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Journal articles on the topic 'Urotensin II'

Author: Grafiati

Published: 4 June 2021

Last updated: 10 March 2023

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1

Giuliani, Luisa, Livia Lenzini, Michele Antonello, Enrico Aldighieri, Anna S. Belloni, Ambrogio Fassina, Celso Gomez-Sanchez, and Gian Paolo Rossi. "Expression and Functional Role of Urotensin-II and Its Receptor in the Adrenal Cortex and Medulla: Novel Insights for the Pathophysiology of Primary Aldosteronism." Journal of Clinical Endocrinology & Metabolism 94, no. 2 (February 1, 2009): 684–90. http://dx.doi.org/10.1210/jc.2008-1131.

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Abstract Context: The involvement of urotensin II, a vasoactive peptide acting via the G protein-coupled urotensin II receptor, in arterial hypertension remains contentious. Objective: We investigated the expression of urotensin II and urotensin II receptor in adrenocortical and adrenomedullary tumors and the functional effects of urotensin II receptor activation. Design: The expression of urotensin II and urotensin II receptor was measured by real time RT-PCR in aldosterone-producing adenoma (n = 22) and pheochromocytoma (n = 10), using histologically normal adrenocortical (n = 6) and normal adrenomedullary (n = 5) tissue as control. Urotensin II peptide and urotensin II receptor protein were investigated with immunohistochemistry and immunoblotting. To identify urotensin II-related and urotensin II receptor-related pathways, a whole transcriptome analysis was used. The adrenocortical effects of urotensin II receptor activation were also assessed by urotensin II infusion with/without the urotensin II receptor antagonist palosuran in rats. Results: Urotensin II was more expressed in pheochromocytoma than in aldosterone-producing adenoma tissue; the opposite was seen for the urotensin II receptor expression. Urotensin II receptor activation in vivo in rats enhanced (by 182 ± 9%; P < 0.007) the adrenocortical expression of immunoreactive aldosterone synthase. Conclusions: Urotensin II is a putative mediator of the effects of the adrenal medulla and pheochromocytoma on the adrenocortical zona glomerulosa. This pathophysiological link might account for the reported causal relationship between pheochromocytoma and primary aldosteronism.

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2

Desai, Nirav, Jameel Sajjad, and William H. Frishman. "Urotensin II." Cardiology in Review 16, no. 3 (May 2008): 142–53. http://dx.doi.org/10.1097/crd.0b013e31815c8048.

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3

Giebing, G., M. Tölle, S. Schmidt, A. Oksche, W. Zidek, and M. Van Der Giet. "UROTENSIN II-RECEPTORS SHOW RAPID DESENSITIZATION AFTER STIMULATION WITH UROTENSIN II." Journal of Hypertension 22, Suppl. 2 (June 2004): S48. http://dx.doi.org/10.1097/00004872-200406002-00161.

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4

Dubessy, Christophe, Dorthe Cartier, Benoît Lectez, Christine Bucharles, Nicolas Chartrel, Maïté Montero-Hadjadje, Patrice Bizet, et al. "Characterization of urotensin II, distribution of urotensin II, urotensin II-related peptide and UT receptor mRNAs in mouse: evidence of urotensin II at the neuromuscular junction." Journal of Neurochemistry 107, no. 2 (August 14, 2008): 361–74. http://dx.doi.org/10.1111/j.1471-4159.2008.05624.x.

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5

Lafta, Israa A., Nahla A. AL-Bakri, and Wasan A. Abdulhameed. "Expression of Urotensin II of Human Placental Tissues and in Serum in Gestational Diabetic Mellitus in Iraqi Woman." INTERNATIONAL JOURNAL OF DRUG DELIVERY TECHNOLOGY 12, no. 01 (June 25, 2022): 70–73. http://dx.doi.org/10.25258/ijddt.12.1.13.

