Journal articles: 'Renin'

1

Kruszelnicki, Karl. "Renin or rennin?" Latest Word: The Bimonthly Newsletter for Medical Transcriptionists, The 14, no. 2 (April 2006): 11. http://dx.doi.org/10.1016/j.latestword.2006.03.006.

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2

Hosoi, Masayuki, Shokei Kim, and Kenjiro Yamamoto. "Evidence for heterogeneity of glycosylation of human renin obtained by using lectins." Clinical Science 81, no. 3 (September 1, 1991): 393–99. http://dx.doi.org/10.1042/cs0810393.

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1. In this study, the carbohydrate structure of pure human renin was examined by using various lectins. 2. Pure renin could be separated into three forms by concanavalin A chromatography, a concanavalin A-unbound form, a loosely bound form and a tightly bound form, termed renins A, B and C, respectively. Renins A, B and C accounted for 3, 13 and 84%, respectively, of the purified renin. These forms were all present in individual human plasma and the relative proportions in plasma were 27 ± 3, 33 ± 4 and 39 ± 5% (means ± sem) for renins A, B and C, respectively (n = 5). 3. Each form, electroblotted on to the nitrocellulose sheet after gel electrophoresis, was incubated with five peroxidase-labelled lectins, lentil lectin, erythroagglutinating phytohaemagglutinin, wheat-germ agglutinin, Ricinus communis agglutinin and peanut agglutinin. The protein was stained with 4-chloro-l-naphthol. 4. The staining pattern obtained with these lectins was significantly different among the three forms of human renin, confirming that they have different carbohydrate structures. Furthermore, the positive staining of human renin with erythroagglutinating phytohaemagglutinin, wheat-germ agglutinin and Ricinus communis agglutinin was in contrast with the lack of binding of rat renin to these lectins. 5. These results indicate the renal secretion of differently glycosylated multiple forms of human renin. The carbohydrate structure of human renin appears to differ from that of rat renin.

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Glorioso, N., C. Troffa, J. H. Laragh, S. A. Atlas, D. Marion, and J. E. Sealey. "The cat: an animal model for studies of inactive renin." American Journal of Physiology-Endocrinology and Metabolism 252, no. 4 (April 1, 1987): E509—E518. http://dx.doi.org/10.1152/ajpendo.1987.252.4.e509.

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Inactive renin, prorenin, is found in high concentrations in human plasma. We report herein the characteristics of trypsin-activated inactive renin from cat kidney and plasma. Cat and human plasma inactive renin were activated by similar concentrations of trypsin. As in humans, there was more inactive than active renin in cat plasma; also, inactive renin was low but detectable after nephrectomy. Trypsin-activated renal inactive renin, purified on Cibacron blue agarose and pepstatin-amino-hexyl-Sepharose chromatography, was inhibited by pepstatin and by a renin inhibitor similarly to cat and human active renins. The pH optimum of cat renin was biphasic: the higher peak of active renin was at pH 5.7, whereas that of activated inactive renin was at pH 7.5. As in humans, active and inactive plasma renin increased during sodium depletion and inactive renin increased during beta-adrenergic blockade, while active renin decreased. These results demonstrate that cat inactive renin is similar to human prorenin. Therefore, the cat may be a useful model for the study of prorenin.

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Kim, S., M. Hiruma, F. Ikemoto, and K. Yamamoto. "Importance of glycosylation for hepatic clearance of renal renin." American Journal of Physiology-Endocrinology and Metabolism 255, no. 5 (November 1, 1988): E642—E651. http://dx.doi.org/10.1152/ajpendo.1988.255.5.e642.

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Three differently glycosylated forms of renin (renin A, B-1, and B-2) were highly purified from rat kidneys by pepstatin-aminohexyl-Sepharose affinity chromatography and by serial lectin affinity chromatography on concanavalin A (con A) and lentil lectin-Sepharose, and the role of glycosylation of renin was investigated. Renin A and renin B-1 were loosely and tightly bound to con A, respectively, but did not bind to lentil lectin. Renin B-2 bound to both con A and lentil lectin. These three forms of renin were all similar in their physicochemical characteristics, including molecular weight, isoelectric point, specific activity, Km, optimum pH, and antigenicity. Each form of renin, labeled with 125I and given intravenously to anesthetized rats, disappeared from the circulation at different rates (metabolic clearance rates of 5.05 +/- 1.02, 17.1 +/- 2.5, and 36.0 +/- 4.1 ml.min-1.kg-1 for renins A, B-1, and B-2, respectively). Labeled renin A distributed to a similar extent in the liver and kidney (21.2 +/- 0.2 and 15.2 +/- 0.8% of the injected dose, respectively), whereas renins B-1 and B-2 were distributed predominantly in the liver (56.3 +/- 1.2 and 72.3 +/- 3.7% of the injected dose, respectively) and to a lesser extent in the kidney (4.3 +/- 0.3 and 2.1 +/- 0.2%, respectively). Deglycosylation of renin B-1 with endoglycosidase F resulted in no loss of its enzymatic activity or antigenicity but greatly reduced the metabolic clearance rate to 18% (from 17.1 +/- 2.5 to 3.09 +/- 0.17 ml.min-1.kg-1). Deglycosylation of renin B-1 greatly decreased its uptake by the liver (from 56.3 +/- 1.2 to 3.3 +/- 0.2%) and increased its uptake by the kidney (from 4.3 +/- 0.3 to 23.9 +/- 0.9%). These studies indicate the importance of glycosylation of renin for its hepatic uptake and metabolic clearance rate.

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Liang, Ping, Craig A. Jones, Brent W. Bisgrove, Lei Song, Sean T. Glenn, H. Joseph Yost, and Kenneth W. Gross. "Genomic characterization and expression analysis of the first nonmammalian renin genes from zebrafish and pufferfish." Physiological Genomics 16, no. 3 (February 13, 2004): 314–22. http://dx.doi.org/10.1152/physiolgenomics.00012.2003.

