EDP Sciences logo
Authentification abonné
rechercher
Menu
Accueil Tous les numéros Volume 215 / Numéro 3-4 (2021) Biologie Aujourd’hui, 215 3-4 (2021) 119-132 Références
Accès gratuit
Numéro
Biologie Aujourd’hui
Volume 215, Numéro 3-4, 2021
Page(s) 119 - 132
DOI https://doi.org/10.1051/jbio/2021012
Publié en ligne 11 mars 2022
  • Azizi, M., Iturrioz, X., Blanchard, A., Peyrard, S., De Mota, N., Chartrel, N., Vaudry, H., Corvol, P., Llorens-Cortès, C. (2008). Reciprocal regulation of plasma apelin and vasopressin by osmotic stimuli. J Am Soc Nephrol, 19, 1015-1024. [CrossRef] [PubMed] [Google Scholar]
  • Bai, B., Tang, J., Liu, H., Chen, J., Li, Y., Song, W. (2008). Apelin-13 induces ERK1/2 but not p38 MAPK activation through coupling of the human apelin receptor to the Gi2 pathway. Acta Biochim Biophys Sin (Shanghai), 40, 311-318. [CrossRef] [PubMed] [Google Scholar]
  • Blanchard, A., Steichen, O., De Mota, N., Curis, E., Gauci, C., Frank, M., Wuerzner, G., Kamenicky, P., Passeron, A., Azizi, M., Llorens-Cortès, C. (2013). An abnormal apelin/vasopressin balance may contribute to water retention in patients with the syndrome of inappropriate antidiuretic hormone (SIADH) and heart failure. J Clin Endocrinol Metab, 98, 2084-2089. [CrossRef] [PubMed] [Google Scholar]
  • Boulkeroua, C., Ayari, H., Khalfaoui, T., Lafrance, M., Besserer-Offroy, É., Ekindi, N., Sabbagh, R., Dumaine, R., Lesur, O., Sarret, P., Chraibi, A. (2019). Apelin-13 Regulates Vasopressin-Induced Aquaporin-2 Expression and Trafficking in Kidney Collecting Duct Cells. Cell Physiol Biochem, 53, 687-700. [CrossRef] [PubMed] [Google Scholar]
  • Brailoiu, G.C., Dun, S.L., Yang, J., Ohsawa, M., Chang, J.K., Dun, N.J. (2002). Apelin-immunoreactivity in the rat hypothalamus and pituitary. Neurosci Lett, 327, 193-197. [CrossRef] [PubMed] [Google Scholar]
  • Brame, A.L., Maguire, J.J., Yang, P., Dyson, A., Torella, R., Cheriyan, J., Singer, M., Glen, R.C., Wilkinson, I.B., Davenport, A.P. (2015). Design, characterization, and first-in-human study of the vascular actions of a novel biased apelin receptor agonist. Hypertension, 65, 834-840. [CrossRef] [PubMed] [Google Scholar]
  • Brownstein, M.J., Russell, J.T., Gainer, H. (1980). Synthesis, transport, and release of posterior pituitary hormones. Science, 207, 373-378. [CrossRef] [PubMed] [Google Scholar]
  • Ceraudo, E., Galanth, C., Carpentier, E., Banegas-Font, I., Schonegge, A.-M., Alvear-Perez, R., Iturrioz, X., Bouvier, M., Llorens-Cortès, C. (2014). Biased signaling favoring gi over β-arrestin promoted by an apelin fragment lacking the C-terminal phenylalanine. J Biol Chem, 289, 24599-24610. [CrossRef] [PubMed] [Google Scholar]
  • Chen, X., Bai, B., Tian, Y., Du, H., Chen, J. (2014). Identification of serine 348 on the apelin receptor as a novel regulatory phosphorylation site in apelin-13-induced G protein-independent biased signaling. J Biol Chem, 289, 31173-31187. [CrossRef] [PubMed] [Google Scholar]
  • Chen, Y., Xu, C., Hu, J., Deng, M., Qiu, Q., Mo, S., Du, Y., Yang, T. (2021). Diuretic Action of Apelin-13 Mediated by Inhibiting cAMP/PKA/sPRR Pathway. Front Physiol, 12, 642274. [CrossRef] [PubMed] [Google Scholar]
