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14-September-2008 18:02:48 - Renin It has been suggested that PRA Medical be merged into this article or section. Discuss Not to be confused with rennin, the active enzyme in rennet. Renin Molecular structure of renin Symbols: REN Other names: Angiotensinogenase Genetic data Locus: Chr. 1 q32 Protein Structure/Function Protein length: 406 Amino Acids Molecular Weight: 45060 Da Functions: Converts angiotensinogen to angiotensin I Motifs: SP motif Alternative Products: 2 known isoforms produced from alternative splicing Other Taxa expressing: Homo sapiens; homologs many metazoan taxa Subcellular localization: Extracellular Biophysicochemical properties: KM=1 µmol/L for angiotensinogen Database Links EC number: 3.4.23.15 Entrez: 5972 OMIM: 179820 RefSeq: NM_000537 UniProt: P00797 Renin pronounced Ree-nin or RÄ“-nin IPA: /ˈriË?nɨn/, also known as Angiotensinogenase, is a circulating enzyme that participates in the body's renin-angiotensin system RAS that mediates the following: Extracellular volume i.e. that of your blood, lymph and other body fluids, and Arterial vasoconstriction - the tone of the musculature of arteries. Thus it regulates one's mean arterial blood pressure. Contents 1 Discovery 2 Biochemistry and Physiology 2.1 Structure 2.2 Secretion: 2.3 The Renin-Angiotensin-Aldosterone Axis / Renin-Angiotensin SystemRAS: 3 Function 4 Genetics 5 Clinical implications 6 See also 7 References 8 External links Discovery Renin was discovered, characterized and named in 1898 by Robert Tigerstedt, Professor of Physiology at the Karolinska Institute in Stockholm.citation needed Biochemistry and Physiology Structure The primary structure of renin precursor consists of 406 amino acids with a pre- and a pro- segment carrying 20 and 46 amino acids respectively. Mature renin contains 340 amino acids and has a mass of 37 kD.1 Secretion: The peptide hormone is secreted by the kidney from specialized cells called granular cells of the juxtaglomerular apparatus in response to: A decrease in arterial blood pressure that could be related to a decrease in blood volume as detected by baroreceptors pressure sensitive cells. This is the most causal link between blood pressure and renin secretion the other two methods operate via longer pathways. A decrease in sodium chloride levels in the ultra-filtrate of the nephron. This flow is measured by the macula densa of the juxtaglomerular apparatus. Sympathetic nervous system activity, that also controls blood pressure, acting through the β1 adrenergic receptors. Human Renin is secreted by at least 2 cellular pathways: a constitutive pathway for the secretion of prorenin and a regulated pathway for the secretion of mature renin.2 The Renin-Angiotensin-Aldosterone Axis / Renin-Angiotensin SystemRAS: Mechanism of action of Renin: The enzyme circulates in the blood stream and breaks down hydrolyzes angiotensinogen secreted from the liver into the peptide angiotensin I. Rest of the RAS: Angiotensin I is further cleaved in the lungs by endothelial bound angiotensin converting enzyme ACE into angiotensin II, the most vasoactive peptide.34 Angiotensin II is a potent constrictor of the all blood vessels. It acts on the musculature and there by raises the resistance posed by these arteries to the heart. The heart, trying to overcome this increase in its 'load' works more vigorously, causing the blood pressure to rise. Angiotensin II also acts on the adrenal glands too and releases Aldosterone, which stimulates the epithelial cells of the kidneys to increase re-absorption of salt and water leading to raised blood volume and raised blood pressure. The RAS also acts on the CNS to increase water intake by stimulating thirst, as well as conserving blood volume, by reducing urinary loss through the secretion of ADH from the posterior