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Liang, Ping, Craig A. Jones, Brent W. Bisgrove, Lei Song, Sean T. Glenn, H. Joseph Yost, and Kenneth W. Gross. Genomic characterization and expression analysis of the first nonmammalian renin genes from zebrafish and pufferfish. Physiol Genomics 16: 314–322, 2004. First published November 25, 2003; 10.1152/physiol-genomics. 00012.2003.—Renin is a key enzyme in the renin-angiotensin system (RAS), a pathway which plays an important physiological role in blood pressure and electrolyte homeostasis. The origin of the RAS is believed to have accompanied early evolution of vertebrates. However, renin genes have so far only been unequivocally identified in mammals. Whether or not a bona fide renin gene exists in nonmammalian vertebrates has been an intriguing question of physiological and evolutionary interest. Using a genomic analytical approach, we identified renin genes in two nonmammalian vertebrates, zebrafish ( Danio rerio) and pufferfish ( Takifugu rubripes). Phylogenetic analysis demonstrates that the predicted fish renins cluster together with mammalian renins to form a distinct subclass of vertebrate aspartyl proteases. RT-PCR results confirm generation of the predicted zebrafish mRNA and its expression in association with the opisthonephric kidney of adult zebrafish. Comparative in situ hybridization analysis of wild-type and developmental mutants indicates that renin expression is first detected bilaterally in cells of the interrenal primordia at 24 h postfertilization, which subsequently migrate to lie adjacent to, but distinct from, the glomerulus of the developing pronephric kidney. Our report provides the first molecular evidence for the existence of renin genes in lower vertebrates. The observation that the earliest renin-expressing cells, arising during ontogeny of this teleost vertebrate, are of adrenocortical lineage raises an interesting hypothesis as regards the origin of renin-expressing cells in the metanephric kidney of higher vertebrates.

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Evans, DB, JC Cornette, TK Sawyer, DJ Staples, AE de Vaux, and SK Sharma. "Substrate specificity and inhibitor structure‐activity relationships of recombinant human renin: implications in the in vivo evaluation of renin inhibitors." Biotechnology and Applied Biochemistry 12, no. 2 (April 1990): 161–75. http://dx.doi.org/10.1111/j.1470-8744.1990.tb00089.x.

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Homogeneous, active recombinant human renin obtained from Chinese hamster ovary (CHO) cells was characterized in vitro by (i) determination of its relative rates of hydrolysis of plasma angiotensinogens (ANGs) from human, monkey, baboon, rat, pig, rabbit, hamster, and dog and (ii) analysis of several synthetic ANG‐based, inhibitors ranging in IC50 from 10(‐10) to 10(‐6) M. Comparison of the recombinant human renin with human kidney renin showed that these enzymes were indistinguishable from each other in terms of their plasma ANG specificities and inhibition by synthetic renin inhibitors. Porcine kidney renin was also characterized and shown to display plasma ANG hydrolysis profiles and inhibitor potencies that were markedly different from those of human renins. Finally, the results using the above plasma ANGs extend previous studies showing that the substrate specificity of human renin may be influenced by the amino acid residues at P2 (i.e., Ile, Val, or Tyr) and P3 (i.e., His or Tyr) sites. The relevance of these data to in vivo evaluation of renin inhibitors in animal models is discussed.

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7

Duan, J., J. Jaramillo, G. L. Jung, A. L. McLeod, B. H. Fernandas, and D. Mathis. "Comparative studies on differential inhibition of the rennin–angiotensin system in the anesthetized guinea pig." Canadian Journal of Physiology and Pharmacology 73, no. 10 (October 1, 1995): 1512–18. http://dx.doi.org/10.1139/y95-209.

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The present study compares the hemodynamic effects and mechanisms of action of angiotensin II (AngII) antagonists, angiotensin converting enzyme (ACE) inhibitors, and renin inhibitors in the guinea pig, an animal with high similarity to primates in terms of in vitro and in vivo responses to several human renin inhibitors. Animals were anesthetized with urethane and ketamine. The carotid artery was catheterized for monitoring blood pressure and heart rate. After 30 min stabilization, drug (or vehicle) effects were monitored for 1 h following each increasing dose (i.v. bolus injection). Drugs tested include losartan, an AngII receptor antagonist; two renin inhibitors, BILA 2157 BS and PD-134672; and captopril, an ACE inhibitor. All drugs dose dependency decreased blood pressure. Diastolic blood pressure was reduced more than systolic blood pressure, suggestive of vasodilation. The maximum decrease (32 ± 6%, p < 0.05 vs. vehicle) in mean arterial blood pressure (MABP) by losartan was achieved with a dose of 1 mg/kg. A similar decrease in MABP was observed with renin inhibitors at a dose of 3 mg/kg, without affecting heart rate. A further increase in the dose of renin inhibitors (6 mg/kg) decreased not only blood pressure but also heart rate. Captopril decreased MABP with a maximum of 48 ± 3% (p < 0.05 vs. vehicle, losartan, and PD-134672). In the presence of HOE-140, a bradykinin antagonist, the MABP decrease by captopril was only 35 ± 4%, (p < 0.05 vs. captopril alone). Bilateral nephrectomy reduced the peak MABP effect of PD-134672 by 67%, while the effects of captopril on MABP were affected to a lesser degree (57%). Therefore, captopril remains more effective in reducing MABP (p < 0.05 vs. that of PD-134672). These results suggest that renin inhibitors and AngII antagonists act more specifically on the rennin–angiotensin system cascade, while captopril acts partially by a bradykinin-dependent mechanism. The small animal model described provides a novel tool for the comparative pharmacologic assessment of different rennin–angiotensin system inhibitors.Key words: blood pressure, guinea pig, rennin–angiotensin system, rennin–angiotensin system inhibition.

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8

Widimský, Jiří. "The new renin inhibitor aliskiren. The new drug blocking renin-angiotensin system. Will it meet the expectations?" Cor et Vasa 49, no. 11 (November 1, 2007): 408–14. http://dx.doi.org/10.33678/cor.2007.143.

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9

Ioannou, P., A. Y. Loh, and D. H. Osmond. "Activation and measurement of plasma prorenin in the rat." Canadian Journal of Physiology and Pharmacology 69, no. 9 (September 1, 1991): 1331–40. http://dx.doi.org/10.1139/y91-197.

