WordNet

of or relating to a cavity or chamber in the body (especially one of the upper chambers of the heart)
amide combining the amino group of one amino acid with the carboxyl group of another; usually obtained by partial hydrolysis of protein
of or relating to natriuresis

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/06/02 22:55:15」(JST)

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Atrial natriuretic peptide (ANP), atrial natriuretic factor (ANF), atrial natriuretic hormone (ANH), Cardionatrine, Cardiodilatine (CDD) or atriopeptin, is a powerful vasodilator, and a protein (polypeptide) hormone secreted by heart muscle cells.^[1]^[2]^[3] It is involved in the homeostatic control of body water, sodium, potassium and fat (adipose tissue). It is released by muscle cells in the upper chambers (atria) of the heart (atrial myocytes) in response to high blood volume. ANP acts to reduce the water, sodium and adipose loads on the circulatory system, thereby reducing blood pressure.^[1] ANP has exactly the opposite function of the aldosterone secreted by the zona glomerulosa.^[4]

Structure

ANP is a 28-amino acid peptide with a 17-amino acid ring in the middle of the molecule. The ring is formed by a disulfide bond between two cysteine residues at positions 7 and 23. ANP is closely related to BNP (brain natriuretic peptide) and CNP (C-type natriuretic peptide), which all share the same amino acid ring. ANP was discovered in 1981 by a team in Kingston, Ontario, Canada, led by Adolfo J. de Bold after they made the seminal observation that injection of atrial (but not ventricular) tissue extracts into rats caused copious natriuresis.^[5]

Production

The ANP gene has 3 exons and 2 introns; it codes 151-amino acid preproANP. Cleaving the 25-amino acid N-terminal results in pro-ANP. Corin, a membrane serine protease, cleaves the final ANP, the 28-amino acid C-terminal.

ANP is produced, stored, and released mainly by cardiac myocytes of the atria of the heart. Synthesis of ANP also takes place in the ventricles, brain, suprarenal glands, and renal glands. It is released in response to atrial stretch and a variety of other signals induced by hypervolemia, exercise, or caloric restriction.^[1] The hormone is constitutively expressed in the ventricles in response to stress induced by increased afterload (e.g. increased ventricular pressure from aortic stenosis) or injury (e.g. myocardial infarction).

ANP is secreted in response to:

Atrial distention, stretching of the vessel walls^[1]
Sympathetic stimulation of β-adrenoceptors
Raised sodium concentration (hypernatremia), though sodium concentration is not the direct stimulus for increased ANP secretion^[1]
Angiotensin-II
Endothelin, a potent vasoconstrictor

The atria become distended by high extracellular fluid and blood volume, and atrial fibrillation. It should be noted that ANP secretion increases in response to immersion of the body in water, which causes atrial stretch due to an altered distribution of intravascular fluid. ANP secretion in response to exercise has also been demonstrated in horses.^[6]

ANP is also produced by the placenta in pregnant women. The exact function of this remains unclear. ^[7]

Receptors

Three types of atrial natriuretic peptide receptors have been identified on which natriuretic peptides act. They are all cell surface receptors and are designated:

guanylyl cyclase-A (GC-A) also known as natriuretic peptide receptor-A (NPRA/ANP_A) or NPR1
guanylyl cyclase-B (GC-B) also known as natriuretic peptide receptor-B (NPRB/ANP_B) or NPR2
natriuretic peptide clearance receptor (NPRC/ANP_C) or NPR3

NPR-A and NPR-B have a single membrane-spanning segment with an extracellular domain that binds the ligand. The intracellular domain maintains two consensus catalytic domains for guanylyl cyclase activity. Binding of a natriuretic peptide induces a conformational change in the receptor that causes receptor dimerization and activation. Thus, binding of ANP to its receptor causes the conversion of GTP to cGMP and raises intracellular cGMP. As a consequence, cGMP activates a cGMP-dependent kinase (PKG or cGK) that phosphorylates proteins at specific serine and threonine residues. In the medullary collecting duct, the cGMP generated in response to ANP may act not only through PKG but also via direct modulation of ion channels.^[8] NPR-C functions mainly as a clearance receptor by binding and sequestering ANP from the circulation. All natriuretic peptides are bound by the NPR-C. Atrial natriuretic peptide and brain natriuretic peptide bind and activate GC-A, whereas CNP binds and activates GC-B.^[9]

Physiological effects

ANP binds to a specific set of receptors – ANP receptors. Receptor-agonist binding causes a reduction in blood volume and, therefore, a reduction in cardiac output and systemic blood pressure. Lipolysis is increased and renal sodium reabsorption is decreased. The overall effect of ANP on the body is to counter increases in blood pressure and volume caused by the renin-angiotensin system.

