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词条 Apelin
释义

  1. Discovery

  2. Biosynthesis

  3. Physiological functions

      Vascular    Cardiac    Exercise    Brain   Adipose tissue   Digestive    Bone    Muscle aging  

  4. References

  5. Further reading

  6. External links

{{Infobox_gene}}

Apelin (also known as APLN) is a peptide that in humans is encoded by the APLN gene.[1] Apelin is the endogenous ligand for the G-protein-coupled APJ receptor[2][3][4][5][6] that is expressed at the surface of some cell types.[7] It is widely expressed in various organs such as the heart, lung, kidney, liver, adipose tissue, gastrointestinal tract, brain, adrenal glands, endothelium, and human plasma.

Discovery

Apelin is a peptide that was identified in 1998 by Professor M. Fujino’s team.[1]

Biosynthesis

Apelin gene encodes a pre-proprotein of 77 amino acids,[1] with a signal peptide in the N-terminal region. After translocation into the endoplasmic reticulum and cleavage of the signal peptide, the proprotein of 55 amino acids may generate several active fragments: a 36 amino acid peptide corresponding to the sequence 42-77 (apelin 36), a 17 amino acid peptide corresponding to the sequence 61-77 (apelin 17) and a 13 amino acid peptide corresponding to the sequence 65-77 (apelin 13). This latter fragment may also undergo a pyroglutamylation at the level of its N-terminal glutamine residue. However the presence and/or the concentrations of those peptides in human plasma has been questioned.[8] Recently, 46 different apelin peptides ranging from apelin 55 (proapelin) to apelin 12 have been identified in bovine colostrum, including C-ter truncated isoforms.[9]

Physiological functions

The sites of receptor expression are clearly linked to the different functions played by apelin in the organism.

Vascular

Vascular expression of the receptor[10][11] participates in the control of blood pressure[2] and its activation promotes the formation of new blood vessels (angiogenesis).[11][12][13][14] The hypotensive effect of apelin results from the activation of receptors expressed at the surface of endothelial cells.[10][11] This activation induces the release of NO,[15] a potent vasodilator, which induces relaxation of the smooth muscle cells of artery wall. Studies performed on mice knocked out for the apelin receptor gene[16] have suggested the existence of a balance between angiotensin II signalling, which increases blood pressure and apelin signalling, which lowers blood pressure. The angiogenic activity is the consequence of apelin action on the proliferation and migration of the endothelial cells. Apelin activates inside the cell transduction cascades (ERKs, Akt, and p70S6kinase phosphorylation),[12][17] which lead to the proliferation of endothelial cells and the formation of new blood vessels.[13] Knockout of the apelin gene is associated with a delay in the development of the retinal vasculature.[18]

Cardiac

The apelin receptor is expressed early during the embryonic development of the heart, where it regulates the migration of cell progenitors fated to differentiate into cardiomyocytes, the contractile cells of the heart.[19][20] Its expression is also detected in the cardiomyocytes of the adult where apelin behaves as one of the most potent stimulator of cardiac contractility.[3][21][22] Aged apelin knockout mice develop progressive impairment of cardiac contractility.[23] Apelin acts as a mediator of the cardiovascular control, including for blood pressure and blood flow. It is one of the most potent stimulators of cardiac contractility yet identified, and plays a role in cardiac tissue remodeling. Apelin levels are increased in left ventricles of patients with chronic heart failure and also in patients with chronic liver disease.[24]

Exercise

The plasma concentration of apelin is shown to increase during exercise.[25]. Paradoxically,exogenous apelin in healthy volunteers reduced peak VO2 in an endurance test.[26]

Brain

Apelin receptor is also expressed in the neurons of brain areas involved in regulating water and food intake.[2][27][28] Apelin injection increases water intake[2] and apelin decreases the hypothalamic secretion of the antidiuretic hormone vasopressin.[29] This diuretic effect of apelin in association with its hypotensive effect participates in the homeostatic regulation of body fluid. Apelin is also detected in brain areas which control appetite, but its effects on food intake are very contradictory.[30][31][32]