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The placenta is an organ between the mother and fetus necessary for fetal growth and development. Gestational diabetes mellitus (DM) is the most frequent metabolic condition detected during pregnancy. It is characterized as hyperglycemia of various severity with onset or first detection during pregnancy that does not clearly describe any form of preexisting diabetes. Urotensin II (UII), a pluripotent vasoactive peptide, is important in developing insulin resistance. This study aimed to determine the level of Urotensin II(UII) in placenta and in the serum of diabetic and nondiabetic women. Methods The blood and placenta tissue collected from 50 ladies had been enrolled in this research ( 25 females with uncomplicated), (25 women with gestational diabetes). Immunohistochemistry (IHC) was used to look at the expression of the Urotensin II (UII) marker in placenta specimens. The IHC analysis revealed that Urotensin II expression was primarily found in placental cytotrophoblast and the syncytiotrophoblast. Results of an immunohistochemistry investigation using the Urotensin II (UII) marker revealed a significant increase (p ≤ 0.001) in diabetic women’s placentas and serum than control groups. Conclusion, the Urotensin II is mainly located in the cytotrophoblast and syncytiotrophoblast. That was significantly higher in the gestational DM group.

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6

Itoh, H., and K. Lederis. "Relationship of urotensin I induced vasodilatory action in rat thoracic aorta to Ca2+ regulation." Canadian Journal of Physiology and Pharmacology 65, no. 3 (March 1, 1987): 298–302. http://dx.doi.org/10.1139/y87-052.

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The relaxant effects of the synthetic fish neuropeptide urotensin I were examined in helical strips of rat aorta. In K+-depolarized aorta strips, urotensin I and verapamil competitively inhibited Ca2+-induced contractions. Urotensin I relaxed, in a concentration-dependent manner, the contraction produced by the Ca2+ ionophore A23187, whereas verapamil had no effect on this contraction, even at a concentration of 10−5 M. In the absence and presence of extracellular Ca2+, urotensin I inhibited both components of the contractions elicited by norepinephrine or urotensin II, another fish neuropeptide. Verapamil reduced only the norepinephrine or urotensin II induced contraction in the presence of extracellular Ca2+, with little or no change in the contraction in Ca2+-free buffer. The urotensin I induced relaxation response in aortic strips contracted by 40 mM KCl was enhanced by pretreatment with papaverine or forskolin. Pretreatment with dibutyryl cAMP did not significantly alter the action of urotensin I. The presence or absence of endothelial cells did not change the response to urotensin I. These results suggest that urotensin I antagonizes the action and (or) mobilization of extracellular and intracellular Ca2+.

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7

Strack, Martin, Étienne Billard, David Chatenet, and William D. Lubell. "Urotensin core mimics that modulate the biological activity of urotensin-II related peptide but not urotensin-II." Bioorganic & Medicinal Chemistry Letters 27, no. 15 (August 2017): 3412–16. http://dx.doi.org/10.1016/j.bmcl.2017.05.088.

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8

Carotenuto, A., P. Grieco, P. Rovero, and E. Novellino. "Urotensin-II Receptor Antagonists." Current Medicinal Chemistry 13, no. 3 (February 1, 2006): 267–75. http://dx.doi.org/10.2174/092986706775476061.

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9

Loirand, Gervaise, Malvyne Rolli-Derkinderen, and Pierre Pacaud. "Urotensin II and atherosclerosis." Peptides 29, no. 5 (May 2008): 778–82. http://dx.doi.org/10.1016/j.peptides.2007.08.024.

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10

Hazon, N., C. Bjenning, and J. M. Conlon. "Cardiovascular actions of dogfish urotensin II in the dogfish Scyliorhinus canicula." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 265, no. 3 (September 1, 1993): R573—R576. http://dx.doi.org/10.1152/ajpregu.1993.265.3.r573.