Renal

Dilates the afferent glomerular arteriole, constricts the efferent glomerular arteriole, and relaxes the mesangial cells. This increases pressure in the glomerular capillaries, thus increasing the glomerular filtration rate (GFR), resulting in greater excretion of sodium and water.

Increases blood flow through the vasa recta, which will wash the solutes (NaCl and urea) out of the medullary interstitium.^[10] The lower osmolarity of the medullary interstitium leads to less reabsorption of tubular fluid and increased excretion.

Decreases sodium reabsorption in the distal convoluted tubule (interaction with NCC)^[11] and cortical collecting duct of the nephron via guanosine 3',5'-cyclic monophosphate (cGMP) dependent phosphorylation of ENaC

Inhibits renin secretion, thereby inhibiting the renin-angiotensin-aldosterone system.

Reduces aldosterone secretion by the adrenal cortex.

Atrial natriuretic peptide (ANP) increases Na⁺ excretion by decreasing the amount of Na⁺ reabsorbed from the inner medullary collecting duct via a decrease in the permeability of the apical membrane of the collecting duct epithelial cells. Less Na⁺ is able to enter the epithelial cells and, therefore, less Na⁺ is reabsorbed. ANP also increases Na⁺ excretion by increasing the filtered load of Na⁺.

Vascular

Relaxes vascular smooth muscle in arterioles and venules by:

Membrane Receptor-mediated elevation of vascular smooth muscle cGMP
Inhibition of the effects of catecholamines

Cardiac

Inhibits maladaptive cardiac hypertrophy
Mice lacking cardiac NPRA develop increased cardiac mass and severe fibrosis and die suddenly^[12]
Re-expression of NPRA rescues the phenotype.

It may be associated with isolated atrial amyloidosis.^[13]

Adipose tissue

Increases the release of free fatty acids from adipose tissue. Plasma concentrations of glycerol and nonesterified fatty acids are increased by i.v. infusion of ANP in humans.
Activates adipocyte plasma membrane type A guanylyl cyclase receptors NPR-A
Increases intracellular cGMP levels that induce the phosphorylation of a hormone-sensitive lipase and perilipin A via the activation of a cGMP-dependent protein kinase-I (cGK-I)
Does not modulate cAMP production or PKA activity

Degradation

Regulation of the effects of ANP is achieved through gradual degradation of the peptide by the enzyme neutral endopeptidase (NEP). Recently, NEP inhibitors have been developed; however they have not yet been licensed. They may be clinically useful in treating congestive heart disease.

Other natriuretic factors

In addition to the mammalian natriuretic peptides (ANP, BNP, CNP), other natriuretic peptides with similar structure and properties have been isolated elsewhere in the animal kingdom. Tervonen (1998) described a salmon natriuretic peptide known as salmon cardiac peptide,^[14] while dendroaspis natriuretic peptide (DNP) can be found in the venom of the green mamba, a species of African snake.^[15]

Pharmacological modulation

Neutral endopeptidase (NEP) is the enzyme that metabolizes natriuretic peptides. Several inhibitors of NEP are currently being developed to treat disorders ranging from hypertension to heart failure. Most of them are dual inhibitors. Omapatrilat (dual inhibitor of NEP and angiotensin-converting enzyme) developed by BMS did not receive FDA approval due to angioedema safety concerns. Other dual inhibitors of NEP with ACE/angiotensin receptor are currently being developed by pharmaceutical companies.^[16]