pituitary gland. The normal concentration in adult human plasma is 1.98-24.6 ng/L in the upright position.5 Function Renin activates the renin-angiotensin system by cleaving angiotensinogen, produced by the liver, to yield angiotensin I, which is further converted into angiotensin II by ACE, the angiotensin-converting enzyme primarily within the capillaries of the lungs. Angiotensin II then constricts blood vessels, increases the secretion of ADH and aldosterone, and stimulates the hypothalamus to activate the thirst reflex, each leading to an increase in blood pressure. Renin is secreted from juxtaglomerular cells of the afferent arterioles, which are activated via signaling the release of prostaglandins from the macula densa, which respond to the rate of fluid flow through the distal tubule, by decreases in renal perfusion pressure through stretch receptors in the vascular wall, and by nervous stimulation, mainly through beta-1 receptor activation. A drop in the rate of flow past the macula densa implies a drop in renal filtration pressure. Renin's primary function is therefore to eventually cause an increase in blood pressure, leading to restoration of perfusion pressure in the kidneys. Renin can bind to ATP6AP2, which results in a fourfold increase in the conversion of angiotensinogen to angiotensin I over that shown by soluble renin. In addition, renin binding results in phosphorylation of serine and tyrosine residues of ATP6AP2.6 Genetics The gene for renin, REN, spans 12 kb of DNA and contains 8 introns.7 It produces several mRNA that encode different REN isoforms. Clinical implications An over-active renin-angiotension system leads to vasoconstriction and retention of sodium and water. These effects lead to hypertension. Therefore, renin inhibitors can be used for the treatment of hypertension. This is measured by the plasma renin activityPRA. Aliskiren, is a first-in-class oral renin inhibitor, developed by Novartis in conjunction with the biotech company Speedel. It was approved by the US Food and Drug Administration in 2007. It is an octanamide, is the first known representative of a new class of completely non-peptide, low-molecular weight, orally active transition-state renin inhibitors. Designed through the use of molecular modeling techniques, it is a potent and specific in vitro inhibitor of human renin IC50 in the low nanomolar range, with a plasma half-life of ≈24 hours. Tekturna has good water solubility and low lipophilicity and is resistant to biodegradation by peptidases in the intestine, blood circulation, and the liver. It was approved by the United States FDA on 6 March 2007, and for use in Europe on 27 August 2007. Its trade name is Tekturna in the USA, and Rasilez in the UK. See also Angiotensin-converting enzyme plasma renin activity. References ^ Imai T, Miyazaki H, Hirose S, et al December 1983. Cloning and sequence analysis of cDNA for human renin precursor. Proc. Natl. Acad. Sci. U.S.A. 80 24: 7405-9. PMID 6324167. PMC:389959. ^ Pratt RE, Flynn JA, Hobart PM, Paul M, Dzau VJ March 1988. Different secretory pathways of renin from mouse cells transfected with the human renin gene. J. Biol. Chem. 263 7: 3137-41. PMID 2893797. ^ Fujino T, Nakagawa N, Yuhki K, et al September 2004. Decreased susceptibility to renovascular hypertension in mice lacking the prostaglandin I2 receptor IP. J. Clin. Invest. 114 6: 805-12. doi:10.1172/JCI21382. PMID 15372104. PMC:516260. ^ Brenner Rector's The Kidney, 7th ed., Saunders, 2004. pp.2118-2119.Full Text with MDConsult subscription ^ Hamilton Regional Laboratory Medicine Program - Laboratory Reference Centre Manual. Renin Direct ^ Nguyen G, Delarue F, Burcklé C, Bouzhir L, Giller T, Sraer JD June 2002. Pivotal role of the renin/prorenin receptor in angiotensin II production and cellular responses to renin. J. Clin. Invest. 