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Prorenin determination in rat plasma has been problematic from the outset. Consequently, its existence is questioned by some and its quantity by others, making it difficult for knowledge to advance as to its function relative to the renin system. The present study examines major variables in the determination of rat plasma prorenin and renin, notably different prorenin activation protocols involving blood samples obtained under various conditions from animals under different anesthetics. We found that a trypsin activation step with 5 mg/mL plasma, 60 min at 23 °C, followed by a PRA step of 10 min at 37 °C, resulted in the highest prorenin estimates, up to approximately 400 ng∙mL−1∙h−1 in terms of angiotensin I, as compared with published values of 0–190, based on other protocols. These estimates were obtained despite considerable destruction of angiotensinogen (renin substrate) by trypsin. Cryoactivation of prorenin was much less effective than in human plasma but, when followed by trypsin, it facilitated greater activation than with trypsin alone. Comparable fresh and fresh-frozen plasmas had similar prorenin–renin values, but lower values were observed in plasmas that had been repeatedly frozen and thawed. Conscious rats and those anesthetized with Inactin or ether had higher renins and prorenins than those anesthetized with methoxyflurane or halothane. Rats with kidneys in place during blood collection had higher renins (but not prorenins) than those whose kidneys were clamped off, suggesting that last-minute renin release during blood collection had occurred. We conclude that (i) trypsin generates increased renin, or renin-like, activity in plasma, suggesting activation of a precursor; (ii) on this basis, high prorenin levels exist in normal rat plasma; (iii) renin and prorenin levels are variously influenced by different anesthetics and blood handling procedures; (iv) variation in prorenin levels suggests that it is a dynamic (functional?) component of the renin system; (v) prorenin measurements are heavily influenced by methodological variations during the trypsin step or the subsequent PRA step; (vi) using standardized methodology, the rat can serve as a model for investigating the function of prorenin in normotension and hypertension.Key words: tryptic activation, angiotensinogen, adrenalectomy, anesthesia.

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10

Sessler, F. M., J. A. Jacquez, and R. L. Malvin. "Different production and decay rates of six renin forms isolated from rat plasma." American Journal of Physiology-Endocrinology and Metabolism 250, no. 5 (May 1, 1986): E551—E557. http://dx.doi.org/10.1152/ajpendo.1986.250.5.e551.

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Rat kidney contains six forms of renin, which are in different proportion from those found in plasma. We tested the hypothesis that differential removal and production of the forms might explain the differences between stored and circulating renins. In one group of rats, the six forms of renin were measured in plasma, 10 min after hemorrhage, or after aortic constriction. Plasma was run on an isoelectric focusing gel, and the six peaks of renin activity were expressed either as angiotensin I per hour per milliliter or as a percentage of the total plasma renin concentration. After hemorrhage or aortic constriction, the concentration of each form was significantly increased; the profile of circulating renin was significantly modified, showing an increase in proportion of form 2 and a decrease of forms 4, 5, and 6. In a second group, the disappearance of each form was measured 0 to 100 min after nephrectomy and fitted a two-exponential decay curve. Interpreted as a two-pool system with degradation from pool 1, the degradation rate decreased progressively, going from form 1 to 6. In a third group, arterial and renal venous blood were collected. The profile of secreted renin was calculated from the arterial venous difference. This profile fitted the prediction of the two-compartment model. Our data support the hypothesis that the proportion of each circulating renin form is the result of a balance between the rate of production of renin of constant composition and the degradation of the six forms at different rates.

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11

Ionova, T. A., G. S. Kolesnikova, and N. Iu Kalinchenko. "Comparative analysis of direct renin levels and plasma renin activity for the purpose of monitoring the patients with congenital adrenal cortical hyperplasia." Problems of Endocrinology 59, no. 5 (October 15, 2013): 9–15. http://dx.doi.org/10.14341/probl20135959-15.

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The high prevalence of diseases associated with the disturbances in the renin-angiotensin-aldosterone system (RAAS) including those affecting the children dictates the necessity of the development and application of highly specific, accurate, and sensitive indices. One of them widely used at present is plasma renin activity (PRA). Meanwhile, foreign researchers have demonstrated significant correlation between PRA and direct renin concentration that can be determined by a technically simpler and readily available method. We are unaware of the studies with the application of this approach reported in the Russian-language publications. The present work was designed to consider the possibility of using direct rennin levels and PRA for monitoring health conditions of the children presenting with congenital adrenal cortical hyperplasia. PRA and direct rennin concentrations were determined with the use of the relevant assay kits in 72 patients admitted to the Pediatric Department of Endocrinological Research Centre. Group 1 was comprised of 44 patients presenting with congenital adrenal cortical hyperplasia (CAH), group 2 consisted of 28 patients with the presumably unaffected adrenal function. Direct rennin concentrations and PRA are known to have virtually identical diagnostic value, i.e. they can equally well be used to diagnose disorders of RAAS functions including those in the patients with CAH. However, the measurement of direct rennin permits to more precisely detect hyperaldosteronism and identify children exhibiting symptoms of mineralocorticoid overdose. The patients with the supposedly normal functioning adrenal glands were also found to show high percentage of abnormal PRA values and direct rennin levels which suggests the relationship between the functions of RAAS and other endocrine organs.

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12

Skøtt, Ole. "Renin." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 282, no. 4 (April 1, 2002): R937—R939. http://dx.doi.org/10.1152/ajpregu.00625.2001.

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13

Campbell, Duncan J. "3 RENIN VS DIRECT RENIN MEASUREMENT." Journal of Hypertension 30 (September 2012): e1-e2. http://dx.doi.org/10.1097/01.hjh.0000419828.82647.7d.

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Brakch, Noureddine, Flore Allemandou, Irene Keller, and Juerg Nussberger. "The Renin Prosequence Enhances Constitutive Secretion of Renin and Optimizes Renin Activity." Current Neurovascular Research 8, no. 2 (May 1, 2011): 121–30. http://dx.doi.org/10.2174/156720211795495367.

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15

Nguyen, Genevieve. "Renin, (pro)renin and receptor: an update." Clinical Science 120, no. 5 (November 19, 2010): 169–78. http://dx.doi.org/10.1042/cs20100432.

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PRR [(pro)renin receptor] was named after its biological characteristics, namely the binding of renin and of its inactive precursor prorenin, that triggers intracellular signalling involving ERK (extracellular-signal-regulated kinase) 1/2. However the gene encoding for PRR is named ATP6ap2 (ATPase 6 accessory protein 2) because PRR was initially found as a truncated form co-purifying with V-ATPase (vacuolar H+-ATPase). There are now data showing that this interaction is not only physical, but also functional in the kidney and the heart. However, the newest and most fascinating development of PRR is its involvement in both the canonical Wnt/β-catenin and non-canonical Wnt/PCP (planar cell polarity) pathways, which are essential for adult and embryonic stem cell biology, embryonic development and disease, including cancer. In the Wnt/β-catenin pathway, it has been shown that PRR acts as an adaptor between the Wnt receptor LRP5/6 (low-density lipoprotein receptor-related protein 5/6) and Fz (frizzled) and that the proton gradient generated by the V-ATPase in endosomes is necessary for LRP5/6 phosphorylation and β-catenin activation. In the Wnt/PCP pathway, PRR binds to Fz and controls its asymetrical subcellular distribution and therefore the polarization of the cells in a plane of a tissue. These essential cellular functions of PRR are independent of renin and open new avenues on the pathophysiological role of PRR. The present review will summarize our knowledge of (pro)renin-dependent functions of PRR and will discuss the newly recognized functions of PRR related to the V-ATPase and to Wnt signalling.