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Bolus injections of synthetic dogfish urotensin II (0.1-1.0 nmol) into the celiac artery of the conscious dogfish Scyliorhinus canicula (n = 8) resulted in sustained and dose-dependent increases in arterial blood pressure and pulse pressure. A maximum rise in mean arterial pressure of 10.5 +/- 1.2 mmHg (equivalent to 38.6 +/- 4.2% over mean basal values) and a maximum increase in pulse pressure of 3.9 +/- 0.8 mmHg was elicited by injection of 0.5 nmol of peptide. In comparison, a bolus injection of epinephrine (5 nmol) elicited a rise of 24.8 +/- 3.3% in mean arterial pressure. Bolus injection of 0.5 nmol synthetic goby (Gillichthys mirabilis) urotensin II under the same conditions did not elicit a significant hypertensive response. When dogfish urotensin II (0.5 nmol) was administered 3 min after an intra-arterial injection of phentolamine, the rise in arterial blood pressure was completely abolished. Dogfish urotensin II produced a dose-dependent contraction (pD2 = 6.58 +/- 0.07; n = 8) of isolated rings of vascular muscle prepared from the first afferent branchial artery of the dogfish. A maximum contractile force of 1.3 mN was produced by 10(-5) M peptide. The urotensin II-induced contraction of the vascular rings was unaffected by pretreatment with tetrodotoxin (1 microM) or indomethacin (14 microM). It is concluded that urotensin II has potent hypertensive activity in the dogfish that is mediated, at least in part, through release of catecholamines, but the sustained nature of the pressor response suggests that the peptide may have a direct action on the heart.

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11

Merlino, Francesco, Salvatore Di Maro, Ali Munaim Yousif, Michele Caraglia, and Paolo Grieco. "Urotensin-II Ligands: An Overview from Peptide to Nonpeptide Structures." Journal of Amino Acids 2013 (February 25, 2013): 1–15. http://dx.doi.org/10.1155/2013/979016.

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Urotensin-II was originally isolated from the goby urophysis in the 1960s as a vasoactive peptide with a prominent role in cardiovascular homeostasis. The identification of human isoform of urotensin-II and its specific UT receptor by Ames et al. in 1999 led to investigating the putative role of the interaction U-II/UT receptor in multiple pathophysiological effects in humans. Since urotensin-II is widely expressed in several peripheral tissues including cardiovascular system, the design and development of novel urotensin-II analogues can improve knowledge about structure-activity relationships (SAR). In particular, since the modulation of the U-II system offers a great potential for therapeutic strategies related to the treatment of several diseases, like cardiovascular diseases, the research of selective and potent ligands at UT receptor is more fascinating. In this paper, we review the developments of peptide and nonpeptide U-II structures so far developed in order to contribute also to a more rational and detectable design and synthesis of new molecules with high affinity at the UT receptor.

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12

Langham, Robyn G., Darren J. Kelly, Renae M. Gow, Yuan Zhang, John K. Dowling, Napier M. Thomson, and Richard E. Gilbert. "Increased expression of urotensin II and urotensin II receptor in human diabetic nephropathy." American Journal of Kidney Diseases 44, no. 5 (November 2004): 826–31. http://dx.doi.org/10.1016/s0272-6386(04)01130-8.

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13

Prosser, H. C. G., M. E. Forster, A. M. Richards, and C. J. Pemberton. "Urotensin II and urotensin II-related peptide (URP) in cardiac ischemia-reperfusion injury." Peptides 29, no. 5 (May 2008): 770–77. http://dx.doi.org/10.1016/j.peptides.2007.08.013.

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14

Russell, Fraser. "Urotensin II in cardiovascular regulation." Vascular Health and Risk Management Volume 4 (August 2008): 775–85. http://dx.doi.org/10.2147/vhrm.s1983.

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15

Sun, Shui-lin, and Liang-ming Liu. "Urotensin II: an inflammatory cytokine." Journal of Endocrinology 240, no. 3 (March 2019): R107—R117. http://dx.doi.org/10.1530/joe-18-0505.

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Urotensin II (UII) is a polypeptide molecule with neurohormone-like activity. It has been confirmed that UII is widely distributed in numerous organs of different animal species from fish to mammals, including humans. The UII receptor is orphan G-protein-coupled receptor 14, also known as UT. The tissue distribution of UII and UT is highly consistent, and their expression may be regulated by autocrine and paracrine mechanisms. In the body, UII has many physiological and pathophysiological activities, such as vasoconstrictor and vasodilatory actions, cell proliferation, pro-fibrosis, neuroendocrine activity, insulin resistance and carcinogenic and inflammatory effects, which have been recognized only in recent years. In fact, UII is involved in the process of inflammatory injury and plays a key role in the onset and development of inflammatory diseases. In this paper, we will review the roles UII plays in inflammatory diseases.