Adipose tissue

Apelin is expressed and secreted by adipocytes, and its production is increased during adipocyte differentiation and is stimulated by insulin.[33] Most obese people have elevated levels of insulin, which may therefore be the reason why obese people have been reported to also have elevated levels of apelin.[33]

Digestive

Apelin receptor is expressed in several cell types of the gastro-intestinal tract : stomach enterochromaffine-like cells;[34][35] unknown cells of endocrine pancreas,[36] colon epithelial cells.[37]

In stomach, activation of receptors on enterochromaffine-like cells by apelin secreted by parietal cells can inhibit histamine release by enterochromaffine-like cells, which in turn decreases acid secretion by parietal cells.[35] In pancreas, apelin inhibits the insulin secretion induced by glucose.[38] This inhibition reveals the functional interdependency between apelin signalling and insulin signalling observed at the adipocyte level where insulin stimulate apelin production.[33] Recently, receptor expression was also detected in skeletic muscle cells. Its activation is involved in glucose uptake and participates in the control of glucose blood levels glycemia.[39]

Bone

Receptor expression is also observed at the surface of osteoblasts, the cell progenitors involved in bone formation.[40]

Muscle aging

Muscle apelin expression decreases with age in rodents and humans[41]. By supplementing aged mice with exogenous apelin, the team of Dr C. Dray shown that the peptide was able to promote muscle hypertrophy and consequently induced a gain in strength[41]. This study also demonstrated that apelin targets muscle cells during aging by different and complementary pathways: it acts on muscle metabolism by activating an AMPK-dependent mitochondria biogenesis, it promotes autophagy and decreases inflammation in aged mice[41]. Moreover, apelin receptor is also present on muscle stem cells and promotes in vitro and in vivo proliferation and differenciation of these cells into mature muscle cells participating to muscle regeneration. Finally, muscle apelin could be used a biomarker of physical exercise success in aged individual since its production is corelated to the benefit of a chronic physical exercise in aged individuals[41].