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16

Opsahl, John A., Kevin L. Smith, Robert D. Murray, Paul A. Abraham, and Stephen A. Katz. "Renin and Renin Inhibition in Anephric Man." Clinical and Experimental Hypertension 15, no. 2 (January 1993): 289–306. http://dx.doi.org/10.3109/10641969309032935.

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17

Akiyoshi, Fukamizu, Nishi Kazuto, Nishimatsu Shin-ichiro, Miyazaki Hitoshi, Hirose Shigehisa, and Murakami Kazuo. "Human renin gene of renin-secreting tumor." Gene 49, no. 1 (January 1986): 139–45. http://dx.doi.org/10.1016/0378-1119(86)90393-8.

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18

Jindra Jr., A., J. Bultas, J. Ort, and R. Kvetnansky. "Investigation of human and rat inactive renin in plasma and kidney." Canadian Journal of Physiology and Pharmacology 69, no. 9 (September 1, 1991): 1341–49. http://dx.doi.org/10.1139/y91-198.

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Under an initial interval of immobilization stress in rats, reciprocal changes of plasma active and inactive renin were observed, suggesting activation of circulating inactive renin. Molecular weight (MW) studies revealed that this activation might proceed via a MW shift from inactive renin with MW of 50 000 to active renin of MW 43 000. In a later interval of stress, under stimulated renin secretion, a lower MW form (38 000) of active renin was released into the circulation. This MW is close to that of active renin (39 000) found in rat kidney renin granules. In renin granules, equilibrated in fractions of 1.6 and 1.7 mol/L sucrose in discontinuous density gradient, trypsin-activatable renin activity formed 36 and 16% of total activity, respectively. In humans, under acute bicycle exercise, a lower MW form (39 000) of active renin was released into the circulation, while the content of inactive renin with MW in the range of 51 000–58 000 and at 47 000 did not substantially change. There was a slight decrease in circulating inactive renin passing through the kidney. The data suggest that, at least in rats, in vivo pathways for activation of inactive renin might exist, other than that proceeding before secretion from renin granules. Under the conditions of increased renin secretion, a lower MW form of active renin is mainly released into the circulation in both rats and humans.Key words: active renin, inactive renin, renal veins, renin granules, stress.

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Mazanti, Ingrid, Kirstine Lintrup Hermann, Arne Høj Nielsen, and Knud Poulsen. "Ultrafiltration of renin in the mouse kidney studied by inhibition of tubular protein reabsorption with lysine." Clinical Science 75, no. 3 (September 1, 1988): 331–36. http://dx.doi.org/10.1042/cs0750331.

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1. In order to study the role of the kidney in the elimination of endogenous plasma renin, renin was measured in the plasma and urine of female mice. 2. The renin concentration was two orders of magnitude lower in urine than in plasma, but it increased after intraperitoneal injection of submandibular mouse renin. No correlation between the plasma renin concentration and the urinary renin concentration and renin excretion rate could be demonstrated. 3. Blockade of the tubular reabsorption of proteins by intraperitoneal injection of the basic amino acid lysine increased the urinary renin concentration, renin excretion rate and renin clearance two to three orders of magnitude, without affecting the plasma renin concentration. 4. This finding demonstrates that ultrafiltered renin is reabsorbed almost completely in the renal tubules and that the mechanism most likely is the same as for other filtered proteins. 5. The large renal renin clearance obtained after intraperitoneal lysine is in accordance with a major role of the kidneys in the elimination of renin from the circulation, by a glomerular ultrafiltration and tubular reabsorption and metabolization of renin.

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Wanka, Heike, Philipp Lutze, Alexander Albers, Janine Golchert, Doreen Staar, and Jörg Peters. "Overexpression of Transcripts Coding for Renin-b but Not for Renin-a Reduce Oxidative Stress and Increase Cardiomyoblast Survival under Starvation Conditions." Cells 10, no. 5 (May 14, 2021): 1204. http://dx.doi.org/10.3390/cells10051204.

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A stimulated renin-angiotensin system is known to promote oxidative stress, apoptosis, necrosis and fibrosis. Renin transcripts (renin-b; renin-c) encoding a cytosolic renin isoform have been discovered that may in contrast to the commonly known secretory renin (renin-a) exert protective effects Here, we analyzed the effect of renin-a and renin-b overexpression in H9c2 cardiomyoblasts on apoptosis and necrosis as well as on potential mechanisms involved in cell death processes. To mimic ischemic conditions, cells were exposed to glucose starvation, anoxia or combined oxygen–glucose deprivation (OGD) for 24 h. Under OGD, control cells exhibited markedly increased necrotic and apoptotic cell death accompanied by enhanced ROS accumulation, loss of mitochondrial membrane potential and decreased ATP levels. The effects of OGD on necrosis were exaggerated in renin-a cells, but markedly diminished in renin-b cells. However, with respect to apoptosis, the effects of OGD were almost completely abolished in renin-b cells but interestingly also moderately diminished in renin-a cells. Under glucose depletion we found opposing responses between renin-a and renin-b cells; while the rate of necrosis and apoptosis was aggravated in renin-a cells, it was attenuated in renin-b cells. Based on our results, strategies targeting the regulation of cytosolic renin-b as well as the identification of pathways involved in the protective effects of renin-b may be helpful to improve the treatment of ischemia-relevant diseases.

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Berka, J. L., D. Alcorn, G. B. Ryan, S. L. Skinner, and D. A. Weaver. "Renin processing in cultured juxtaglomerular cells of the hydronephrotic mouse kidney." Journal of Histochemistry & Cytochemistry 41, no. 3 (March 1993): 365–73. http://dx.doi.org/10.1177/41.3.8429199.

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We examined renin processing in cultured juxtaglomerular (JG) cells of the hydronephrotic mouse kidney with immunocytochemical and biochemical techniques. Compared with JG cells in normal kidneys, there was less intense labeling for renin protein in mature granules of cultured JG cells. However, pro-renin labeling of transport vesicles and juvenile granules was maintained, suggesting incomplete passage of pro-renin through intermediate and mature granules. Immunogold evidence of exocytosis of mature granules containing renin protein was present at all stages. Labeling of transport vesicles for pro-renin, together with the absence of exocytosis of pro-renin from juvenile granules, indicated that pro-renin was exclusively released by a constitutive process. Active renin release into supernatants decreased with time, whereas the ratio of total renin to active renin increased, indicating that pro-renin synthesis and release were maintained but that the processing of pro-renin to active renin was interrupted. Angiotensin II inhibited and verapamil stimulated active renin release in culture; neither substance affected pro-renin release. Application of secretagogues that act via intracellular calcium or cAMP resulted in depletion of mature granules and their deformation by myelin figures and vacuoles, findings consistent with an exocytosis from mature granules. The absence of effect of any secretagogues on pro-renin release suggests that these stimulatory mechanisms are exclusively post-Golgi. In cultured JG cells in renal explants, renin vesicular transport and granular exocytosis are maintained but a defect in pro-renin passage from juvenile to intermediate granules is apparent.