References

^ ^a ^b ^c ^d ^e Widmaier, Eric P.; Hershel Raff; Kevin T. Strang (2008). Vander's Human Physiology, 11th Ed. McGraw-Hill. pp. 291, 509–10. ISBN 978-0-07-304962-5.
^ Potter LR, Yoder AR, Flora DR, Antos LK, Dickey DM (2009). "Natriuretic peptides: their structures, receptors, physiologic functions and therapeutic applications". Handb Exp Pharmacol. Handbook of Experimental Pharmacology 191 (191): 341–66. doi:10.1007/978-3-540-68964-5_15. ISBN 978-3-540-68960-7. PMID 19089336.
^ Addicks K, Forssmann WG, Henkel H, Holthausen U, Menz V, Rippegather G, Ziskoven D (1989). "Calcium-calmodulin antagonists Influences the release of cardiodilatin/ANP from atrial cardiocytes". In Wambach G, Kaufmann W. Endocrinology of the heart. Berlin: Springer-Verlag. ISBN 0-387-51409-0.
^ Marieb Human Anatomy & Physiology 9th edition, chapter:16, page:629, question number:14
^ de Bold A (1985). "Atrial natriuretic factor: a hormone produced by the heart". Science 230 (4727): 767–70. doi:10.1126/science.2932797. PMID 2932797.
^ Kokkonen, Ulla-Maija (2002). Plasma Atrial Natriuretic peptides in the horse and goat with special reference to exercising horses.
^ http://www.biolreprod.org/content/54/4/834.full.pdf
^ Mohler ER, Finkbeiner WE (2011). Medical Physiology (Boron) (2 ed.). Philadelphia: Saunders. ISBN 1-4377-1753-5.
^ Mäkikallio, Kaarin (2002). "ANP". Placental insufficiency and fetal heart: Doppler ultrasonographic and biochemical markers of fetal cardiac dysfunction. Oulu: Oulun yliopisto. ISBN 951-42-6737-0. OCLC 58358685.
^ Kiberd BA, Larson TS, Robertson CR, Jamison RL (June 1987). "Effect of atrial natriuretic peptide on vasa recta blood flow in the rat". Am. J. Physiol. 252 (6 Pt 2): F1112–7. PMID 2954471.
^ Reeves WB, Andreoli TE (2008). "Chapter 31 – Sodium Chloride Transport in the Loop of Henle, Distal Convoluted Tubule, and Collecting Duct". In Giebisch GH, Alpern RA, Herbert SC, Seldin, DW. Seldin and Giebisch's the kidney: physiology and pathophysiology. Amsterdam: Elsevier/Academic Press. doi:10.1016/B978-012088488-9.50034-6. ISBN 0-12-088488-7.
^ Kong X, Wang X, Hellermann G, Lockey RF, Mohapatra S (2007). "Mice Deficient in Atrial Natriuretic Peptide Receptor A (NPRA) Exhibit Decreased Lung Inflammation: Implication of NPRA Signaling in As`thma Pathogenesis". The Journal of Allergy and Clinical Immunology 119 (1): S127. doi:10.1016/j.jaci.2006.11.482.
^ Röcken C, Peters B, Juenemann G, et al. (October 2002). "Atrial amyloidosis: an arrhythmogenic substrate for persistent atrial fibrillation". Circulation 106 (16): 2091–7. doi:10.1161/01.CIR.0000034511.06350.DF. PMID 12379579.
^ Tervonen V, Arjamaa O, Kokkonen K, Ruskoaho H, Vuolteenaho O (September 1998). "A novel cardiac hormone related to A-, B- and C-type natriuretic peptides". Endocrinology 139 (9): 4021–5. doi:10.1210/en.139.9.4021. PMID 9724061.
^ Schweitz H, Vigne P, Moinier D, Frelin C, Lazdunski M (July 1992). "A new member of the natriuretic peptide family is present in the venom of the green mamba (Dendroaspis angusticeps)". J Biol Chem. 267 (20): 13928–32. PMID 1352773.
^ Venugopal J (2003). "Pharmacological modulation of the natriuretic peptide system". Expert Opinion on Therapeutic Patents 13 (9): 1389. doi:10.1517/13543776.13.9.1389.

External links

Atrial Natriuretic Factor at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

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1. Chapter 6D：ナトリウム利尿ペプチド chapter 6d natriuretic peptides
2. 心不全におけるナトリウム利尿ペプチド測定 natriuretic peptide measurement in heart failure
3. 非心不全下におけるナトリウム利尿ペプチド測定 natriuretic peptide measurement in non heart failure settings
4. 心不全の病態生理：神経体液性の適応 pathophysiology of heart failure neurohumoral adaptations
5. 虚血後（虚血性）の急性尿細管壊死において考え得る予防および治療 possible prevention and therapy of postischemic ischemic acute tubular necrosis

English Journal

Cardiac-specific Traf2 overexpression enhances cardiac hypertrophy through activating AKT/GSK3β signaling.