References

1. ^1 2 {{cite journal |vauthors=Tatemoto K, Hosoya M, Habata Y, Fujii R, Kakegawa T, Zou MX, Kawamata Y, Fukusumi S, Hinuma S, Kitada C, Kurokawa T, Onda H, Fujino M | title = Isolation and characterization of a novel endogenous peptide ligand for the human APJ receptor | journal = Biochem. Biophys. Res. Commun. | volume = 251 | issue = 2 | pages = 471–6 | year = 1998 | pmid = 9792798 | doi = 10.1006/bbrc.1998.9489 }}
2. ^1 2 3 {{cite journal |vauthors=Lee DK, Cheng R, Nguyen T, Fan T, Kariyawasam AP, Liu Y, Osmond DH, George SR, O'Dowd BF | title = Characterization of apelin, the ligand for the APJ receptor | journal = J. Neurochem. | volume = 74 | issue = 1 | pages = 34–41 | year = 2000 | pmid = 10617103 | doi = 10.1046/j.1471-4159.2000.0740034.x }}
3. ^1 {{cite journal |vauthors=Szokodi I, Tavi P, Földes G, Voutilainen-Myllylä S, Ilves M, Tokola H, Pikkarainen S, Piuhola J, Rysä J, Tóth M, Ruskoaho H | title = Apelin, the novel endogenous ligand of the orphan receptor APJ, regulates cardiac contractility | journal = Circ. Res. | volume = 91 | issue = 5 |pages = 434–40 | year = 2002 | pmid = 12215493 | doi = 10.1161/01.RES.0000033522.37861.69}}
4. ^{{cite journal |vauthors=Kleinz MJ, Davenport AP | title = Emerging roles of apelin in biology and medicine | journal = Pharmacol. Ther. | volume = 107 | issue = 2 |pages = 198–211 | year = 2005 | pmid = 15907343 | doi = 10.1016/j.pharmthera.2005.04.001 }}
5. ^{{cite journal |vauthors=O'Dowd BF, Heiber M, Chan A, Heng HH, Tsui LC, Kennedy JL, Shi X, Petronis A, George SR, Nguyen T | title = A human gene that shows identity with the gene encoding the angiotensin receptor is located on chromosome 11 | journal = Gene | volume = 136 | issue = 1–2 | pages = 355–60 |date=December 1993 | pmid = 8294032 | doi = 10.1016/0378-1119(93)90495-O| url = }}
6. ^{{cite journal |vauthors=Devic E, Paquereau L, Vernier P, Knibiehler B, Audigier Y | title = Expression of a new G protein-coupled receptor X-msr is associated with an endothelial lineage in Xenopus laevis | journal = Mech. Dev. | volume = 59 | issue = 2 | pages = 129–40 |date=October 1996 | pmid = 8951791 | doi = 10.1016/0925-4773(96)00585-0| url = }}
7. ^{{cite journal | author = Audigier Y | title = Apelin Receptor | url = http://www.signaling-gateway.org/molecule/query?afcsid=A000304&mpv=1 | journal = UCSD-Nature Molecule Pages | doi = 10.1038/mp.a000304.01 | date = 2006-04-07| accessdate = 2009-09-02| quote = }}
8. ^{{cite journal |vauthors=Mesmin C, Dubois M, Becher F, Fenaille F, Ezan E | title = Liquid chromatography/tandem mass spectrometry assay for the absolute quantification of the expected circulating apelin peptides in human plasma | journal = Rapid Commun Mass Spectrom | year = 2010 | volume = 24 | issue = 19 | pages = 2875–84 | pmid = 20857448 | doi = 10.1002/rcm.4718 }}
9. ^{{cite journal |vauthors=Mesmin C, Fenaille F, Becher F, Tabet JC, Ezan E | title = Identification and characterization of apelin peptides in bovine colostrum and milk by liquid chromatography-mass spectrometry. | journal = J Proteome Res | year = 2011 | pmid = 21939284 | doi = 10.1021/pr200725x | volume=10 | issue=11 | pages=5222–31}}
10. ^1 {{cite journal |vauthors=Devic E, Rizzoti K, Bodin S, Knibiehler B, Audigier Y | title = Amino acid sequence and embryonic expression of msr/apj, the mouse homolog of Xenopus X-msr and human APJ | journal = Mech. Dev. | volume = 84 | issue = 1–2 | pages = 199–203 |date=June 1999 | pmid = 10473142 | doi = 10.1016/S0925-4773(99)00081-7| url = }}
11. ^1 2 {{cite journal |vauthors=Saint-Geniez M, Masri B, Malecaze F, Knibiehler B, Audigier Y | title = Expression of the murine msr/apj receptor and its ligand apelin is upregulated during formation of the retinal vessels | journal = Mech. Dev. | volume = 110 | issue = 1–2 | pages = 183–6 |date=January 2002 | pmid = 11744380 | doi = 10.1016/S0925-4773(01)00558-5| url = }}