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16

Langham, Robyn G., and Darren J. Kelly. "Urotensin II and the kidney." Current Opinion in Nephrology and Hypertension 22, no. 1 (January 2013): 107–12. http://dx.doi.org/10.1097/mnh.0b013e32835b6d57.

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17

Thanassoulis, George, Thao Huyhn, and Adel Giaid. "Urotensin II and cardiovascular diseases." Peptides 25, no. 10 (October 2004): 1789–94. http://dx.doi.org/10.1016/j.peptides.2004.05.027.

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18

Papadopoulos, Panayiota, Nicolas Bousette, and Adel Giaid. "Urotensin-II and cardiovascular remodeling." Peptides 29, no. 5 (May 2008): 764–69. http://dx.doi.org/10.1016/j.peptides.2007.09.012.

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19

do Rego, Jean-Claude, Jérôme Leprince, Elizabeth Scalbert, Hubert Vaudry, and Jean Costentin. "Behavioral actions of urotensin-II." Peptides 29, no. 5 (May 2008): 838–44. http://dx.doi.org/10.1016/j.peptides.2007.12.016.

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20

Bousette, Nicolas, and Adel Giaid. "Urotensin-II and cardiovascular diseases." Current Hypertension Reports 8, no. 6 (November 2006): 479–83. http://dx.doi.org/10.1007/s11906-006-0026-7.

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21

NICHOLLS, H. "Urotensin II in human plasma." Trends in Endocrinology and Metabolism 12, no. 9 (November 1, 2001): 381–82. http://dx.doi.org/10.1016/s1043-2760(01)00510-0.

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22

Carotenuto, Alfonso, Paolo Grieco, Ettore Novellino, and Paolo Rovero. "Urotensin-II receptor peptide agonists." Medicinal Research Reviews 24, no. 5 (2004): 577–88. http://dx.doi.org/10.1002/med.20001.

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23

Malagon, Maria M., Marcelo Molina, Manuel D. Gahete, Mario Duran-Prado, Antonio J. Martinez-Fuentes, Francisco J. Alcain, Marie-Christine Tonon, et al. "Urotensin II and urotensin II-related peptide activate somatostatin receptor subtypes 2 and 5." Peptides 29, no. 5 (May 2008): 711–20. http://dx.doi.org/10.1016/j.peptides.2007.12.015.

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24

Loretz, C. A., M. E. Howard, and A. J. Siegel. "Ion transport in goby intestine: cellular mechanism of urotensin II stimulation." American Journal of Physiology-Gastrointestinal and Liver Physiology 249, no. 2 (August 1, 1985): G284—G293. http://dx.doi.org/10.1152/ajpgi.1985.249.2.g284.

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The Na- and Cl-absorbing goby posterior intestinal epithelium is composed predominantly of mitochondria-rich, tall columnar cells. Glass intracellular microelectrode recording technique was applied to absorptive cells of this relatively leaky epithelium to measure apical cell membrane potential difference (psi mc) and apical membrane fractional resistance. As determined by ion-substitution studies, absorptive cells are characterized by a large, Ba2+-inhibitable apical K conductance, which is a major factor determining psi mc and smaller Cl and Na conductances. Inhibition of the apical Na-Cl-coupled influx directly by furosemide or indirectly by the phosphodiesterase inhibitor 3-isobutyl-1-methylxanthine produced hyperpolarization of psi mc, consistent with the greater apical membrane conductance to Cl than Na. The urophysial neurosecretory peptide urotensin II, which stimulates Na-Cl-coupled absorption, markedly depolarized psi mc in posterior intestinal tissues from 5% seawater-adapted gobies. This response is consistent with a stimulatory effect of urotensin II at the apical membrane carrier rather than at the basolateral Na-K-ATPase. Urotensin II is without effect on psi mc in tissues from seawater-adapted fish and somatostatin, a natural analogue of urotensin II, is without effect on tissues from fish adapted to either salinity. This specificity parallels that determined using radiotracer fluxes.