  • Choe, W., Albright, A., Sulcove, J., Jaffer, S., Hesselgesser, J., Lavi, E., Crino, P., Kolson, D.L. (2000) Functional expression of the seven-transmembrane HIV-1 co-receptor APJ in neural cells. J Neurovirol, 6, S61-S69. [CrossRef] [MathSciNet] [PubMed] [Google Scholar]
  • Clarke, K.J., Whitaker, K.W., Reyes, T.M. (2009) Diminished metabolic responses to centrally-administered apelin-13 in diet-induced obese rats fed a high-fat diet. J Neuroendocrinol, 21, 83-89. [CrossRef] [MathSciNet] [PubMed] [Google Scholar]
  • D’Aniello, C., Lonardo, E., Iaconis, S., Guardiola, O., Liguoro, A.M., Liguori, G.L., Autiero, M., Carmeliet, P., Minchiotti, G. (2009). G protein-coupled receptor APJ and its ligand apelin act downstream of Cripto to specify embryonic stem cells toward the cardiac lineage through extracellular signal-regulated kinase/p70S6 kinase signaling pathway. Circ Res, 105, 231-238. [CrossRef] [PubMed] [Google Scholar]
  • De Falco, M., De Luca, L., Onori, N., Cavallotti, I., Artigiano, F., Esposito, V., De Luca, B., Laforgia, V., Groeger, A.M., De Luca, A. (2002). Apelin expression in normal human tissues. In Vivo, 16, 333-336. [Google Scholar]
  • De Mota, N., Lenkei, Z., Llorens-Cortès, C. (2000). Cloning, pharmacological characterization and brain distribution of the rat apelin receptor. Neuroendocrinology, 72, 400-407. [CrossRef] [PubMed] [Google Scholar]
  • De Mota, N., Réaux-Le Goazigo, A., El Messari, S., Chartrel, N., Roesch, D., Dujardin, C., Kordon, C., Vaudry, H., Moos, F., Llorens-Cortès, C. (2004). Apelin, a potent diuretic neuropeptide counteracting vasopressin actions through inhibition of vasopressin neuron activity and vasopressin release. Proc Natl Acad Sci USA, 101, 10464-10469. [Google Scholar]
  • Denton, D.A., McKinley, M.J., Weisinger, R.S. (1996). Hypothalamic integration of body fluid regulation. Proc Natl Acad Sci USA, 93, 7397-7404. [CrossRef] [PubMed] [Google Scholar]
  • Devic, E., Rizzoti, K., Bodin, S., Knibiehler, B., Audigier, Y. (1999). Amino acid sequence and embryonic expression of msr/apj, the mouse homolog of Xenopus X-msr and human APJ. Mech Dev, 84, 199-203. [CrossRef] [PubMed] [Google Scholar]
  • El Messari, S., Iturrioz, X., Fassot, C., De Mota, N., Roesch, D., Llorens-Cortès, C. (2004). Functional dissociation of apelin receptor signaling and endocytosis: implications for the effects of apelin on arterial blood pressure. J Neurochem, 90, 1290-1301. [CrossRef] [PubMed] [Google Scholar]
  • Ellison, D.H., Berl, T. (2007). Clinical practice. The syndrome of inappropriate antidiuresis. N Engl J Med, 356, 2064-2072. [CrossRef] [PubMed] [Google Scholar]
  • Evans, N.A., Groarke, D.A., Warrack, J., Greenwood, C.J., Dodgson, K., Milligan, G., Wilson, S. (2001). Visualizing differences in ligand-induced beta-arrestin-GFP interactions and trafficking between three recently characterized G protein-coupled receptors. J Neurochem, 77, 476-485. [CrossRef] [PubMed] [Google Scholar]
  • Eyries, M., Siegfried, G., Ciumas, M., Montagne, K., Agrapart, M., Lebrin, F., Soubrier, F. (2008). Hypoxia-induced apelin expression regulates endothelial cell proliferation and regenerative angiogenesis. Circ Res, 103, 432-440. [CrossRef] [PubMed] [Google Scholar]