12. ^1 {{cite journal |vauthors=Masri B, Morin N, Cornu M, Knibiehler B, Audigier Y | title = Apelin (65-77) activates p70 S6 kinase and is mitogenic for umbilical endothelial cells | journal = FASEB J. | volume = 18 | issue = 15 | pages = 1909–11 |date=December 2004 | pmid = 15385434 | doi = 10.1096/fj.04-1930fje | url = }}
13. ^1 {{cite journal |vauthors=Kasai A, Shintani N, Oda M, Kakuda M, Hashimoto H, Matsuda T, Hinuma S, Baba A | title = Apelin is a novel angiogenic factor in retinal endothelial cells | journal = Biochem. Biophys. Res. Commun. | volume = 325 | issue = 2 | pages = 395–400 |date=December 2004 | pmid = 15530405 | doi = 10.1016/j.bbrc.2004.10.042 | url = }}
14. ^{{cite journal |vauthors=Cox CM, D'Agostino SL, Miller MK, Heimark RL, Krieg PA | title = Apelin, the ligand for the endothelial G-protein-coupled receptor, APJ, is a potent angiogenic factor required for normal vascular development of the frog embryo | journal = Dev. Biol. | volume = 296 | issue = 1 | pages = 177–89 |date=August 2006 | pmid = 16750822 | doi = 10.1016/j.ydbio.2006.04.452 | url = }}
15. ^{{cite journal |vauthors=Tatemoto K, Takayama K, Zou MX, Kumaki I, Zhang W, Kumano K, Fujimiya M | title = The novel peptide apelin lowers blood pressure via a nitric oxide-dependent mechanism | journal = Regul. Pept. | volume = 99 | issue = 2–3 | pages = 87–92 |date=June 2001 | pmid = 11384769 | doi = 10.1016/S0167-0115(01)00236-1| url = }}
16. ^{{cite journal |vauthors=Ishida J, Hashimoto T, Hashimoto Y, Nishiwaki S, Iguchi T, Harada S, Sugaya T, Matsuzaki H, Yamamoto R, Shiota N, Okunishi H, Kihara M, Umemura S, Sugiyama F, Yagami K, Kasuya Y, Mochizuki N, Fukamizu A | title = Regulatory roles for APJ, a seven-transmembrane receptor related to angiotensin-type 1 receptor in blood pressure in vivo | journal = J. Biol. Chem. | volume = 279 | issue = 25 | pages = 26274–9 |date=June 2004 | pmid = 15087458 | doi = 10.1074/jbc.M404149200 | url = }}
17. ^{{cite journal |vauthors=Masri B, Lahlou H, Mazarguil H, Knibiehler B, Audigier Y | title = Apelin (65-77) activates extracellular signal-regulated kinases via a PTX-sensitive G protein | journal = Biochem. Biophys. Res. Commun. | volume = 290 | issue = 1 | pages = 539–45 |date=January 2002 | pmid = 11779205 | doi = 10.1006/bbrc.2001.6230 | url = }}
18. ^{{cite journal |vauthors=Kasai A, Shintani N, Kato H, Matsuda S, Gomi F, Haba R, Hashimoto H, Kakuda M, Tano Y, Baba A | title = Retardation of retinal vascular development in apelin-deficient mice | journal = Arterioscler. Thromb. Vasc. Biol. | volume = 28 | issue = 10 | pages = 1717–22 |date=October 2008 | pmid = 18599802 | doi = 10.1161/ATVBAHA.108.163402 | url = }}
19. ^{{cite journal |vauthors=Scott IC, Masri B, D'Amico LA, Jin SW, Jungblut B, Wehman AM, Baier H, Audigier Y, Stainier DY | title = The g protein-coupled receptor agtrl1b regulates early development of myocardial progenitors | journal = Dev. Cell | volume = 12 | issue = 3 | pages = 403–13 |date=March 2007 | pmid = 17336906 | doi = 10.1016/j.devcel.2007.01.012 | url = }}
20. ^{{cite journal |vauthors=Zeng XX, Wilm TP, Sepich DS, Solnica-Krezel L | title = Apelin and its receptor control heart field formation during zebrafish gastrulation | journal = Dev. Cell | volume = 12 | issue = 3 | pages = 391–402 |date=March 2007 | pmid = 17336905 | doi = 10.1016/j.devcel.2007.01.011 | url = }}
21. ^{{cite journal |vauthors=Berry MF, Pirolli TJ, Jayasankar V, Burdick J, Morine KJ, Gardner TJ, Woo YJ | title = Apelin has in vivo inotropic effects on normal and failing hearts | journal = Circulation | volume = 110 | issue = 11 Suppl 1 | pages = II187–93 |date=September 2004 | pmid = 15364861 | doi = 10.1161/01.CIR.0000138382.57325.5c | url = }}