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Brown, Mark A., Vivienne C. Zammit, and Delma Adsett. "Stimulation of Active Renin Release in Normal and Hypertensive Pregnancy." Clinical Science 79, no. 5 (November 1, 1990): 505–11. http://dx.doi.org/10.1042/cs0790505.

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1. Active plasma renin concentration but not total renin concentration is reduced in women with pregnancy-induced hypertension compared with normotensive pregnant women. This study was conducted to determine whether women with pregnancy-induced hypertension are able to stimulate release of active renin. 2. Active plasma renin concentration was measured as the generation of angiotensin I at physiological pH in the presence of excess renin substrate, and total renin concentration was determined in the same way after trypsin activation. Inactive plasma renin concentration was calculated as the difference between total renin and active plasma renin concentrations. 3. Resting active plasma renin concentration was significantly greater in third-trimester primigravidae compared with normotensive non-pregnant women and active plasma renin and total renin concentrations rose significantly without a fall in inactive plasma renin concentration in both groups after 2 h ambulation, suggesting increased release of active plasma renin and not conversion of circulating inactive to active renin. These responses were blunted in women taking oral contraceptives. 4. Although the active plasma renin concentration was significantly reduced in third-trimester primigravidae with pregnancy-induced hypertension, total renin concentration was not significantly different compared with normotensive women of similar gestation and in both groups 30 min 60° head-up tilt increased active but not inactive plasma renin concentration. 5. These studies show that in normal pregnancy active plasma renin concentration can be stimulated to a similar extent as in non-pregnant women, despite a higher resting level. This appears to be due to increased secretion of active plasma renin rather than conversion of circulating inactive to active renin. Women with pregnancy-induced hypertension are also still able to stimulate secretion of active renin despite resting concentrations similar to those of non-pregnant women. These data suggest that in pregnancy-induced hypertension basal secretion of active renin is prematurely reset to that in the non-pregnant state but that secretion of active renin responds normally to posture.

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23

Tree, M., M. Szelke, B. Leckie, B. Atrash, B. Donovan, A. Hallett, D. M. Jones, et al. "Renin Inhibitors." Journal of Cardiovascular Pharmacology 7 (1985): S49—S52. http://dx.doi.org/10.1097/00005344-198507004-00010.

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24

Haber, Edgar, Kwan Y. Hui, William D. Carlson, and Michael S. Bernatowicz. "Renin Inhibitors." Journal of Cardiovascular Pharmacology 10 (1987): 54–58. http://dx.doi.org/10.1097/00005344-198706107-00009.

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25

Schweda, Frank, Ulla Friis, Charlotte Wagner, Ole Skott, and Armin Kurtz. "Renin Release." Physiology 22, no. 5 (October 2007): 310–19. http://dx.doi.org/10.1152/physiol.00024.2007.

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The aspartyl-protease renin is the key regulator of the renin-angiotensin-aldosterone system, which is critically involved in salt, volume, and blood pressure homeostasis of the body. Renin is mainly produced and released into circulation by the so-called juxtaglomerular epithelioid cells, located in the walls of renal afferent arterioles at the entrance of the glomerular capillary network. It has been known for a long time that renin synthesis and secretion are stimulated by the sympathetic nerves and the prostaglandins and are inhibited in negative feedback loops by angiotensin II, high blood pressure, salt, and volume overload. In contrast, the events controlling the function of renin-secreting cells at the organ and cellular level are markedly less clear and remain mysterious in certain aspects. The unravelling of these mysteries has led to new and interesting insights into the process of renin release.

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26

Fisher, Naomi DL, and Emma A. Meagher. "Renin Inhibitors." Journal of Clinical Hypertension 13, no. 9 (July 27, 2011): 662–66. http://dx.doi.org/10.1111/j.1751-7176.2011.00514.x.

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Haber, E. "Renin inhibitors." Hypertension 8, no. 12 (December 1986): 1093–95. http://dx.doi.org/10.1161/01.hyp.8.12.1093.

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Kelly, Darren J., Jennifer L. Wilkinson-Berka, and Richard E. Gilbert. "Renin Inhibition." Hypertension 46, no. 3 (September 2005): 471–72. http://dx.doi.org/10.1161/01.hyp.0000179574.10913.08.

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29

Azizi, Michel. "Renin inhibition." Current Opinion in Nephrology and Hypertension 15, no. 5 (September 2006): 505–10. http://dx.doi.org/10.1097/01.mnh.0000242176.36953.f7.

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30

Greenlee, William J. "Renin inhibitors." Medicinal Research Reviews 10, no. 2 (April 1990): 173–236. http://dx.doi.org/10.1002/med.2610100203.

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31

Kleinert, Hollis D. "Renin inhibition." Cardiovascular Drugs and Therapy 9, no. 5 (October 1995): 645–55. http://dx.doi.org/10.1007/bf00878547.

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32

Nathan, Naveen. "Rediscovering Renin." Anesthesia & Analgesia 138, no. 5 (April 15, 2024): 928. http://dx.doi.org/10.1213/ane.0000000000006965.

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Takahashi, Hideki, kachio Kozakai, Sinji Yamaguchi, Masaaki Takano, Toshio Nakagome, Yoshikazu Miura, and Yuzo Maruyama. "372. Plasma renin concentration by Renin IRMA Pasuteur." Japanese Journal of Radiological Technology 46, no. 8 (1990): 1343. http://dx.doi.org/10.6009/jjrt.kj00003322494.

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CORVOL, P., and J. MENARD. "RENIN INHIBITION: IMMUNOLOGICAL PROCEDURES AND RENIN INHIBITOR PEPTIDES." Fundamental & Clinical Pharmacology 3, no. 4 (July 8, 1989): 347–62. http://dx.doi.org/10.1111/j.1472-8206.1989.tb00676.x.

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Camenzind, Edoardo, Jürg Nussberger, Lucienne Juillerat, Alain Munafo, Walter Fischli, Philippe Coassolo, Peter van Brummelen, Cornelis H. Kleinbloesem, Bernard Waeber, and Hans R. Brunner. "Effect of the Renin Response During Renin Inhibition." Journal of Cardiovascular Pharmacology 18, no. 3 (September 1991): 299–307. http://dx.doi.org/10.1097/00005344-199109000-00001.