  • Fischer, C., Lamer, T., Fernandez, K., Gheblawi, M., Wang, W., Pascoe, C., Lambkin, G., Iturrioz, X., Llorens-Cortès, C., Oudit, G.Y., Vederas, J.C. (2020). Optimizing PEG-extended apelin analogues as cardioprotective drug leads: Importance of the KFRR motif and aromatic head group for improved physiological activity. J Med Chem, 63, 12073-12082. [CrossRef] [PubMed] [Google Scholar]
  • Fischer, C., Lamer, T., Wang, W., McKinnie, S.M.K., Iturrioz, X., Llorens-Cortès, C., Oudit, G.Y., Vederas, J.C. (2019). Plasma kallikrein cleaves and inactivates apelin-17: Palmitoyl- and PEG-extended apelin-17 analogs as metabolically stable blood pressure-lowering agents. Eur J Med Chem, 166, 119-124. [CrossRef] [PubMed] [Google Scholar]
  • Flahault, A., Girault-Sotias, P.-E., Keck, M., Alvear-Perez, R., De Mota, N., Estéoulle, L., Ramanoudjame, S.M., Iturrioz, X., Bonnet, D., Llorens-Cortès, C. (2021). A metabolically stable apelin-17 analog decreases AVP-induced antidiuresis and improves hyponatremia. Nat Commun, 12, 305. [CrossRef] [PubMed] [Google Scholar]
  • Galon-Tilleman, H., Yang, H., Bednarek, M.A., Spurlock, S.M., Paavola, K.J., Ko, B., To, C., Luo, J., Tian, H., Jermutus, L., Grimsby, J., Rondinone, C.M., Konkar, A., Kaplan, D.D. (2017). Apelin-36 modulates blood glucose and body weight independently of canonical APJ receptor signaling. J Biol Chem, 292, 1925-1933. [CrossRef] [PubMed] [Google Scholar]
  • Gerbier, R., Alvear-Perez, R., Margathe, J.-F., Flahault, A., Couvineau, P., Gao, J., De Mota, N., Dabire, H., Li, B., Ceraudo, E., Hus-Citharel, A., Esteoulle, L., Bisoo, C., Hibert, M., Berdeaux, A., Iturrioz, X., Bonnet, D., Llorens-Cortès, C. (2017). Development of original metabolically stable apelin-17 analogs with diuretic and cardiovascular effects. FASEB J, 31, 687-700. [CrossRef] [PubMed] [Google Scholar]
  • Gerbier, R., Leroux, V., Couvineau, P., Alvear-Perez, R., Maigret, B., Llorens-Cortès, C., Iturrioz, X. (2015). New structural insights into the apelin receptor: identification of key residues for apelin binding. FASEB J, 29, 314-322. [CrossRef] [PubMed] [Google Scholar]
  • Gimpl, G., Fahrenholz, F. (2001). The oxytocin receptor system: structure, function, and regulation. Physiol Rev, 81, 629-683. [CrossRef] [PubMed] [Google Scholar]
  • Gouzènes, L., Desarménien, M.G., Hussy, N., Richard, P., Moos, F.C. (1998). Vasopressin regularizes the phasic firing pattern of rat hypothalamic magnocellular vasopressin neurons. J Neurosci, 18, 1879-1885. [CrossRef] [PubMed] [Google Scholar]
  • Habata, Y., Fujii, R., Hosoya, M., Fukusumi, S., Kawamata, Y., Hinuma, S., Kitada, C., Nishizawa, N., Murosaki, S., Kurokawa, T., Onda, H., Tatemoto, K., Fujino, M. (1999). Apelin, the natural ligand of the orphan receptor APJ, is abundantly secreted in the colostrum. Biochim Biophys Acta, 1452, 25-35. [CrossRef] [PubMed] [Google Scholar]
  • Hosoya, M., Kawamata, Y., Fukusumi, S., Fujii, R., Habata, Y., Hinuma, S., Kitada, C., Honda, S., Kurokawa, T., Onda, H., Nishimura, O., Fujino, M. (2000). Molecular and functional characteristics of APJ. Tissue distribution of mRNA and interaction with the endogenous ligand apelin. J Biol Chem, 275, 21061-21067. [CrossRef] [PubMed] [Google Scholar]