Huang Y1, Wu D2, Zhang X1, Jiang M1, Hu C3, Lin J1, Tang J1, Wu L4.Author information 1Department of Cardiology, The Second Affiliated Hospital of Wenzhou Medical University, 109 Xueyuan Road, Wenzhou 25035, Zhejiang, China.2Medical College of Zhejiang University City College, 51 Huzhou Road, Hangzhou 310000, China.3Department of Cardiology, The Tongji Hospital of Tongji University, 309 Xincun Road, Putuo District, Shanghai 200065, China.4Department of Cardiology, The Second Affiliated Hospital of Wenzhou Medical University, 109 Xueyuan Road, Wenzhou 25035, Zhejiang, China. Electronic address: wulianpin@gmail.com.AbstractTumor necrosis factor superfamily ligands provoke a dilated cardiac phenotype signal through a common scaffolding protein termed tumor necrosis factor receptor-associated factor 2 (Traf2); however, Traf2 signaling in the adult mammalian cardiac hypertrophy is not fully understood. This study was aimed to identify the effect of Traf2 on cardiac hypertrophy and the underlying mechanisms. A significant up-regulation of Traf2 expression was observed in mice failing hearts. To further investigate the role of Traf2 in cardiac hypertrophy, we used cultured neonatal rat cardiomyocytes with gain and loss of Traf2 function and cardiac-specific Traf2-overexpressing transgenic (TG) mice. In cultured cardiomyocytes, Traf2 positively regulated angiotensin II (Ang II)-mediated hypertrophic growth, as detected by [(3)H]-Leucine incorporation, cardiac myocyte area, and hypertrophic marker protein levels. Cardiac hypertrophy in vivo was produced by constriction of transverse aortic (TAC) in TG mice and their wild-type controls. The extent of cardiac hypertrophy was evaluated by echocardiography as well as by pathological and molecular analyses of heart samples. Traf2 overexpression in the heart remarkably enhanced cardiac hypertrophy, left ventricular dysfunction in mice in response to TAC. Further analysis of the signaling pathway in vitro and in vivo suggested that these adverse effects of Traf2 were associated with the activation of AKT/glycogen synthase kinase 3β (GSK3β). The present study demonstrates that Traf2 serves as a novel mediator that enhanced cardiac hypertrophy by activating AKT/GSK3β signaling.
Gene.Gene.2014 Feb 25;536(2):225-31. doi: 10.1016/j.gene.2013.12.052. Epub 2013 Dec 27.
Tumor necrosis factor superfamily ligands provoke a dilated cardiac phenotype signal through a common scaffolding protein termed tumor necrosis factor receptor-associated factor 2 (Traf2); however, Traf2 signaling in the adult mammalian cardiac hypertrophy is not fully understood. This study was aim
PMID 24378234

COX-2 is involved in ET-1-induced hypertrophy of neonatal rat cardiomyocytes: Role of NFATc3.