22. ^{{cite journal |vauthors=Ashley EA, Powers J, Chen M, Kundu R, Finsterbach T, Caffarelli A, Deng A, Eichhorn J, Mahajan R, Agrawal R, Greve J, Robbins R, Patterson AJ, Bernstein D, Quertermous T | title = The endogenous peptide apelin potently improves cardiac contractility and reduces cardiac loading in vivo | journal = Cardiovasc. Res. | volume = 65 | issue = 1 | pages = 73–82 |date=January 2005 | pmid = 15621035 | pmc = 2517138 | doi = 10.1016/j.cardiores.2004.08.018 | url = }}
23. ^{{cite journal |vauthors=Kuba K, Zhang L, Imai Y, Arab S, Chen M, Maekawa Y, Leschnik M, Leibbrandt A, Markovic M, Makovic M, Schwaighofer J, Beetz N, Musialek R, Neely GG, Komnenovic V, Kolm U, Metzler B, Ricci R, Hara H, Meixner A, Nghiem M, Chen X, Dawood F, Wong KM, Sarao R, Cukerman E, Kimura A, Hein L, Thalhammer J, Liu PP, Penninger JM | title = Impaired heart contractility in Apelin gene-deficient mice associated with aging and pressure overload | journal = Circ. Res. | volume = 101 | issue = 4 | pages = e32–42 |date=August 2007 | pmid = 17673668 | doi = 10.1161/CIRCRESAHA.107.158659 | url = }}
24. ^{{cite journal |vauthors=Principe A, Melgar-Lesmes P, Fernández-Varo G, Del Arbol LR, Ros J, Morales-Ruiz M, Bernardi M, Arroyo V, Jiménez W | title = The hepatic apelin system: A new therapeutic target for liver disease | journal = Hepatology | volume = 48 | issue = 4 | pages = 1193–1201 | year = 2008 | pmid = 18816630 | doi = 10.1002/hep.22467 }}
25. ^{{cite journal |vauthors=Kechyn S,Barnes G, Howard L| title = Assessing dynamic changes in plasma apelin concentration in response to maximal exercise in man | journal = European Respiratory Journal |year=2015 |volume=46 |page=PA2316 | doi = 10.1183/13993003.congress-2015.PA2316}}
26. ^{{cite journal |last1=Kechyn |first1=Svyatoslav |last2=Barnes |first2=Gareth |last3=Thongmee |first3=Akaphot |last4=Howard |first4=Luke |title=Effect of apelin on cardiopulmonary performance during endurance exercise |journal=European Respiratory Journal |date=September 2015 |issue=46 suppl 59 |pages=2241 |doi=10.1183/13993003.congress-2015.PA2241}}
27. ^{{cite journal |vauthors=O'Carroll AM, Selby TL, Palkovits M, Lolait SJ | title = Distribution of mRNA encoding B78/apj, the rat homologue of the human APJ receptor, and its endogenous ligand apelin in brain and peripheral tissues | journal = Biochim. Biophys. Acta | volume = 1492 | issue = 1 | pages = 72–80 |date=June 2000 | pmid = 11004481 | doi = 10.1016/S0167-4781(00)00072-5| url = }}
28. ^De Mota et al., 2000
29. ^{{cite journal |vauthors=De Mota N, Lenkei Z, Llorens-Cortès C | title = Cloning, pharmacological characterization and brain distribution of the rat apelin receptor | journal = Neuroendocrinology | volume = 72 | issue = 6 | pages = 400–7 |date=December 2000 | pmid = 11146423 | doi = 10.1159/000054609| url = }}
30. ^{{cite journal |vauthors=Taheri S, Murphy K, Cohen M, Sujkovic E, Kennedy A, Dhillo W, Dakin C, Sajedi A, Ghatei M, Bloom S | title = The effects of centrally administered apelin-13 on food intake, water intake and pituitary hormone release in rats | journal = Biochem. Biophys. Res. Commun. | volume = 291 | issue = 5 | pages = 1208–12 |date=March 2002 | pmid = 11883945 | doi = 10.1006/bbrc.2002.6575 | url = }}
31. ^{{cite journal |vauthors=Sunter D, Hewson AK, Dickson SL | title = Intracerebroventricular injection of apelin-13 reduces food intake in the rat | journal = Neurosci. Lett. | volume = 353 | issue = 1 | pages = 1–4 |date=December 2003 | pmid = 14642423 | doi = 10.1016/S0304-3940(03)00351-3| url = }}
32. ^{{cite journal |vauthors=O'Shea M, Hansen MJ, Tatemoto K, Morris MJ | title = Inhibitory effect of apelin-12 on nocturnal food intake in the rat | journal = Nutr Neurosci | volume = 6 | issue = 3 | pages = 163–7 |date=June 2003 | pmid = 12793520 | doi = 10.1080/1028415031000111273| url = }}