  • Hurbin, A., Boissin-Agasse, L., Orcel, H., Rabié, A., Joux, N., Desarménien, M.G., Richard, P., Moos, F.C. (1998). The V1a and V1b, but not V2, vasopressin receptor genes are expressed in the supraoptic nucleus of the rat hypothalamus, and the transcripts are essentially colocalized in the vasopressinergic magnocellular neurons. Endocrinology, 139, 4701-4707. [CrossRef] [PubMed] [Google Scholar]
  • Hus-Citharel, A., Bouby, N., Frugière, A., Bodineau, L., Gasc, J.-M., Llorens-Cortès, C. (2008). Effect of apelin on glomerular hemodynamic function in the rat kidney. Kidney Int, 74, 486-494. [CrossRef] [PubMed] [Google Scholar]
  • Hus-Citharel, A., Bodineau, L., Frugière, A., Joubert, F., Bouby, N., Llorens-Cortès, C. (2014). Apelin counteracts vasopressin-induced water reabsorption via cross talk between apelin and vasopressin receptor signaling pathways in the rat collecting duct. Endocrinology, 155, 4483-4493. [CrossRef] [PubMed] [Google Scholar]
  • 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. (2004) Regulatory Roles for APJ, a Seven-transmembrane Receptor Related to Angiotensin-type 1 Receptor in Blood Pressure in Vivo. J Biol Chem, 279, 26274-26279. [CrossRef] [PubMed] [Google Scholar]
  • Iturrioz, X., Gerbier, R., Leroux, V., Alvear-Perez, R., Maigret, B., Llorens-Cortès, C. (2010). By interacting with the C-terminal Phe of apelin, Phe255 and Trp259 in helix VI of the apelin receptor are critical for internalization. J Biol Chem, 285, 32627-32637 [CrossRef] [PubMed] [Google Scholar]
  • Japp, A.G., Cruden, N.L., Barnes, G., van Gemeren, N., Mathews, J., Adamson, J., Johnston, N.R., Denvir, M.A., Megson, I.L., Flapan, A.D., Newby, D.E. (2010). Acute cardiovascular effects of apelin in humans: Potential role in patients with chronic heart failure. Circulation, 121, 1818-1827. [CrossRef] [PubMed] [Google Scholar]
  • Jia, Z.Q., Hou, L., Leger, A., Wu, I., Kudej, A.B., Stefano, J., Jiang, C., Pan, C.Q., Akita, G.Y. (2012). Cardiovascular effects of a PEGylated apelin. Peptides, 38, 181-188. [CrossRef] [PubMed] [Google Scholar]
  • Johnson, A.K., Cunningham, J.T., Thunhorst, R.L. (1996). Integrative role of the lamina terminalis in the regulation of cardiovascular and body fluid homeostasis. Clin Exp Pharmacol Physiol, 23, 183-191. [CrossRef] [PubMed] [Google Scholar]
  • Juhl, C., Els-Heindl, S., Schönauer, R., Redlich, G., Haaf, E., Wunder, F., Riedl, B., Burkhardt, N., Beck-Sickinger, A.G., Bierer, D. (2016). Development of potent and metabolically stable APJ ligands with high therapeutic potential. Chem Med Chem, 11, 2378-2384. [CrossRef] [Google Scholar]
  • Kawamata, Y., Habata, Y., Fukusumi, S., Hosoya, M., Fujii, R., Hinuma, S., Nishizawa, N., Kitada, C., Onda, H., Nishimura, O., Fujino, M. (2001). Molecular properties of apelin: Tissue distribution and receptor binding. Biochim Biophys Acta, 1538, 162-171. [CrossRef] [PubMed] [Google Scholar]
