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)

Renin is found in mouse plasma as high molecular weight forms, in addition to the fully active 40 000 dalton form. By using freshly 125 I-labelled 40 000 dalton pure submaxillary mouse renin, no binding to plasma proteins was demonstrable. However, unfolding and refolding of the labelled renin by guanidine facilitated binding to specific mouse and human plasma proteins. By using antibodies against individual human plasma proteins, the specific binding proteins were identified to be the plasma protease inhibitors: alpha2-macroglobulin, inter-alpha-trypsin inhibitor, alpha2-antithrombin. Binding was also demonstrated to alpha1- and beta1-lipoproteins, albumin and to a non trypsin binding unidentified plasma protein. No binding to 56 other tested proteins was demonstrable. It is concluded that the native 40 000 renin does not bind, but that a conformational change of the renin molecule most likely is necessary before binding occurs. It is discussed whether or not inactive or high molecular weight forms of renin in plasma are 40 000 renin bound to plasma protease inhibitors and lipoprotein.
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PMID:Renin binding proteins in plasma. Binding of renin to some of the plasma protease inhibitors, to lipoproteins, and to a non-trypsin-binding unidentified plasma protein. 42 6

Tryptophan administration was used to evaluate the possibility that serotonergic neurons are involved in regulating the release of cortisol, renin, and aldosterone. Eleven studies were undertaken using 2 or 10 g tryptophan administered to fasting patients in continued supine posture. Aldosterone rose significantly to 208% (range, 128-329%) of baseline in all seven studies using 10 g and in one of the four studies using 2 g. Renin rose significantly to 189% (range, 116-340%) of baseline in four of the seven studies using 10 g and in two of the four studies using 2 g. Cortisol rose from 10.1 +/- 3.3 to 20.0 +/- 3.7 micrograms/100 ml (P less than 0.001 by t test) in six of the seven studies using 10 g and three of the four studies using 2 g. In eight studies, there was a significant rise of more than one substance after tryptophan administration. In six of these, peak values of the responding hormones occurred at the same time or within a single 30-min sampling interval despite the absence of a constant relationship between their rises. The results suggest participation of the central serotonergic nervous system in the control of renin and aldosterone in addition to its previously postulated role in cortisol release.
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PMID:Stimulation of aldosterone, renin, and cortisol by tryptophan. 42 5

Experiments were designed to clarify the factors affecting renin released during in vitro experiments. Kidneys from rat, dog, and pig were used. Experiments were done in which the gas phase was either bubbled through the incubation medium or layered above it. Renin released into the incubation medium disappeared very rapidly when gas was bubbled through the medium. The decline was similar in mediums bubbled with oxygen-CO2 (95%--5%) or nitrogen-CO2 (95%--5%). The half-life of renin activity in the bubbled medium was approximately 15 min in both cases. However, in experiments in which nonbubbled medium was used throughout, renin released into the incubation medium did not disappear after removal of slices. These data are interpreted to mean that the renin released into the incubation medium is inactivated at the air-water interface.
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PMID:Renin inactivation during in vitro experiments. 44 87

Renin substrate in plasma from normal and biolaterally nephrectomized rats was measured using an excess of rat or rabbit renin which had the same pressor activity when directly assayed in the rat. The amounts of angiotensin I generated with an excess of rat renin were similar to those generated with an excess of rabbit renin in plasma from normal and bilaterally nephrectomized rats. Further addition of an excess of homologous renin to the incubation mixture did not generate more angiotensin I from normal and bilaterally nephrectomized rat plasma which had been incubated before with an excess of rabbit renin. The isoelectric focusing profiles of plasma renin substrate from normal and bilaterally nephrectomized rats were almost identical using an excess of either rat or rabbit renin. It is concluded that there is no species-specific renin substrate for homologous renin in normal or bilaterally nephrectomized rats.
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PMID:No evidence for the existence of a species-specific renin substrate in plasma from normal and bilaterally nephrectomized rats. 46 38

Differences in the rate of renin release by superficial and deep areas of the cat kidney cortex were studied in vitro and in vivo. Renin release in vitro by outer cortical slices was significantly higher than by their inner counterparts: 19.6 +/- 2.3 vs. 12.8 +/- 1.95 ng angiotensin I-h-1-mg fresh tissue-1-h of incubation-1. In vivo blood was sampled from subcapsular (outer cortical) and deep (inner cortical and medullary) renal venous circulation from anesthetized cats. Renal venous minus arterial plasma renin concentration was respectively, 4.3 +/- 1.12 and 1.9 +/- 1.04 ng angiotensin I-ml-1-h-1 (P less than 0.01). By assuming that in these experiments renal blood flow distribution was approximately equal to each of the two areas of venous drainage, as reported in the isolated perfused cat kidney, we infer from the regional differences in arteriovenous concentration that the rate of renin release of the outer cortex is higher than that of the innder cortex in the cat kidney in vivo. Tissue content of renin was found to decrease toward the deep cortex. The results support the concept that the rate of regional renin release correlates with tissue renin content, at least under the conditions of the present experiments.
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PMID:Regional renin release by the cat kidney in vitro and in vivo. 47 59