33. ^1 2 {{cite journal|vauthors=Boucher J, Masri B, Daviaud D, Gesta S, Guigné C, Mazzucotelli A, Castan-Laurell I, Tack I, Knibiehler B, Carpéné C, Audigier Y, Saulnier-Blache JS, Valet P|title=Apelin, a newly identified adipokine up-regulated by insulin and obesity|journal=Endocrinology |date=April 2005|volume=146|issue=4|pages=1764–71|doi=10.1210/en.2004-1427|pmid=15677759}}
34. ^{{cite journal |vauthors=Wang G, Anini Y, Wei W, Qi X, OCarroll AM, Mochizuki T, Wang HQ, Hellmich MR, Englander EW, Greeley GH | title = Apelin, a new enteric peptide: localization in the gastrointestinal tract, ontogeny, and stimulation of gastric cell proliferation and of cholecystokinin secretion | journal = Endocrinology | volume = 145 | issue = 3 | pages = 1342–8 |date=March 2004 | pmid = 14670994 | doi = 10.1210/en.2003-1116 | url = }}
35. ^1 {{cite journal |vauthors=Lambrecht NW, Yakubov I, Zer C, Sachs G | title = Transcriptomes of purified gastric ECL and parietal cells: identification of a novel pathway regulating acid secretion | journal = Physiol. Genomics | volume = 25 | issue = 1 | pages = 153–65 |date=March 2006 | pmid = 16403840 | doi = 10.1152/physiolgenomics.00271.2005 | url = }}
36. ^Sorhede Winzell et al., 2005
37. ^{{cite journal |vauthors=Wang G, Kundu R, Han S, Qi X, Englander EW, Quertermous T, Greeley GH | title = Ontogeny of apelin and its receptor in the rodent gastrointestinal tract | journal = Regul. Pept. | volume = 158| issue = 1–3| pages = 32–9|date=August 2009 | pmid = 19660504 | doi = 10.1016/j.regpep.2009.07.016 | url = | pmc = 2761510 }}
38. ^{{cite journal |vauthors=Sörhede Winzell M, Magnusson C, Ahrén B | title = The apj receptor is expressed in pancreatic islets and its ligand, apelin, inhibits insulin secretion in mice | journal = Regul. Pept. | volume = 131 | issue = 1–3 | pages = 12–7 |date=November 2005 | pmid = 15970338 | doi = 10.1016/j.regpep.2005.05.004 | url = }}
39. ^{{cite journal |vauthors=Dray C, Knauf C, Daviaud D, Waget A, Boucher J, Buléon M, Cani PD, Attané C, Guigné C, Carpéné C, Burcelin R, Castan-Laurell I, Valet P | title = Apelin stimulates glucose utilization in normal and obese insulin-resistant mice | journal = Cell Metab. | volume = 8 | issue = 5 | pages = 437–45 |date=November 2008 | pmid = 19046574 | doi = 10.1016/j.cmet.2008.10.003 | url = }}
40. ^{{cite journal |vauthors=Xie H, Tang SY, Cui RR, Huang J, Ren XH, Yuan LQ, Lu Y, Yang M, Zhou HD, Wu XP, Luo XH, Liao EY | title = Apelin and its receptor are expressed in human osteoblasts | journal = Regul. Pept. | volume = 134 | issue = 2–3 | pages = 118–25 |date=May 2006 | pmid = 16563531 | doi = 10.1016/j.regpep.2006.02.004 | url = }}
41. ^1 2 3 {{cite journal |last1=Vinel |first1=Claire |last2=Lukjanenko |first2=Laura |last3=Batut |first3=Aurelie |last4=Deleruyelle |first4=Simon |last5=Pradère |first5=Jean-Philippe |last6=Le Gonidec |first6=Sophie |last7=Dortignac |first7=Allizée |last8=Geoffre |first8=Nancy |last9=Pereira |first9=Ophélie |last10=Karaz |first10=Sonia |last11=Lee |first11=Umi |last12=Camus |first12=Mylène |last13=Chaoui |first13=Karima |last14=Mouisel |first14=Etienne |last15=Bigot |first15=Anne |last16=Mouly |first16=Vincent |last17=Vigneau |first17=Mathieu |last18=Pagano |first18=Allan |last19=Chopard |first19=Angèle |last20=Pillard |first20=Fabien |last21=Guyonnet |first21=Sophie |last22=Cesari |first22=Matteo |last23=Burlet |first23=Odile |last24=Pahor |first24=Marco |last25=Feige |first25=Jerome |last26=Vellas |first26=Bruno |last27=Valet |first27=Philippe |last28=Dray |first28=Cedric |title=The exerkine apelin reverses age-associated sarcopenia. |journal=Nature Medicine |volume=24 |issue=9 |pages=1360–1371 |date=30 July 2018 |doi=10.1038/s41591-018-0131-6 |pmid=30061698 }}