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25

Pavanato, Maria Amália, Bernardo Baldisserotto, Roni João Rakoski, and Olga Martins Mimura. "Transepithelial potential difference of the intestine and gallbladder of Hoplias malabaricus, a freshwater teleost. effect of urotensins I and II." Ciência e Natura 18, no. 18 (December 9, 1996): 83. http://dx.doi.org/10.5902/2179460x26607.

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This study analyzed the effect of the injection of urotensin I (UI) and urotensis II (UII) on the stabilization of the transepithelial potential difference (TPD) of the medium intestine, rectum, and gallbladder of Hoplias malabaricus to investigate if the transport of ions in these organs is affected "in vivo" by these neurohormones. The TPD of the medium intestine, rectum and gallbladder was serosa positive, and remained constant since the first measurement. The injection of both urotensins did not alter the stabilization of the TPD of the medium intestine and rectum when compared with saline-injected group. The injection of UI increased the TPD of the gallbladder in the beginning (0-10 min) of the stabilization period and in the interval of 20-30 min of the stabilization period when fishes were killed 2h and 4h after the injection, respectively, in relation to saline-injected group. The UII injection increased the TPD of the gallbladder only in the beginning (time 0) of the stabilization period in relation to saline when fishes were killed 2h after the injection. No changes in the TPD of the studied organs were detected when fishes were killed 4h after the injection of UII. This study confirms the hypothesis that UI and UII can participate in the regulation of the composition of the bile of fishes, since the injection of both hormones altered the TPD of the gallbladder of H. malabaricus.

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26

Katugampola, S. D., J. J. Maguire, R. E. Kuc, K. E. Wiley, and A. P. Davenport. "Discovery of recently adopted orphan receptors for apelin, urotensin II, and ghrelin identified using novel radioligands and functional role in the human cardiovascular system." Canadian Journal of Physiology and Pharmacology 80, no. 5 (May 1, 2002): 369–74. http://dx.doi.org/10.1139/y02-029.

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Using novel synthetic radioligands, we have discovered receptors for the recently paired apelin (APJ orphan receptor), ghrelin (GHS orphan receptor), and urotensin II (orphan GPR14) in the human cardiovascular system and determined their anatomical localisation. In addition, we have established functional vasoactive properties for these three peptides as potential vasoconstrictor/vasodilator mediators and provided evidence for alteration of receptor density in cardiovascular disease. We find that receptors for apelin, ghrelin, and urotensin II are widely distributed in human cardiovascular tissue, suggesting perhaps vasoactive roles for these peptides in human vascular physiology and a potential role in pathophysiology. Apelin and urotensin II are potent vasoconstrictors with low efficacy, consistent with their low receptor density. Ghrelin receptor density was increased (approximately three- to fourfold) with atherosclerosis of coronary artery disease and accelerated atherosclerosis of saphenous vein grafts, compared with normal vessels, highlighting a potentially beneficial role for this novel vasodilator peptide in human vascular disease. Our approach has demonstrated one successful strategy for translating genetic information encoding recently paired orphan receptor ligands into discovery of function. This study has the advantage of focussing on the actual disease processes, which allow the more precise identification of novel therapeutic targets.Key words: apelin, ghrelin, urotensin II, human, orphan receptor.

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27

Kim, Junghyun, Eunjin Sohn, Chan-Sik Kim, Yun Mi Lee, Kyuhyung Jo, and Jin Sook Kim. "Effect of KIOM-79 on Diabetes-Induced Myocardial Fibrosis in Zucker Diabetic Fatty Rats." Evidence-Based Complementary and Alternative Medicine 2013 (2013): 1–8. http://dx.doi.org/10.1155/2013/547653.