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Danser, A. H. Jan, and Jaap Deinum. "Renin, Prorenin and the Putative (Pro)renin Receptor." Hypertension 46, no. 5 (November 2005): 1069–76. http://dx.doi.org/10.1161/01.hyp.0000186329.92187.2e.

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Nakamura, N., F. Soubrier, J. Menard, J. J. Panthier, F. Rougeon, and P. Corvol. "Nonproportional changes in plasma renin concentration, renal renin content, and rat renin messenger RNA." Hypertension 7, no. 6_pt_1 (November 1985): 855–59. http://dx.doi.org/10.1161/01.hyp.7.6.855.

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REICHBERG, S. "Direct renin: an automated immunoassay for renin with sensitivity comparable to plasma renin activity." American Journal of Hypertension 15, no. 4 (April 2002): A215. http://dx.doi.org/10.1016/s0895-7061(02)02855-8.

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Nabi, AHM N., Kazal B. Biswas, Akio Ebihara, Tsutomu Nakagawa, and Fumiaki Suzuki. "RENIN ANGIOTENSIN SYSTEM IN THE CONTEXT OF RENIN, PRORENIN, AND THE (PRO)RENIN RECEPTOR." Reviews in Agricultural Science 1 (2013): 43–60. http://dx.doi.org/10.7831/ras.1.43.

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40

Batenburg, Wendy W., and A. H. Jan Danser. "(Pro)renin and its receptors: pathophysiological implications." Clinical Science 123, no. 3 (April 5, 2012): 121–33. http://dx.doi.org/10.1042/cs20120042.

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Tissue angiotensin generation depends on the uptake of circulating (kidney-derived) renin and/or its precursor prorenin [together denoted as (pro)renin]. Since tissue renin levels are usually somewhat higher than expected based upon the amount of (renin-containing) blood in tissue, an active uptake mechanism has been proposed. Several candidates have been evaluated in the past three decades, including a renin-binding protein, the mannose 6-phosphate/insulin-like growth factor II receptor and the (pro)renin receptor. Although the latter seemed the most promising, its nanomolar affinity for renin and prorenin is several orders of magnitude above their actual (picomolar) levels in blood, raising doubt on whether (pro)renin–(pro)renin receptor interaction will ever occur in vivo. A wide range of in vitro studies have now demonstrated (pro)renin-receptor-induced effects at nanomolar renin and prorenin concentrations, resulting in a profibrotic phenotype. In addition, beneficial in vivo effects of the putative (pro)renin receptor blocker HRP (handle region peptide) have been observed, particularly in diabetic animal models. Despite these encouraging results, many other studies have reported either no or even contrasting effects of HRP, and (pro)renin-receptor-knockout studies revealed lethal consequences that are (pro)renin-independent, most probably due to the fact that the (pro)renin receptor co-localizes with vacuolar H+-ATPase and possibly determines the stability of this vital enzyme. The present review summarizes all of the recent findings on the (pro)renin receptor and its blockade, and critically compares it with the other candidates that have been proposed to mediate (pro)renin uptake from blood. It ends with the conclusion that the (pro)renin–(pro)renin receptor interaction, if it occurs in vivo, is limited to (pro)renin-synthesizing organs such as the kidney.

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Razga, Zsolt, Gabor Kovacs, Nikolett Bódi, Petra Talapka, and Mária Bagyánszki. "Regulation of (Pro)Renin Receptor in Renin-Positive Smooth Muscle Cells of Kidney Arterioles in Rats with STZ-Induced Diabetes." International Journal of Nephrology 2019 (March 28, 2019): 1–6. http://dx.doi.org/10.1155/2019/6971928.

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Objective. The nephron (pro)renin receptor may play a pathophysiological role in renal disorders in hypertension or diabetes. The aim of this study was to determine the relationship of (pro)renin receptors and transdifferentiation between the renin-negative and renin-positive SMCs in the afferent arteriole by estimating the distribution of (pro)renin receptors in renin-positive and renin-negative SMCs of the afferent arteriole of kidneys in normal and streptozotocin- (STZ-) induced diabetic rats. Therefore in diabetes the renin granulation of afferent arterioles is different as in normal, the diabetes model for finding the differences to normal in distribution of (pro)renin receptors of afferent arterioles was used. Method. To estimate the number of (pro)renin receptors in arteriolar SMCs a special protocol of immunohistochemistry to stereology was followed. Results. Our results showed that on the surface of renin-positive SMCs the number of (pro)renin receptors was upregulated, while in the cytoplasm of SMCs there was downregulation in comparison to renin-negative SMCs. There is a significant difference between the number of (pro)renin receptors on the surface and in the cytoplasm of renin-positive SMCs in normal rats. These differences in the number of (pro)renin receptors were not present in rats with STZ-induced diabetes. Any other differences in the number of (pro)renin receptors between the STZ-induced diabetic and normal rats were not detected. The tissue level of angiotensin II did not change in the kidneys of STZ-induced diabetic rats. Conclusion. The distribution of (pro)renin receptors in afferent arteriolar SMCs is related to renin granulation of SMCs, but independent of angiotensin II plasma or tissue levels in the kidney.

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Pentz, Ellen Steward, Magali Cordaillat, Oscar A. Carretero, Ana E. Tucker, Maria Luisa S. Sequeira Lopez, and R. Ariel Gomez. "Histone acetyl transferases CBP and p300 are necessary for maintenance of renin cell identity and transformation of smooth muscle cells to the renin phenotype." American Journal of Physiology-Heart and Circulatory Physiology 302, no. 12 (June 15, 2012): H2545—H2552. http://dx.doi.org/10.1152/ajpheart.00782.2011.

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In response to a homeostatic threat circulating renin increases by increasing the number of cells expressing renin by dedifferentiation and re-expression of renin in arteriolar smooth muscle cells (aSMCs) that descended from cells that expressed renin in early life. However, the mechanisms that govern the maintenance and reacquisition of the renin phenotype are not well understood. The cAMP pathway is important for renin synthesis and release: the transcriptional effects are mediated by binding of cAMP responsive element binding protein with its co-activators, CBP and p300, to the cAMP response element in the renin promoter. We have shown previously that mice with conditional deletion of CBP and p300 (cKO) in renin cells had severely reduced renin expression in adult life. In this study we investigated when the loss of renin-expressing cells in the cKO occurred and found that the loss of renin expression becomes evident after differentiation of the kidney is completed during postnatal life. To determine whether CBP/p300 is necessary for re-expression of renin we subjected cKO mice to low sodium diet + captopril to induce retransformation of aSMCs to the renin phenotype. The cKO mice did not increase circulating renin, their renin mRNA and protein expression were greatly diminished compared with controls, and only a few aSMCs re-expressed renin. These studies underline the crucial importance of the CREB/CBP/p300 complex for the ability of renin cells to retain their cellular memory and regain renin expression, a fundamental survival mechanism, in response to a threat to homeostasis.