Li H1, Gao S1, Ye J1, Feng X1, Cai Y2, Liu Z1, Lu J1, Li Q1, Huang X1, Chen S3, Liu P4.Author information 1Department of Pharmacology and Toxicology, School of Pharmaceutical Sciences, Sun Yat-sen University, Higher Education Mega Center, Guangzhou 510006, Guangdong, PR China.2Guangzhou Research Institute of Snake Venom, Guangzhou Medical College, Guangzhou 510182, Guangdong, PR China.3Department of Pharmacology and Toxicology, School of Pharmaceutical Sciences, Sun Yat-sen University, Higher Education Mega Center, Guangzhou 510006, Guangdong, PR China. Electronic address: chshaor@mail.sysu.edu.cn.4Department of Pharmacology and Toxicology, School of Pharmaceutical Sciences, Sun Yat-sen University, Higher Education Mega Center, Guangzhou 510006, Guangdong, PR China. Electronic address: liupq@mail.sysu.edu.cn.AbstractEndothelin-1 (ET-1) is a critical molecule that involved in heart failure. It has been proved that ET-1 stimulation results in cardiac hypertrophy both in vitro and in vivo, but the mechanisms underlying remain largely unknown. In this study, we reported that cyclooxygenase-2 (COX-2) might be an important mediator of hypertrophic responses to ET-1 stimulation. In the cultured rat neonatal cardiomyocytes, ET-1 significantly upregulated the expression and activity of COX-2, which was accompanied by increase in cell surface area and BNP mRNA level. In contrast, ET-1-dependent cardiomyocyte hypertrophy was abolished by COX-2 selective inhibitors, NS-398 and celecoxib, or by COX-2 RNA interference, but the inhibitory effects could be diminished by pretreatment with PGE2. Furthermore, cyclosporin A (CsA) and knockdown of nuclear factor of activated T-cells c3 (NFATc3) inhibited the expression of COX-2 induced by ET-1, and NFATc3 could also bound to the -GGAAA- sequence in the promoter region of rat COX-2 gene, indicating that calcineurin/NFATc3 signaling participated in the transcriptional regulation of COX-2 following ET-1 treatment. These findings provided further insight into the roles of ET-1 in cardiac hypertrophy and suggested a potential therapeutic strategy against cardiac hypertrophy by inhibiting COX-2.
Molecular and cellular endocrinology.Mol Cell Endocrinol.2014 Feb 15;382(2):998-1006. doi: 10.1016/j.mce.2013.11.012. Epub 2013 Nov 26.
Endothelin-1 (ET-1) is a critical molecule that involved in heart failure. It has been proved that ET-1 stimulation results in cardiac hypertrophy both in vitro and in vivo, but the mechanisms underlying remain largely unknown. In this study, we reported that cyclooxygenase-2 (COX-2) might be an imp
PMID 24291639

Usefulness of a combination of monocyte chemoattractant protein-1, galectin-3, and N-terminal probrain natriuretic Peptide to predict cardiovascular events in patients with coronary artery disease.

Tuñón J1, Blanco-Colio L2, Cristóbal C3, Tarín N4, Higueras J5, Huelmos A6, Alonso J3, Egido J7, Asensio D8, Lorenzo O9, Mahíllo-Fernández I10, Rodríguez-Artalejo F11, Farré J12, Martín-Ventura JL9, López-Bescós L13.Author information 1Department of Cardiology, IIS-Fundación Jiménez Díaz, Madrid, Spain; Autónoma University, Madrid, Spain; Laboratory of Vascular Pathology, Instituto de Investigación Sanitaria-Fundación Jiménez Díaz, Madrid, Spain. Electronic address: jtunon@secardiologia.es.2Laboratory of Vascular Pathology, Instituto de Investigación Sanitaria-Fundación Jiménez Díaz, Madrid, Spain.3Department of Cardiology, Hospital de Fuenlabrada, Madrid, Spain; Rey Juan Carlos University, Alcorcón, Madrid, Spain.4Department of Cardiology, Hospital Universitario de Móstoles, Madrid, Spain.5Department of Cardiology, Hospital Clínico Universitario San Carlos, Madrid, Spain.6Department of Cardiology, Hospital Universitario Fundación Alcorcón, Madrid, Spain.7Autónoma University, Madrid, Spain; Laboratory of Vascular Pathology, Instituto de Investigación Sanitaria-Fundación Jiménez Díaz, Madrid, Spain; Centro de Investigación Biomédica en Red de Diabetes y Enfermedades Metabólicas Asociadas, Madrid, Spain.8Department of Biochemistry, IIS-Fundación Jiménez Díaz, Madrid, Spain.9Autónoma University, Madrid, Spain; Laboratory of Vascular Pathology, Instituto de Investigación Sanitaria-Fundación Jiménez Díaz, Madrid, Spain.10Department of Preventive Medicine, IIS-Fundación Jiménez Díaz, Madrid, Spain.11Department of Preventive Medicine and Public Health, School of Medicine, Autónoma University, Madrid, Spain.12Department of Cardiology, IIS-Fundación Jiménez Díaz, Madrid, Spain; Autónoma University, Madrid, Spain.13Rey Juan Carlos University, Alcorcón, Madrid, Spain.AbstractPatients with coronary artery disease may develop not only ischemic events but also heart failure and death due to previous myocardial damage. The purpose of this study was to test the prognostic value of a panel of plasma biomarkers related to vascular (monocyte chemoattractant protein-1 [MCP-1] and soluble tumor necrosis factor-like weak inducer of apoptosis) and myocardial damage (galectin-3, N-terminal fragment of brain natriuretic peptide [NT-proBNP], and neutrophil gelatinase-associated lipocalin) in 706 patients with chronic coronary artery disease followed for 2.2 ± 0.99 years. Secondary outcomes were the incidence of acute ischemic events (ST elevation myocardial infarction, non-ST elevation acute coronary syndrome, stroke, or transient ischemic attack) and death or heart failure. The primary outcome was the combination of the secondary outcomes. Cox proportional hazards model was used for analysis. Fifty-three patients developed acute ischemic events. Increasing MCP-1 plasma levels (p = 0.002), age, and body mass index predicted this outcome independently. Thirty-three patients developed death and/or heart failure. Galectin-3 (p = 0.007), NT-proBNP plasma levels (p = 0.004), hypertension, glomerular filtration rate, and the use of nitrates and anticoagulants were associated with this outcome independently. The development of the primary outcome was predicted independently by MCP-1 (p <0.001), NT-proBNP (p = 0.005), and galectin-3 (p = 0.019); hypertension; atrial fibrillation; and treatment with nitrates. Every biomarker with a value above the median increased the risk of developing this outcome by 1.832 (95% confidence interval 1.356 to 2.474, p <0.001). High-sensitivity C-reactive protein and lipid levels were not associated with any outcome. In conclusion, increasing MCP-1, galectin-3, and NT-proBNP plasma levels are associated with a greater incidence of cardiovascular events.
The American journal of cardiology.Am J Cardiol.2014 Feb 1;113(3):434-40. doi: 10.1016/j.amjcard.2013.10.012. Epub 2013 Nov 7.
Patients with coronary artery disease may develop not only ischemic events but also heart failure and death due to previous myocardial damage. The purpose of this study was to test the prognostic value of a panel of plasma biomarkers related to vascular (monocyte chemoattractant protein-1 [MCP-1] an
PMID 24295549

