment, and that inactive renin does not contribute to plasma angiotensin II.
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PMID:Active and inactive renin in normal human plasma. Comparison between acid activation and cryoactivation. 23 Sep 17

1. Renin-associated, chronic psychosocial hypertension of 150-160 mmHg develops in groups of mice interacting socially in complex population cages. 2. The blood pressures of 16 males in a cage were measured and an intraperitoneal injection of the angiotensin coverting enzyme inhibitor captopril (SQ 14,225) was given. Three hours later blood pressures were measured again. 3. During the first 3 weeks of psychosocial hypertension SQ 14,225 was without effect. But at 1 month and subsequently up to 7 months, SQ 14,225 reduced blood pressure to the normal range of 120-130 mmHg. 4. Plasma renin activities were not related to the extent of blood pressure reduction by SQ 14,225. Hence other factors in addition to the renin-angiotensin mechanism play a part in maintaining chronic psychosocial hypertension.
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PMID:Effects of an angiotensin converting enzyme inhibitor on psychosocial hypertension in mice. 23 19

The effect of the primarily beta 2 type adrenergic receptor stimulating terbutaline (10(-7)--10(-5) M) and of the beta 1 and beta 2 type adrenergic receptor stimulating isoproterenol (10(-7)--10(-5) M) was studied on renin release from incubated slices of renal cortex. Renin release and cAMP content of the slices were significantly higher in the presence of both terbutaline and isoproterenol. A logarithmic dose--response relationship was shown to be present between the beta mimetics and the renin concentration in the medium, and the cAMP content of tissue slices. In equal doses isoproterenol was about 1.5 times more potent than terbutaline. No change was seen in the renin content of the tissue slices. The results supports the view that beside the beta 1 type adrenergic receptors of the renal cortex--even if to a lesser extent--the beta 2 type adrenergic receptors, too, are involved in the regulation of renin release.
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PMID:The role of beta receptors in the regulation of renin release. 23 5

Renin in extracts of frozen rabbit kidney exists in two forms: active (molecular weight about 37,000) and inactive (molecular weight about 55,000) renin. The inactive form becomes active after exposure to pH 2.5 at 4 degrees C. If extracts are chromatographed on DEAE cellulose, the inactive renin dissociates into active renin plus a renin inhibitor (molecular weight about 13,000). The inhibitor recombines with active renin if the two are incubated together at 37 degrees C. The inhibitor is destroyed by acid treatment at pH 2.5 at 4 degrees C. We conclude that the activation of inactive renin is due to destruction of the inhibitor by acid. The inactive material may be a renin proenzyme or a storage form of active renin combined with inhibitor.
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PMID:A renin inhibitor from rabbit kidney: conversion of a large inactive renin to a smaller active enzyme. 23 8

Renin activity (EC 3.4.99.19) was measured in submaxillary gland extracts from four sets of recombinant inbred mouse strains. Recombination between Rnr, a gene that mediates the susceptibility of submaxillary gland renin to induction by androgen, and Dip-1, a chromosome 1 marker, was found in only 1 of 51 recombinant inbred strains, indicating that the two genes are closely linked on chromosome 1. Renin activity in androgen-treated female mice of all recombinant inbred strains resembled that of one or the other progenitor strains, as expected if a single gene is responsible. Documentation that a single gene can have major effects on renin in the submaxillary gland of the mouse implies that single gene differences might explain known variations in renin in other species.
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PMID:Location on chromosome 1 of Rnr, a gene that regulates renin in the submaxillary gland of the mouse. 28 12

1. Human renal renin has been purified 200 000-fold from cadaver kidney cortex by a method which employs affinity chromatography on aminohexyl peptstatin. 2. The product of this purification has a specific activity of 400 Goldblatt units/mg when compared with Haas human renin standard. 3. This product appears as a single band on sodium dodecyl sulphate gel and polyacrylamide-disc gel electrophoresis. Renin enzymatic activity was recovered after elution from a polyacrylamide-disc gel run at pH 7.8. 4. Yield with this method was 1%.
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PMID:Purification of human renal renin. 28 38

1. Two high-molecular-weight forms of renin (molecular weights 800 000 and 70 000) are present in mouse plasma. 2. The 800 000 form could be activated and converted into the fully active 40 000 form, by acid or limited proteolysis. The 70 000 form was activated without change in molecular weight. 3. In addition to its enzymic activity, renin was measured by a direct radioimmunoassay, which revealed that the current acid treatment of plasma did not activate all the renin present. 4. Renin is stored as fully active 40 000 renin, with a specific enzymic reactivity of 0.4 times 10(-3) GU ng(-1), in the submaxillary gland of mice. 5. Pure 125I-labelled 40 000 submaxillary renin did not bind to plasma proteins. However, by changing the tertiary structure of renin, it was bound to some of the plasma protease inhibitors; alpha2-macroglobulin, inter-alpha-trypsin inhibitor and alpha2-antithrombin. It was also bound to alpha1- and beta1-lipoprotein, albumin and an unidentified plasma protein. No binding was seen to more than 50 other studied plasma proteins.
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PMID:Is high-molecular-weight-renin binding of renin to the protease inhibitors and lipoproteins? 28 39

1. The intrarenal role of angiotensin II in the recovery of urinary concentration after frusemide was examined in anaesthetized dogs by the intrarenal infusion of angiotensin II antagonists. 2. Renin secretion and renal inner medullary blood flow (tissue clearance of intraparenchymatously injected 133Xenon) were simultaneously measured before and 3 h after frusemide injection. 3. Intrarenal angiotensin II blockade delayed the recovery of urinary osmolality after frusemide. 4. An inverse relationship was found between renin secretion and renal inner medullary blood flow.
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PMID:Intrarenal control of urine concentration by angiotensin II. 28 57


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