  • Kim, W.R., Biggins, S.W., Kremers, W.K., Wiesner, R.H., Kamath, P.S., Benson, J.T., Edwards, E., Therneau, T.M. (2008). Hyponatremia and mortality among patients on the liver-transplant waiting list. N Engl J Med, 359, 1018-1026. [CrossRef] [PubMed] [Google Scholar]
  • Kleinz, M.J., Skepper, J.N., Davenport, A.P. (2005). Immunocytochemical localisation of the apelin receptor, APJ, to human cardiomyocytes, vascular smooth muscle and endothelial cells. Regul Pept, 126, 233-240. [CrossRef] [PubMed] [Google Scholar]
  • Kovesdy, C.P., Lott, E.H., Lu, J.L., Malakauskas, S.M., Ma, J.Z., Molnar, M.Z., Kalantar-Zadeh, K. (2012). Hyponatremia, hypernatremia, and mortality in patients with chronic kidney disease with and without congestive heart failure. Circulation, 125, 677-684. [CrossRef] [PubMed] [Google Scholar]
  • Lee, D.K., Cheng, R., Nguyen, T., Fan, T., Kariyawasam, A.P., Liu, Y., Osmond, D.H., George, S.R., O’Dowd, B.F. (2000). Characterization of apelin, the ligand for the APJ receptor. J Neurochem, 74, 34-41. [Google Scholar]
  • Lee, D.K., Saldivia, V.R., Nguyen, T., Cheng, R., George, S.R., O’Dowd, B.F. (2005). Modification of the terminal residue of apelin-13 antagonizes its hypotensive action. Endocrinology, 146, 231-236. [CrossRef] [PubMed] [Google Scholar]
  • Lee, D.K., Ferguson, S.S.G., George, S.R., O’Dowd, B.F. (2010). The fate of the internalized apelin receptor is determined by different isoforms of apelin mediating differential interaction with beta-arrestin. Biochem Biophys Res Commun, 395, 185-189. [CrossRef] [PubMed] [Google Scholar]
  • Llorens-Cortès, C., Moos, F. (2012). Apelin and vasopressin: two work better than one. J Neuroendocrinol, 24, 1085-1086. [CrossRef] [PubMed] [Google Scholar]
  • Ludwig, M. (1998). Dendritic release of vasopressin and oxytocin. J Neuroendocrinol, 10, 881-895. [CrossRef] [PubMed] [Google Scholar]
  • Manning, M., Lowbridge, J., Haldar, J., Sawyer, W.H. (1977). Design of neurohypophyseal peptides that exhibit selective agonistic and antagonistic properties. Fed Proc, 36, 1848-1852. [PubMed] [Google Scholar]
  • Masri, B., Lahlou, H., Mazarguil, H., Knibiehler, B., Audigier, Y. (2002). Apelin (65-77) activates extracellular signal-regulated kinases via a PTX-sensitive G protein. Biochem Biophys Res Commun, 290, 539-545. [CrossRef] [PubMed] [Google Scholar]
  • Masri, B., Morin, N., Pedebernade, L., Knibiehler, B., Audigier, Y. (2006). The apelin receptor is coupled to Gi1 or Gi2 protein and is differentially desensitized by apelin fragments. J Biol Chem, 281, 18317-18326. [CrossRef] [PubMed] [Google Scholar]
  • McKinnie, S.M.K., Fischer, C., Tran, K.M.H., Wang, W., Mosquera, F., Oudit, G.Y., Vederas, J.C. (2016). The metalloprotease neprilysin degrades and inactivates apelin peptides. Chembiochem, 17, 1495-1498. [CrossRef] [PubMed] [Google Scholar]
  • Medhurst, A.D., Jennings, C.A., Robbins, M.J., Davis, R.P., Ellis, C., Winborn, K.Y., Lawrie, K.W.M., Hervieu, G., Riley, G., Bolaky, J.E., Herrity, N.C., Murdock, P., Darker, J.G. (2003). Pharmacological and immunohistochemical characterization of the APJ receptor and its endogenous ligand apelin. J Neurochem, 84, 1162-1172. [CrossRef] [PubMed] [Google Scholar]