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KIOM-79, a herbal mixture of parched Puerariae radix, gingered Magnoliae cortex, Glycyrrhizae radix, and Euphorbiae radix, has a strong inhibitory effect on advanced glycation end products (AGEs) formation. We investigated the beneficial effects of KIOM-79 on cardiac fibrosis in Zucker diabetic fatty (ZDF) rats. KIOM-79 (50 or 500 mg/kg/day) was orally administered for 13 weeks. AGEs formation and collagen expression in the myocardium were assessed by immunohistochemistry. The expression levels of the receptor for AGEs (RAGE), transforming growth factor-β1 (TGF-β1), collagen IV, fibronectin, urotensin II, and urotensin II receptor were examined in the myocardial tissue of ZDF rats. KIOM-79 treatment at 500 mg/kg inhibited the accumulation of AGEs, reduced RAGE mRNA and protein expression, and reduced the upregulation of cardiac fibrogenic factors, such as fibronectin and collagen IV, in heart of ZDF rats. Additionally, KIOM-79 ameliorated urotensin II/receptor gene expression in the cardiac tissue of ZDF rats. Our findings indicate that KIOM-79 diminishes cardiac fibrosis in ZDF rats by preventing AGEs accumulation and RAGE overexpression and by modulating the cardiac urotensin II/receptor pathway, which decreases the amount of profibrotic factors, such as TGF-β1, fibronectin, and collagen in cardiac tissue.

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28

Hirose, Takuo, Kazuhiro Takahashi, Nobuyoshi Mori, Takashi Nakayama, Masahiro Kikuya, Takayoshi Ohkubo, Masahiro Kohzuki, Kazuhito Totsune, and Yutaka Imai. "Increased expression of urotensin II, urotensin II-related peptide and urotensin II receptor mRNAs in the cardiovascular organs of hypertensive rats: Comparison with endothelin-1." Peptides 30, no. 6 (June 2009): 1124–29. http://dx.doi.org/10.1016/j.peptides.2009.02.009.

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29

Khan, Kashif, Isabella Albanese, Bin Yu, Yousif Shalal, Hamood Al-Kindi, Hossney Alaws, Jean-Claude Tardif, Ophélie Gourgas, Marta Cerutti, and Adel Schwertani. "Urotensin II, urotensin-related peptide, and their receptor in aortic valve stenosis." Journal of Thoracic and Cardiovascular Surgery 161, no. 1 (January 2021): e1-e15. http://dx.doi.org/10.1016/j.jtcvs.2019.09.029.

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30

Khan, K., I. Albanese, B. Yu, A. Hafiane, H. Al-Kindi, R. Cecere, and A. Schwertani. "UROTENSIN II, UROTENSIN-RELATED PEPTIDE AND THEIR RECEPTOR IN AORTIC VALVE STENOSIS." Canadian Journal of Cardiology 34, no. 10 (October 2018): S71. http://dx.doi.org/10.1016/j.cjca.2018.07.307.

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31

Watanabe, Takuya, Tomoko Kanome, Toshiaki Suguro, and Akira Miyazaki. "Human Urotensin II and Metabolic Syndrome." Vascular Disease Prevention 3, no. 1 (December 1, 2008): 91–98. http://dx.doi.org/10.2174/1567270000603010015.

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32

Watanabe, Takuya, Tomoko Kanome, Toshiaki Suguro, and Akira Miyazaki. "Human Urotensin II and Metabolic Syndrome." Vascular Disease Prevention 3, no. 2 (May 1, 2006): 91–98. http://dx.doi.org/10.2174/156727006776819396.

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33

Giuliani, L., L. Lenzini, E. Aldighieri, A. C. Pessina, and G. P. Rossi. "Urotensin II is Overexpressed in Pheochromocytoma." High Blood Pressure & Cardiovascular Prevention 14, no. 3 (2007): 145–96. http://dx.doi.org/10.2165/00151642-200714030-00095.

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34

Maguire, Janet J., and Anthony P. Davenport. "Is urotensin-II the new endothelin?" British Journal of Pharmacology 137, no. 5 (November 2002): 579–88. http://dx.doi.org/10.1038/sj.bjp.0704924.