Japanese Journal

'A Single Night' Beneficial Effects of Adaptive Servo-Ventilation on Cardiac Overload, Sympathetic Nervous Activity, and Myocardial Damage in Patients With Chronic Heart Failure and Sleep-Disordered Breathing

YOSHIHISA Akiomi,SUZUKI Satoshi,MIYATA Makiko,YAMAKI Takayoshi,SUGIMOTO Koichi,KUNII Hiroyuki,NAKAZATO Kazuhiko,SUZUKI Hitoshi,SAITOH Shu-ichi,TAKEISHI Yasuchika
Circulation journal : official journal of the Japanese Circulation Society 76(9), 2153-2158, 2012-08-25
… We performed polysomnography (baseline, O2, and ASV) for 3 consecutive days, and we measured levels of atrial natriuretic peptide (ANP), B-type natriuretic peptide (BNP), noradrenalin, urinary catecholamines, and high-sensitivity troponin T. …
NAID 10030696593

高ナトリウム血症にヒト心房性ナトリウム利尿ペプチドが有効であった1症例

木村太,工藤隆司,石原弘規
麻酔 61(6), 634-637, 2012-06
NAID 40019341958

Related Pictures

★リンクテーブル★

リンク元	「心房性ナトリウム利尿ペプチド」「ANP」「urodilatin」
拡張検索	「atrial natriuretic peptide receptor」
関連記事	「atrial」「natriuretic」「atrial natriuretic」「natriuretic peptide」

「心房性ナトリウム利尿ペプチド」

Natriuretic peptide A
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1ANP, 1YK0, 3N57
Identifiers
Symbols	NPPA ; ANF; ANP; ATFB6; CDD-ANF; PND
External IDs	OMIM: 108780 MGI: 97367 HomoloGene: 4498 ChEMBL: 1293193 GeneCards: NPPA Gene
Gene ontology
Molecular function	• receptor binding; • hormone activity; • peptide hormone receptor binding;
Cellular component	• extracellular region; • extracellular space; • nucleus; • mast cell granule; • perinuclear region of cytoplasm;
Biological process	• cGMP biosynthetic process; • transcription initiation from RNA polymerase II promoter; • receptor guanylyl cyclase signaling pathway; • female pregnancy; • regulation of blood pressure; • gene expression; • cardiac muscle hypertrophy in response to stress; • negative regulation of cell growth; • response to insulin stimulus; • regulation of blood vessel size;
	Sources: Amigo / QuickGO
Orthologs
	This box: view; talk; edit;

　　[★]