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Chansel, D., J. C. Dussaule, N. Ardaillou, and R. Ardaillou. "Identification and regulation of renin in human cultured mesangial cells." American Journal of Physiology-Renal Physiology 252, no. 1 (January 1, 1987): F32—F38. http://dx.doi.org/10.1152/ajprenal.1987.252.1.f32.

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Renin activity was measured in the incubation medium, and the cellular extract of human mesangial cells, which had been cultured in the presence of renin-free human plasma (three kidneys; 4-7 passages). Active renin and total renin obtained after trypsin treatment was estimated by radioimmunoassay of angiotensin I using renin-free human plasma as a substrate. Mesangial cell renin had characteristics similar to those of standard human renin; optimum enzymatic activity at pH 5.8, marked inhibition in the presence of two (monoclonal and polyclonal) human renin-specific antibodies and of SR 42128, a new potent statine-containing renin inhibitory peptide. The synthetic capability of the mesangial cells varied markedly with the original kidney (1-49 and 0.3-0.9 ng X h-1 X mg-1 for total renin in the medium and the cellular extract respectively). Renin was secreted mainly as inactive renin. Prostaglandin E2 (PGE2) and carba-prostaglandin I2 (PGI2) (a stable analogue) produced a dose-dependent (0.1-1.10 microM) increase in renin activity in both the cellular extract and the culture medium. Isoproterenol (200 microM) increased renin activity only in the medium. The effects of these agonists were more marked on inactive than on active renin. These results demonstrate that cultured human mesangial cells synthesize and release renin in a stable manner over a long period of culture, thus providing a useful tool for the in vitro study of renin secretion and its control.

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Horváth, Dóra, Zoltán Lőcsei, Zsuzsanna Csizmadia, Erzsébet Toldy, István Szabolcs, and Károly Rácz. "Clinical evaluation of the renin-aldosterone system: Comparison of two methods in different clinical conditions." Orvosi Hetilap 153, no. 43 (October 2012): 1701–10. http://dx.doi.org/10.1556/oh.2012.29476.

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Introduction: Measurement of plasma aldosterone/renin ratio is the key step in the diagnosis of primary aldosteronism. Aim: The aim of the authors was to analyze and compare the diagnostic utility of plasma aldosterone/renin activity and plasma aldosterone/renin concentration ratios. Methods: Plasma aldosterone and plasma renin activity were determined by radioimmunoassays and plasma renin concentration was measured by immunoradiometric assay in 134 subjects (80 women and 54 men, aged 46±15.5 years) including 49 healthy blood donors (control group), 59 patients with hypertension (25 treated and 34 untreated) and 26 patients with incidentally discovered adrenal adenomas. Results: There was a weak correlation (r = 0.59) between plasma renin activity and plasma renin concentration in the lower range (plasma renin activity, 0.63±0.41 ng/ml/h; plasma renin concentration, 8.1±4.9 ng/l). Considering the cut-off value of plasma aldosterone/renin ratios determined in controls (plasma aldosterone/renin activity ratio, 30 ng/dl/ng/ml/h; plasma aldosterone/renin concentration ratio, 3.0 ng/dl/ng/l), high proportion of falsely positive results were found among patients on beta-receptor blocker therapy (plasma aldosterone/renin activity ratio, 22.2%; plasma aldosterone/renin concentration ratio, 44.4%) Conclusion: The widely used plasma aldosterone/renin activity ratio can only be replaced with plasma aldosterone/renin concentration ratio with precaution on different clinical conditions. Orv. Hetil., 2012, 153, 1701–1710.

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45

Sequeira-Lopez, Maria Luisa S., Vidya K. Nagalakshmi, Minghong Li, Curt D. Sigmund, and R. Ariel Gomez. "Vascular versus tubular renin: role in kidney development." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 309, no. 6 (September 15, 2015): R650—R657. http://dx.doi.org/10.1152/ajpregu.00313.2015.

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Renin, the key regulated enzyme of the renin-angiotensin system regulates blood pressure, fluid-electrolyte homeostasis, and renal morphogenesis. Whole body deletion of the renin gene results in severe morphological and functional derangements, including thickening of renal arterioles, hydronephrosis, and inability to concentrate the urine. Because renin is found in vascular and tubular cells, it has been impossible to discern the relative contribution of tubular versus vascular renin to such a complex phenotype. Therefore, we deleted renin independently in the vascular and tubular compartments by crossing Ren1 c fl/fl mice to Foxd1-cre and Hoxb7-cre mice, respectively. Deletion of renin in the vasculature resulted in neonatal mortality that could be rescued with daily injections of saline. The kidneys of surviving mice showed the absence of renin, hypertrophic arteries, hydronephrosis, and negligible levels of plasma renin. In contrast, lack of renin in the collecting ducts did not affect kidney morphology, intra-renal renin, or circulating renin in basal conditions or in response to a homeostatic stress, such as sodium depletion. We conclude that renin generated in the renal vasculature is fundamental for the development and integrity of the kidney, whereas renin in the collecting ducts is dispensable for normal kidney development and cannot compensate for the lack of renin in the vascular compartment. Further, the main source of circulating renin is the kidney vasculature.

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46

Campbell, Duncan J., Juerg Nussberger, Michael Stowasser, A. H. Jan Danser, Alberto Morganti, Erik Frandsen, and Joël Ménard. "Activity Assays and Immunoassays for Plasma Renin and Prorenin: Information Provided and Precautions Necessary for Accurate Measurement." Clinical Chemistry 55, no. 5 (May 1, 2009): 867–77. http://dx.doi.org/10.1373/clinchem.2008.118000.