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35

Richards, A. Mark, and Chris Charles. "Urotensin II in the cardiovascular system." Peptides 25, no. 10 (October 2004): 1795–802. http://dx.doi.org/10.1016/j.peptides.2004.04.017.

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36

Mark Richards, A., M. Gary Nicholls, John G. Lainchbury, Stephen Fisher, and Timothy G. Yandle. "Plasma urotensin II in heart failure." Lancet 360, no. 9332 (August 2002): 545–46. http://dx.doi.org/10.1016/s0140-6736(02)09709-x.

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37

Guidolin, Diego, Giovanna Albertin, and Domenico Ribatti. "Urotensin-II as an angiogenic factor." Peptides 31, no. 6 (June 2010): 1219–24. http://dx.doi.org/10.1016/j.peptides.2010.03.022.

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38

Jin, Jian, and Stephen A. Douglas. "Non-peptidic urotensin-II receptor modulators." Expert Opinion on Therapeutic Patents 16, no. 4 (March 24, 2006): 467–79. http://dx.doi.org/10.1517/13543776.16.4.467.

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39

Vaudry, Hubert, Jean-Claude Do Rego, Jean-Claude Le Mevel, David Chatenet, Hervé Tostivint, Alain Fournier, Marie-Christine Tonon, Georges Pelletier, J. Michael Conlon, and Jérôme Leprince. "Urotensin II, from fish to human." Annals of the New York Academy of Sciences 1200, no. 1 (July 2010): 53–66. http://dx.doi.org/10.1111/j.1749-6632.2010.05514.x.

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40

Ong, Kwok-Leung, Bernard M. Y. Cheung, and Karen Siu-Ling Lam. "Urotensin II and the Circulatory System." Hong Kong Journal of Nephrology 7, no. 1 (April 2005): 9–13. http://dx.doi.org/10.1016/s1561-5413(09)60174-5.

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41

Lehmann, Fredrik, Erika A. Currier, Roger Olsson, Uli Hacksell, and Kristina Luthman. "Isochromanone-based urotensin-II receptor agonists." Bioorganic & Medicinal Chemistry 13, no. 8 (April 2005): 3057–68. http://dx.doi.org/10.1016/j.bmc.2005.01.056.

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42

Zhong, Huan, Yu He, Zhi-Li Tan, and Liang-Ming Liu. "Effect of urotensin II/urotensin II receptor system on autophagy in acute liver failure in mice." World Chinese Journal of Digestology 26, no. 4 (2018): 228. http://dx.doi.org/10.11569/wcjd.v26.i4.228.

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43

Mori, Masaaki, and Masahiko Fujino. "Urotensin II-related peptide, the endogenous ligand for the urotensin II receptor in the rat brain." Peptides 25, no. 10 (October 2004): 1815–18. http://dx.doi.org/10.1016/j.peptides.2004.06.025.

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44

Sugo, Tsukasa, Yuko Murakami, Yukio Shimomura, Mioko Harada, Michiko Abe, Yoshihiro Ishibashi, Chieko Kitada, et al. "Identification of urotensin II-related peptide as the urotensin II-immunoreactive molecule in the rat brain." Biochemical and Biophysical Research Communications 310, no. 3 (October 2003): 860–68. http://dx.doi.org/10.1016/j.bbrc.2003.09.102.

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Hassan, Ghada S., Fazila Chouiali, Takayuki Saito, Fu Hu, Stephen A. Douglas, Zhaohui Ao, Robert N. Willette, Eliot H. Ohlstein, and Adel Giaid. "Effect of human urotensin-II infusion on hemodynamics and cardiac function." Canadian Journal of Physiology and Pharmacology 81, no. 2 (February 1, 2003): 125–28. http://dx.doi.org/10.1139/y03-004.