  • Miyazaki, T., Yamamura, Y., Onogawa, T., Nakamura, S., Kinoshita, S., Nakayama, S., Fujiki, H., Mori, T. (2005). Therapeutic effects of tolvaptan, a potent, selective nonpeptide vasopressin V2 receptor antagonist, in rats with acute and chronic severe hyponatremia. Endocrinology, 146, 3037-3043. [CrossRef] [PubMed] [Google Scholar]
  • Morello, J.P., Bichet, D.G. (2001). Nephrogenic diabetes insipidus. Annu Rev Physiol, 63, 607-630. [CrossRef] [PubMed] [Google Scholar]
  • Murza, A., Belleville, K., Longpré, J.-M., Sarret, P., Marsault, É. (2014). Stability and degradation patterns of chemically modified analogs of apelin-13 in plasma and cerebrospinal fluid. Biopolymers, 102, 297-303. [CrossRef] [PubMed] [Google Scholar]
  • Murza, A., Besserer-Offroy, É., Côté, J., Bérubé, P., Longpré, J.-M., Dumaine, R., Lesur, O., Auger-Messier, M., Leduc, R., Sarret, P., Marsault, É. (2015). C-Terminal modifications of apelin-13 significantly change ligand binding, receptor signaling, and hypotensive action. J Med Chem, 58, 2431-2440. [CrossRef] [PubMed] [Google Scholar]
  • Murza, A., Sainsily, X., Coquerel, D., Côté, J., Marx, P., Besserer-Offroy, É., Longpré, J.-M., Lainé, J., Reversade, B., Salvail, D., Leduc, R., Dumaine, R., Lesur, O., Auger-Messier, M., Sarret, P., Marsault, E. (2016). Discovery and structure-activity relationship of a bioactive fragment of ELABELA that modulates vascular and cardiac functions. J Med Chem, 59, 2962-2972. [CrossRef] [PubMed] [Google Scholar]
  • Murza, A., Sainsily, X., Côté, J., Bruneau-Cossette, L., Besserer-Offroy, É., Longpré, J.-M., Leduc, R., Dumaine, R., Lesur, O., Auger-Messier, M., Sarret, P., Marsault, É. (2017). Structure-activity relationship of novel macrocyclic biased apelin receptor agonists. Org Biomol Chem, 15, 449-458. [CrossRef] [MathSciNet] [PubMed] [Google Scholar]
  • Nielsen, S., Chou, C.L., Marples, D., Christensen, E.I., Kishore, B.K., Knepper, M.A. (1995). Vasopressin increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane. Proc Natl Acad Sci USA, 92, 1013-1017. [CrossRef] [PubMed] [Google Scholar]
  • O’Carroll, A.-M., Lolait, S.J. (2003). Regulation of rat APJ receptor messenger ribonucleic acid expression in magnocellular neurones of the paraventricular and supraopric nuclei by osmotic stimuli. J Neuroendocrinol, 15, 661-666. [CrossRef] [PubMed] [Google Scholar]
  • O’Carroll, A.-M., Salih, S., Griffiths, P.R., Bijabhai, A., Knepper, M.A., Lolait, S.J. (2017). Expression and functional implications of the renal apelinergic system in rodents. PLoS One, 12, e0183094. [CrossRef] [PubMed] [Google Scholar]
  • O’Carroll, A.M., Selby, T.L., Palkovits, M., Lolait, S.J. (2000). Distribution of mRNA encoding B78/apj, the rat homologue of the human APJ receptor, and its endogenous ligand apelin in brain and peripheral tissues. Biochim Biophys Acta, 1492, 72-80. [CrossRef] [MathSciNet] [Google Scholar]
  • O’Dowd, B.F., Heiber, M., Chan, A., Heng, H.H., Tsui, L.C., Kennedy, J.L., Shi, X., Petronis, A., George, S.R., Nguyen, T. (1993). A human gene that shows identity with the gene encoding the angiotensin receptor is located on chromosome 11. Gene, 136, 355-360. [CrossRef] [PubMed] [Google Scholar]