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AbstractBackground: Measurement of plasma renin is important for the clinical assessment of hypertensive patients. The most common methods for measuring plasma renin are the plasma renin activity (PRA) assay and the renin immunoassay. The clinical application of renin inhibitor therapy has thrown into focus the differences in information provided by activity assays and immunoassays for renin and prorenin measurement and has drawn attention to the need for precautions to ensure their accurate measurement.Content: Renin activity assays and immunoassays provide related but different information. Whereas activity assays measure only active renin, immunoassays measure both active and inhibited renin. Particular care must be taken in the collection and processing of blood samples and in the performance of these assays to avoid errors in renin measurement. Both activity assays and immunoassays are susceptible to renin overestimation due to prorenin activation. In addition, activity assays performed with peptidase inhibitors may overestimate the degree of inhibition of PRA by renin inhibitor therapy. Moreover, immunoassays may overestimate the reactive increase in plasma renin concentration in response to renin inhibitor therapy, owing to the inhibitor promoting conversion of prorenin to an open conformation that is recognized by renin immunoassays.Conclusions: The successful application of renin assays to patient care requires that the clinician and the clinical chemist understand the information provided by these assays and of the precautions necessary to ensure their accuracy.

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47

Eggena, P., P. Willsey, N. Jamgotchian, L. Truckenbrod, M. S. Hu, J. D. Barrett, M. P. Eggena, K. Clegg, F. Nakhoul, and D. B. Lee. "Influence of recombinant human erythropoietin on blood pressure and tissue renin-angiotensin systems." American Journal of Physiology-Endocrinology and Metabolism 261, no. 5 (November 1, 1991): E642—E646. http://dx.doi.org/10.1152/ajpendo.1991.261.5.e642.

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In humans, blockade of the renin-angiotensin system with angiotensin converting-enzyme inhibitors (ANG CEI) prevents the rise in blood pressure associated with the administration of recombinant human erythropoietin (rhEPO). This study was conducted to determine whether rhEPO elevates blood pressure in normal Wistar rats and whether the renin-ANG system is affected. Groups of 10 rats each were given rhEPO, ANG CEI (enalapril), rhEPO + ANG CEI, or vehicle. Renin and/or renin substrate mRNA was measured in aortas, kidney, and heart; renin activity (PRA), inactive renin, and renin substrate were measured in plasma. rhEPO raised blood pressure in the normal rat without changing the plasma renin system. ANG CEI prevented this blood pressure rise. Renin-specific mRNA was increased by rhEPO in renal tissue, and renin substrate mRNA was significantly elevated in the kidney and aorta. mRNA for renin and renin substrate were not altered in the heart. In both aorta and kidney, a significant correlation was observed between renin substrate mRNA and blood pressure. The data indicate that rhEPO modulates specific tissue renin-ANG systems, which may contribute to blood pressure elevation.

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48

Katz, S. A., J. A. Opsahl, L. M. Forbis, and W. Ayenew. "Active renin and renin glycoform dynamics in the carotid artery." American Journal of Physiology-Heart and Circulatory Physiology 271, no. 1 (July 1, 1996): H184—H191. http://dx.doi.org/10.1152/ajpheart.1996.271.1.h184.

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Active renin and five major active renin glycoforms were measured in plasma and the carotid wall of anesthetized rabbits before and after 1.5- and 24-h bilateral nephrectomy (BNX). Before BNX, there was no difference in renin glycoform proportions between plasma and the carotid wall. Plasma renin concentration (PRC) fell by 67% after 1.5-h BNX due to preferential clearance of renin glycoforms I+II, but no significant change in renin concentration was seen in the carotid artery (or aorta). Twenty-four hours after BNX, PRC and carotid wall renin concentrations were reduced by 99.7 and 97.7%, respectively, while the proportion of renin glycoforms I+II in the carotid wall was significantly elevated. These data are consistent with the view that vascular renin is derived from plasma renin of renal origin. After BNX, renin disappearance from the carotid (and aortic wall) is slower than renin decay from plasma, and the less negatively charged active renin glycoforms I+II exit the carotid wall much more slowly than the more negatively charged glycoforms. After 24-h BNX, renin glycoforms I+II were still effluxing from the vascular wall and represented the only glycoforms present in the carotid wall.

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Ichihara, Atsuhiro, Hiroyuki Kobori, Yutaka Miyashita, Matsuhiko Hayashi, and Takao Saruta. "Differential effects of thyroid hormone on renin secretion, content, and mRNA in juxtaglomerular cells." American Journal of Physiology-Endocrinology and Metabolism 274, no. 2 (February 1, 1998): E224—E231. http://dx.doi.org/10.1152/ajpendo.1998.274.2.e224.

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The effects of thyroid hormone on renin secretion, renin content, and renin mRNA levels in juxtaglomerular (JG) cells harvested from rat kidneys were determined by radioimmunoassays and reverse transcriptase-polymerase chain reaction. Despite a lack of immediate effect, incubation with triiodothyronine dose dependently increased renin secretion during the first 6 h and elevated renin content and renin mRNA levels during the subsequent period. Simultaneous incubation with triiodothyronine and the calcium ionophore A-23187 abolished the increase in renin secretion and attenuated the increase in renin content but did not affect the increase in renin mRNA levels. During simultaneous incubation with triiodothyronine and the adenylate cyclase inhibitor SQ-22536 or membrane-soluble guanosine 3′,5′-cyclic monophosphate (cGMP), the increases in renin secretion, content, and mRNA were similar to those observed in the presence of triiodothyronine alone, except for a cGMP-induced attenuation of the increase in renin secretion. These findings suggest that thyroid hormone stimulates renin secretion by JG cells through the calcium-dependent mechanism, whereas the stimulation of renin gene expression by thyroid hormone does not involve intracellular calcium or cyclic nucleotides.

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50

Castrop, Hayo, Klaus Höcherl, Armin Kurtz, Frank Schweda, Vladimir Todorov, and Charlotte Wagner. "Physiology of Kidney Renin." Physiological Reviews 90, no. 2 (April 2010): 607–73. http://dx.doi.org/10.1152/physrev.00011.2009.

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The protease renin is the key enzyme of the renin-angiotensin-aldosterone cascade, which is relevant under both physiological and pathophysiological settings. The kidney is the only organ capable of releasing enzymatically active renin. Although the characteristic juxtaglomerular position is the best known site of renin generation, renin-producing cells in the kidney can vary in number and localization. (Pro)renin gene transcription in these cells is controlled by a number of transcription factors, among which CREB is the best characterized. Pro-renin is stored in vesicles, activated to renin, and then released upon demand. The release of renin is under the control of the cAMP (stimulatory) and Ca2+(inhibitory) signaling pathways. Meanwhile, a great number of intrarenally generated or systemically acting factors have been identified that control the renin secretion directly at the level of renin-producing cells, by activating either of the signaling pathways mentioned above. The broad spectrum of biological actions of (pro)renin is mediated by receptors for (pro)renin, angiotensin II and angiotensin-( 1 – 7 ).

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Journal articles on the topic 'Renin'

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