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Abstract:

Recent studies have shown that the vasoactive peptide urotensin-II (U-II) exerts a wide range of action on the cardiovascular system of various species. In the present study, we determined the in vivo effects of U-II on basal hemodynamics and cardiac function in the anesthetized intact rat. Intravenous bolus injection of human U-II resulted in a dose-dependent decrease in mean arterial pressure and left ventricular systolic pressure. Cardiac contractility represented by ±dP/dt was decreased after injection of U-II. However, there was no significant change in heart rate or diastolic pressure. The present study suggests that upregulation of myocardial U-II may contribute to impaired myocardial function in disease conditions such as congestive heart failure.Key words: urotensin-II, rat, infusion, heart.

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Gong, Hui, Yan-Xia Wang, Yi-Zhun Zhu, Wen-Wei Wang, Ming-Jie Wang, Tai Yao, and Yi-Chun Zhu. "Cellular distribution of GPR14 and the positive inotropic role of urotensin II in the myocardium in adult rat." Journal of Applied Physiology 97, no. 6 (December 2004): 2228–35. http://dx.doi.org/10.1152/japplphysiol.00540.2004.

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Abstract:

Urotensin II is a cyclic neuropeptide recently shown to play a role via its receptor GPR14 in regulating vascular tone in the mammalian cardiovascular system. The existence of GPR14 in rat heart has been validated by ligand binding assay and RT-PCR. In the present study, we investigated the cellular distribution of GPR14 protein in rat heart by using immunohistochemistry and confocal microscopic immunofluorescence double staining with antipeptide polyclonal antibodies against GPR14 and cell type markers for myocytes and endothelial cells. The direct effect of urotensin II on left ventricular contractility was further evaluated in isolated left ventricular papillary muscles of the rat. In paraffin-embedded heart sections, positive immunohistochemical staining was observed in the left ventricle but not in the right ventricle and atria. Immunofluorescence double staining revealed the cardiac myocyte as the only cell type expressing GPR14 protein in frozen heart sections as well as in isolated cardiac myocytes. There was no visible signal for GPR14 in intramyocardial coronary arteries and capillaries. The existence of GPR14 protein in rat heart was further validated by immunoprecipitation and Western blot analysis. In isolated rat left ventricular papillary muscle preparations, urotensin II induced an increase in active contractile force. GPR14 mRNA was also detected in rat heart by RT-PCR. These data provide the first direct evidence for the cellular localization of GPR14 receptor protein and a positive inotropic effect of urotensin II in normal rat heart.

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Parmentier, Caroline, Emilie Hameury, Isabelle Lihrmann, Jacques Taxi, Hélène Hardin-Pouzet, Hubert Vaudry, André Calas, and Hervé Tostivint. "Comparative distribution of the mRNAs encoding urotensin I and urotensin II in zebrafish." Peptides 29, no. 5 (May 2008): 820–29. http://dx.doi.org/10.1016/j.peptides.2008.01.023.

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Chatenet, David, Christophe Dubessy, Cédric Boularan, Elizabeth Scalbert, Bruno Pfeiffer, Pierre Renard, Isabelle Lihrmann, et al. "Structure−Activity Relationships of a Novel Series of Urotensin II Analogues: Identification of a Urotensin II Antagonist." Journal of Medicinal Chemistry 49, no. 24 (November 2006): 7234–38. http://dx.doi.org/10.1021/jm0602110.

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Boivin, Stéphane, Isabelle Ségalas-Milazzo, Laure Guilhaudis, Hassan Oulyadi, Alain Fournier, and Daniel Davoust. "Solution structure of urotensin-II receptor extracellular loop III and characterization of its interaction with urotensin-II." Peptides 29, no. 5 (May 2008): 700–710. http://dx.doi.org/10.1016/j.peptides.2008.02.024.

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Nishi, Mina, Kiyoaki Yonesu, Hideki Tagawa, Mikio Kato, Shinji Marumoto, and Takahiro Nagayama. "A Novel and Highly Potent Urotensin II Receptor Antagonist Inhibits Urotensin II–Induced Pressure Response in Mice." Journal of Cardiovascular Pharmacology 73, no. 1 (January 2019): 15–21. http://dx.doi.org/10.1097/fjc.0000000000000618.

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