1. Renin activity in rabbit plasma increases after acidification (pH 3.3), probably due to activation of an inactive form of renin. 2. Both active and inactive renin in plasma increase after haemorrhage. This stimulus does not change the relative proportions of the two forms. 3. After ligation of the renal blood vessels neither form of renin increases in response to haemorrhage. 4. One day after bilateral nephrectomy no inactive renin could be demonstrated in plasma. 5. In the rabbit, therefore, the kidney is a major source of the inactive renin in plasma.
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PMID:Inactive renin in rabbit plasma: effect of haemorrhage. 47 91

Renin activity and aldosterone concentration in plasma and excretion of sodium and potassium in urine were measured during a period of 24 hours in 12 patients undergoing hysterectomy under general anaesthesia or epidural analgesia. Analgesia extended from T4 to S5 and was effective throughout the study. The normal stress-induced increase in plasma renin activity and aldosterone was inhibited by epidural analgesia. Urinary excretion of potassium was significantly lower in the epidural group, but sodium and water retention showed no difference between groups. It is concluded that neurogenic stimuli from the surgical area are important release mechanisms of the renin-aldosterone response to surgery. The results suggest that post-operative sodium retention is caused by factors other than the mineralocorticoid system.
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PMID:Epidural analgesia inhibits the renin and aldosterone response to surgery. 48 83

1. These studies were conducted on isolated, perfused rat kidneys to determine the mechanism through which high concentrations of extracellular Mg (20mM) stimulated renin release. 2. Raising K concentrations in the perfusion fluid from 5 to 50 mM, and raising renal perfusion pressure from 100 to 150 mmHg inhibited the renin release induced by 20 mM-Mg. The response was reversible. 3. Renin release induced by low renal perfusion pressure (50 mmHg) or isoprenaline (2.43 microM) was unaffected by 20 mM-Mg. However, this release was augmented when 5 mM-Ca was added in conjunction with 20 mM-Mg. 4. In medium containing 20 mM-Mg, lowering Na concentration from 145 to 100 mM augmented the renin release induced by low perfusion pressure and isoprenaline. Further lowering Na to 25 mM had no additional effect. 5. It is concluded that 20 mM-Mg activates renin release by a mechanism which involves hyperpolarization of the juxtaglomerular cell membrane and an associated decrease in cytoplasmic Ca. Such a mechanism might be coupled to a Mg-Na exchange pump.
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PMID:Influence of potassium, sodium, calcium, perfusion pressure, and isoprenaline on renin release induced by high concentrations of magnesium. 49 Mar 66

Studies of 16 adults with nephrotic edema reveal a spectrum of disease, the extremes of which suggest two different pathophysiologic forms. Patients with the "classic" form--vasoconstriction or hypovolemic nephrosis--have high renin and aldosterone levels that are stimulated rather than suppressed by salt-loading but become lower before steroid diuresis. These patients have minimal lesion disease and, perhaps from diffuse capillary damage, tend to have hypovolemia with renin-induced vasoconstriction. Patients with the second, and heretofore undescribed, form--hypervolemic or overfilling nephrosis--have low renin and aldosterone values that rise normally after sodium depletion. Hypertension, mild renal insufficiency, hypervolemia, and steroid resistance with chronic glomerulonephritis are seen histologically. This form appears volume overloaded from impaired renal sodium excretion. In remission of either type, renin system deviations tend towards normal, but one form does not convert to the other. Renin-sodium profiling may help reveal the two forms and predict steroid responsiveness.
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PMID:Nephrotic syndrome: vasoconstriction and hypervolemic types indicated by renin-sodium profiling. 49 1

A normal size form of renin, which seems to be a storage form in renin granules, changed neither in molecular weight nor activity by acidification to pH 3.0. High molecular weight (HMW) renin fractionated by gel chromatography from crude renal extract prepared with thiol group blockers was converted into normal size renin by acdification, accompanied with an increase in renin activity by about 50%. The molecular weight conversion by acidification appeared due to destruction or loss of binding ability of the renin binding substance which was present in the cytosol of renal cortical tissue. Renin and renin binding substance could combine into HMW renin at neutral pH in the presence of thiol group blockers and renin activity decreased.
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PMID:Relationship between molecular weight conversion and renin activity in dog renal renin. 50 2


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