Further reading

{{refbegin | colwidth = 30em}}
  • {{cite journal |vauthors=Lee DK, George SR, O'Dowd BF | title = Unravelling the roles of the apelin system: prospective therapeutic applications in heart failure and obesity | journal = Trends Pharmacol. Sci. | volume = 27 | issue = 4 | pages = 190–4 | year = 2006 | pmid = 16530855 | doi = 10.1016/j.tips.2006.02.006 }}
  • {{cite journal |vauthors=Lee DK, Saldivia VR, Nguyen T, Cheng R, George SR, O'Dowd BF | title = Modification of the terminal residue of apelin-13 antagonizes its hypotensive action | journal = Endocrinology | volume = 146 | issue = 1 | pages = 231–6 | year = 2005 | pmid = 15486224 | doi = 10.1210/en.2004-0359 }}
  • {{cite journal |vauthors=Lee DK, Lança AJ, Cheng R, Nguyen T, Ji XD, Gobeil F, Chemtob S, George SR, O'Dowd BF | title = Agonist-independent nuclear localization of the Apelin, angiotensin AT1, and bradykinin B2 receptors | journal = J. Biol. Chem. | volume = 279 | issue = 9 | pages = 7901–8 | year = 2004 | pmid = 14645236 | doi = 10.1074/jbc.M306377200 }}
  • {{cite journal |vauthors=O'Dowd BF, Heiber M, Chan A, Heng HH, Tsui LC, Kennedy JL, Shi X, Petronis A, George SR, Nguyen T | title = A human gene that shows identity with the gene encoding the angiotensin receptor is located on chromosome 11 | journal = Gene | volume = 136 | issue = 1–2 | pages = 355–60 | year = 1993 | pmid = 8294032 | doi = 10.1016/0378-1119(93)90495-O }}
  • {{cite journal |vauthors=Chun HJ, Ali ZA, Kojima Y, Kundu RK, Sheikh AY, Agrawal R, Zheng L, Leeper NJ, Pearl NE, Patterson AJ, Anderson JP, Tsao PS, Lenardo MJ, Ashley EA, Quertermous T | title = Apelin signaling antagonizes Ang II effects in mouse models of atherosclerosis | journal = The Journal of Clinical Investigation | volume = 118 | issue = 10 | pages = 3343–54 |date=October 2008 | pmid = 18769630 | pmc = 2525695 | doi = 10.1172/JCI34871 }}
  • {{cite journal |vauthors=Barnes G, Japp AG, Newby DE | title = Translational promise of the apelin--APJ system | journal = Heart | volume = 96 | issue = 13 | pages = 1011–6 |date=July 2010 | pmid = 20584856 | doi = 10.1136/hrt.2009.191122 }}
{{refend}}

External links

  • {{MeshName|Apelin+protein,+human}}
  • {{cite web | url = http://www.iuphar-db.org/GPCR/ChapterMenuForward?chapterID=1329 | title = Apelin | accessdate = | date = | format = | work = IUPHAR Database of Receptors and Ion Channels | publisher = International Union of Basic and Clinical Pharmacology | pages = | language = | archiveurl = | archivedate = | quote = }}
  • {{UCSC gene info|APLN}}

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