  • O’Harte, F.P.M., Flatt, P.R. (2015). Patent: Apelin analogues – WO 2015/165936 Al. [Google Scholar]
  • Ostrowski, N.L., Lolait, S.J., Bradley, D.J., O’Carroll, A.M., Brownstein, M.J., Young, W.S. (1992). Distribution of V1a and V2 vasopressin receptor messenger ribonucleic acids in rat liver, kidney, pituitary and brain. Endocrinology, 131, 533-535. [CrossRef] [PubMed] [Google Scholar]
  • Peri, A. (2019). Management of hyponatremia: causes, clinical aspects, differential diagnosis and treatment. Expert Rev Endocrinol Metab, 14, 13-21. [CrossRef] [PubMed] [Google Scholar]
  • Poulain, D.A., Wakerley, J.B., Dyball, R.E. (1977). Electrophysiological differentiation of oxytocin- and vasopressin-secreting neurones. Proc R Soc Lond B Biol Sci, 196, 367-384. [CrossRef] [PubMed] [Google Scholar]
  • Réaux, A., De Mota, N., Skultetyova, I., Lenkei, Z., El Messari, S., Gallatz, K., Corvol, P., Palkovits, M., Llorens-Cortès, C. (2001). Physiological role of a novel neuropeptide, apelin, and its receptor in the rat brain. J Neurochem, 77, 1085-1096. [CrossRef] [PubMed] [Google Scholar]
  • Réaux, A., Gallatz, K., Palkovits, M., Llorens-Cortès, C. (2002). Distribution of apelin-synthesizing neurons in the adult rat brain. Neuroscience, 113, 653-662. [CrossRef] [PubMed] [Google Scholar]
  • Réaux-Le Goazigo, A., Morinville, A., Burlet, A., Llorens-Cortès, C., Beaudet, A. (2004). Dehydration-induced cross-regulation of apelin and vasopressin immunoreactivity levels in magnocellular hypothalamic neurons. Endocrinology, 145, 4392-4400. [CrossRef] [PubMed] [Google Scholar]
  • Ripoll, E., Pluvinet, R., Torras, J., Olivar, R., Vidal, A., Franquesa, M., Cassis, L., Cruzado, J.M., Bestard, O., Grinyó, J.M., Aran, J.M., Herrero-Fresneda, I. (2011). In vivo therapeutic efficacy of intra-renal CD40 silencing in a model of humoral acute rejection. Gene Ther, 18, 945-952. [CrossRef] [PubMed] [Google Scholar]
  • Roberts, E.M., Newson, M.J.F., Pope, G.R., Landgraf, R., Lolait, S.J., O’Carroll, A.-M. (2009). Abnormal fluid homeostasis in apelin receptor knockout mice. J Endocrinol, 202, 453-462. [CrossRef] [PubMed] [Google Scholar]
  • Sands, J.M., Naruse, M., Baum, M., Jo, I., Hebert, S.C., Brown, E.M., Harris, H.W. (1997). Apical extracellular calcium/polyvalent cation-sensing receptor regulates vasopressin-elicited water permeability in rat kidney inner medullary collecting duct. J Clin Invest, 99, 1399-1405. [CrossRef] [PubMed] [Google Scholar]
  • Tatemoto, K., Hosoya, M., Habata, Y., Fujii, R., Kakegawa, T., Zou, M.X., Kawamata, Y., Fukusumi, S., Hinuma, S., Kitada, C., Kurokawa, T., Onda, H., Fujino, M. (1998). Isolation and characterization of a novel endogenous peptide ligand for the human APJ receptor. Biochem Biophys Res Commun, 251, 471-476. [CrossRef] [PubMed] [Google Scholar]
  • Tatemoto, K., Takayama, K., Zou, M.-X., Kumaki, I., Zhang, W., Kumano, K., Fujimiya, M. (2001). The novel peptide apelin lowers blood pressure via a nitric oxide-dependent mechanism. Regulatory Peptides, 99, 87-92. [CrossRef] [PubMed] [Google Scholar]