109 11: 1417-27. doi:10.1172/JCI14276. PMID 12045255. ^ Hobart PM, Fogliano M, O'Connor BA, Schaefer IM, Chirgwin JM August 1984. Human renin gene: structure and sequence analysis. Proc. Natl. Acad. Sci. U.S.A. 81 16: 5026-30. PMID 6089171. PMC:391630. External links MeSH Renin renin at eMedicine Dictionary v d e Endocrine system: hormones/endocrine glands Peptide hormones, Steroid hormones Hypothalamic-pituitary Hypothalamus: TRH, CRH , GnRH, GHRH, somatostatin, dopamine - Posterior pituitary: vasopressin, oxytocin - Anterior pituitary: α FSH, LH, TSH, GH, prolactin, POMC ACTH, MSH, endorphins, lipotropin Adrenal axis Adrenal medulla: epinephrine, norepinephrine - Adrenal cortex: aldosterone, cortisol, DHEA Thyroid axis Thyroid: thyroid hormone T3 and T4 - calcitonin - Parathyroid: PTH Gonadal axis Testis: testosterone, AMH, inhibin - Ovary: estradiol, progesterone, inhibin/activin, relaxin pregnancy Other end. glands Pancreas: glucagon, insulin, somatostatin - Pineal gland: melatonin Non-end. glands Placenta: hCG, HPL, estrogen, progesterone - Kidney: renin, EPO, calcitriol, prostaglandin - Heart atrium: ANP - Stomach: gastrin, ghrelin - Duodenum: CCK, GIP, secretin, motilin, VIP - Ileum: enteroglucagon - Adipose tissue: leptin, adiponectin, resistin - Thymus: Thymosin - Thymopoietin - Thymulin - Skeleton: Osteocalcin - Liver/other: Insulin-like growth factor IGF-1, IGF-2 Target-derived NGF, BDNF, NT-3 v d e Cardiovascular system Systemic circulation Heart → Aorta → Arteries → Arterioles → Capillaries → Venules → Veins → Vena cava → Heart Pulmonary circulation Heart → Pulmonary arteries → Lungs → Pulmonary vein → Heart Blood vessels Endothelium - Tunica intima - Tunica media - Tunica externa v d e Urinary system, physiology: renal physiology and acid base physiology Filtration Renal blood flow - Ultrafiltration - Countercurrent exchange Hormones affecting filtration Antidiuretic hormone ADH - Aldosterone - Atrial natriuretic peptide Secretion/clearance Pharmacokinetics - Clearance of medications Reabsorption Solvent drag - Na+ - Cl- - urea - glucose - oligopeptides - protein Endocrine Renin - Erythropoietin EPO - Calcitriol Active vitamin D - Prostaglandins Assessing Renal function/ Measures of dialysis Glomerular filtration rate - Creatinine clearance - Renal clearance ratio - Urea reduction ratio - Kt/V - Standardized Kt/V - Hemodialysis product - PAH clearance Effective renal plasma flow - Extraction ratio Acid base physiology Fluid balance - Darrow Yannet diagram - Body water - Interstitial fluid - Extracellular fluid - Intracellular fluid/Cytosol - Plasma - Transcellular fluid - Base excess - Davenport diagram - Anion gap - Arterial blood gas Buffering/compensation Bicarbonate buffering system - Respiratory compensation - Renal compensation v d e Proteases: aspartic acid proteases EC 3.4.23 Vertebrate Pepsin · Chymosin · Renin · Signal peptide peptidase · Beta secretase Pathogenic Plasmepsin · HIV-1 protease Retrieved from http://en..org/wiki/Renin Categories: EC 3.4.23 | Hormones of the kidneys | Peptide hormones | Renal physiologyHidden categories: Articles to be merged since March 2008 | All articles with statements | Articles with statements since March 2008 Views Article Discussion this page History Personal tools Log in / create account Navigation Main page Contents Featured content Current events Random article Search Go Search Interaction Community portal Recent changes Contact Donate to Help Toolbox What links here Related changes Upload file Special pages Printable version Permanent link Cite this page Languages العربية Deutsch Þ‹Þ¨ÞˆÞ¬Þ€Þ¨Þ„Þ¦Þ?Þ° Español Français Italiano Nederlands 日本語 ‪Norsk bokmÃ¥l‬ Polski Português РуÑ?Ñ?кий Simple English СрпÑ?ки / Srpski Svenska This page was last modified on 10 September 2008, at 01:26
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