英: atrial natriuretic peptide, ANP (SP)
同: 心房性Na利尿ペプチド、心房性利尿ペプチド、心房性ナトリウム利尿因子 atrial natriuretic factor ANF、心房性ナトリウム利尿ホルモン atrial natriuretic hormone ANH
関: カルペリチド、ナトリウム利尿ペプチド

[show details]

ヒト心房性ナトリウム利尿ポリペプチド : 66 件
ヒト心房性ナトリウム利尿ペプチド : 約 58,100 件
心房性ナトリウム利尿ポリペプチド : 71 件
心房性ナトリウム利尿ペプチド : 約 25,900 件

アルドステロン・レニン-アンジオテンシン、プロスタグランジンE2、カリクレイン-キニンと共に体液調節に関わる

分類

性状

ペプチド
28 a.a.

産生組織

心房筋　(→心室で産生されるものはBNP

標的組織

血管平滑筋
腎臓

糸球体
直血管
髄質集合管

受容体

作用

血管平滑筋　→　弛緩
腎臓　→　Na排泄の上昇

GFRの増加、腎髄質血流の増加、尿細管のNa輸送の抑制

バソプレシン作用の抑制 (SP.793)

分泌の調整

心房の伸展　←　循環血液量の増加

分子機構

受容体に結合した後、膜結合型のグアニル酸シクラーゼを活性化し、cGMPがセカンドメッセンジャーとして機能

臨床関連

心不全の治療薬として使われる　→　カルペリチド

「ANP」

　　[★] 心房性ナトリウム利尿ペプチド atrial natriuretic peptide

「urodilatin」

　　[★]

関: atrial natriuretic peptide

関: atrial natriuretic peptide

「atrial natriuretic peptide receptor」

　　[★]

心房性ナトリウム利尿ペプチド受容体、心房性ナトリウム利尿ペプチドレセプター

関: ANP receptor

「atrial」

　　[★]

adj.

心房性の、心房の

関: atria、atrium、heart atria、heart atrium

「natriuretic」

　　[★]

ナトリウム利尿の、ナトリウム排泄増加の

関: natriuresis

「atrial natriuretic」

　　[★]

心房性ナトリウム利尿の

「natriuretic peptide」

　　[★]

ナトリウム利尿ペプチド

[Widmaier-1] Widmaier, Eric P.; Hershel Raff; Kevin T. Strang (2008). Vander's Human Physiology, 11th Ed. McGraw-Hill. pp. 291, 509–10. ISBN 978-0-07-304962-5.

[pmid19089336-2] Potter LR, Yoder AR, Flora DR, Antos LK, Dickey DM (2009). "Natriuretic peptides: their structures, receptors, physiologic functions and therapeutic applications". Handb Exp Pharmacol. Handbook of Experimental Pharmacology 191 (191): 341–66. doi:10.1007/978-3-540-68964-5_15. ISBN 978-3-540-68960-7. PMID 19089336.

[isbn0-387-51409-0-3] Addicks K, Forssmann WG, Henkel H, Holthausen U, Menz V, Rippegather G, Ziskoven D (1989). "Calcium-calmodulin antagonists Influences the release of cardiodilatin/ANP from atrial cardiocytes". In Wambach G, Kaufmann W. Endocrinology of the heart. Berlin: Springer-Verlag. ISBN 0-387-51409-0.

[4] Marieb Human Anatomy & Physiology 9th edition, chapter:16, page:629, question number:14

[5] Bold A (1985). "Atrial natriuretic factor: a hormone produced by the heart". Science 230 (4727): 767–70. doi:10.1126/science.2932797. PMID 2932797.

[6] Kokkonen, Ulla-Maija (2002). Plasma Atrial Natriuretic peptides in the horse and goat with special reference to exercising horses.

[7] ttp://www.biolreprod.org/content/54/4/834.full.pdf

[isbn1-4377-1753-5-8] Mohler ER, Finkbeiner WE (2011). Medical Physiology (Boron) (2 ed.). Philadelphia: Saunders. ISBN 1-4377-1753-5.

[9] Mäkikallio, Kaarin (2002). "ANP". Placental insufficiency and fetal heart: Doppler ultrasonographic and biochemical markers of fetal cardiac dysfunction. Oulu: Oulun yliopisto. ISBN 951-42-6737-0. OCLC 58358685.

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atrial natriuretic peptide