  • Terada, Y., Tomita, K., Nonoguchi, H., Yang, T., Marumo, F. (1993). Different localization and regulation of two types of vasopressin receptor messenger RNA in microdissected rat nephron segments using reverse transcription polymerase chain reaction. J Clin Invest, 92, 2339-2345. [CrossRef] [PubMed] [Google Scholar]
  • Trân, K., Murza, A., Sainsily, X., Coquerel, D., Côté, J., Belleville, K., Haroune, L., Longpré, J.-M., Dumaine, R., Salvail, D., Lesur, O., Auger-Messier, M., Sarret, P., Marsault, É. (2018). A systematic exploration of macrocyclization in Apelin-13: Impact on binding, signaling, stability, and cardiovascular effects. J Med Chem, 61, 2266-2277. [CrossRef] [PubMed] [Google Scholar]
  • Verbalis, J.G. (2019). Euvolemic hyponatremia secondary to the syndrome of inappropriate antidiuresis. Front Horm Res, 52, 61-79. [CrossRef] [PubMed] [Google Scholar]
  • Verbalis, J.G., Goldsmith, S.R., Greenberg, A., Korzelius, C., Schrier, R.W., Sterns, R.H., Thompson, C.J. (2013). Diagnosis, evaluation, and treatment of hyponatremia: expert panel recommendations. Am J Med, 126, S1-42. [CrossRef] [PubMed] [Google Scholar]
  • Waikar, S.S., Mount, D.B., Curhan, G.C. (2009). Mortality after hospitalization with mild, moderate, and severe hyponatremia. Am J Med, 122, 857-865. [CrossRef] [PubMed] [Google Scholar]
  • Wang, W., McKinnie, S.M.K., Farhan, M., Paul, M., McDonald, T., McLean, B., Llorens-Cortès, C., Hazra, S., Murray, A.G., Vederas, J.C., Oudit, G.Y. (2016). Angiotensin-converting enzyme 2 metabolizes and partially inactivates Pyr-Apelin-13 and Apelin-17: Physiological effects in the cardiovascular system. Hypertension, 68, 365-377. [CrossRef] [PubMed] [Google Scholar]
  • Xu, C., Wang, F., Chen, Y., Xie, S., Sng, D., Reversade, B., Yang, T. (2020). ELABELA antagonizes intrarenal renin-angiotensin system to lower blood pressure and protects against renal injury. Am J Physiol Renal Physiol, 318, F1122- F1135. [CrossRef] [PubMed] [Google Scholar]
  • Zhou, N., Fan, X., Mukhtar, M., Fang, J., Patel, C.A., DuBois, G.C., Pomerantz, R.J. (2003a). Cell-cell fusion and internalization of the CNS-based, HIV-1 co-receptor, APJ. Virology, 307, 22-36 [CrossRef] [Google Scholar]
  • Zhou, N., Zhang, X., Fan, X., Argyris, E., Fang, J., Acheampong, E., DuBois, G.C., Pomerantz, R.J. (2003b). The N-terminal domain of APJ, a CNS-based coreceptor for HIV-1, is essential for its receptor function and coreceptor activity. Virology, 317, 84-94. [CrossRef] [Google Scholar]
  • Zini, S., Fournie-Zaluski, M.C., Chauvel, E., Roques, B.P., Corvol, P., Llorens-Cortès, C. (1996). Identification of metabolic pathways of brain angiotensin II and III using specific aminopeptidase inhibitors: predominant role of angiotensin III in the control of vasopressin release. Proc Natl Acad Sci USA, 93, 11968-11973. [CrossRef] [PubMed] [Google Scholar]

Les statistiques affichées correspondent au cumul d'une part des vues des résumés de l'article et d'autre part des vues et téléchargements de l'article plein-texte (PDF, Full-HTML, ePub... selon les formats disponibles) sur la platefome Vision4Press.

Les statistiques sont disponibles avec un délai de 48 à 96 heures et sont mises à jour quotidiennement en semaine.

Le chargement des statistiques peut être long.