Post‐translational processing of prepro‐urotensin II

Conlon, J. Michael; Arnold-Reed, Diane; Balment, R. J.

doi:10.1016/0014-5793(90)81500-n

Cited by 48 publications

(23 citation statements)

References 14 publications

(19 reference statements)

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“…This sequence varied slightly from that obtained in a previous study (28), but this variation was attributed to alternative splicing. The mature hUII was found to be the same in both experiments: an 11-amino acid protein (ETPDCFWKTCV) with a cyclic six amino acid sequence identical to that previously described in fish species (27). Although the sources of UII production in the body remain to be fully unraveled, arteriovenous gradients exist across the heart (36%), liver (40%), and kidney (44%) in anesthetized sheep (21), indicating that these organs may be primary producers of UII.…”

supporting

confidence: 65%

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Role of urotensin II in health and disease

Ross

McKendy

Giaid

2010

American Journal of Physiology-Regulatory, Integrative and Comp

126

107

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Urotensin II (UII) is an 11 amino acid cyclic peptide originally isolated from the goby fish. The amino acid sequence of UII is exceptionally conserved across most vertebrate taxa, sharing structural similarity to somatostatin. UII binds to a class of G protein-coupled receptor known as GPR14 or the urotensin receptor (UT). UII and its receptor, UT, are widely expressed throughout the cardiovascular, pulmonary, central nervous, renal, and metabolic systems. UII is generally agreed to be the most potent endogenous vasoconstrictor discovered to date. Its physiological mechanisms are similar in some ways to other potent mediators, such as endothelin-1. For example, both compounds elicit a strong vascular smooth muscle-dependent vasoconstriction via Ca 2ϩ release. UII also exerts a wide range of actions in other systems, such as proliferation of vascular smooth muscle cells, fibroblasts, and cancer cells. It also 1) enhances foam cell formation, chemotaxis of inflammatory cells, and inotropic and hypertrophic effects on heart muscle; 2) inhibits insulin release, modulates glomerular filtration, and release of catecholamines; and 3) may help regulate food intake and the sleep cycle. Elevated plasma levels of UII and increased levels of UII and UT expression have been demonstrated in numerous diseased conditions, including hypertension, atherosclerosis, heart failure, pulmonary hypertension, diabetes, renal failure, and the metabolic syndrome. Indeed, some of these reports suggest that UII is a marker of disease activity. As such, the UT receptor is emerging as a promising target for therapeutic intervention. Here, a concise review is given on the vast physiologic and pathologic roles of UII.UT receptor; somatostatin; human; experimental animals; autocrine/paracrine UROTENSIN II (UII) was initially isolated from the urophysis of the goby fish (Gillichthys mirabilis) (97). The peptide was subsequently isolated from the white sucker (Catostomus commersoni) and the carp (Cyprinus carpio). Although there were variations in the amino acid sequence near the amino terminus, in both species the UII molecule retained the COOH-terminal cyclic sequence: -Cys

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confidence: 65%

“…Although there were variations in the amino acid sequence near the amino terminus, in both species the UII molecule retained the COOH-terminal cyclic sequence: -Cys 1). It is this sequence, similar to somatostatin, particularly in the biologically active region, that is thought to confer the peptide its biological activity (27).…”

mentioning

confidence: 99%

Role of urotensin II in health and disease

Ross

McKendy

Giaid

2010

American Journal of Physiology-Regulatory, Integrative and Comp

126

107

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“…AngII and losartan were co-administered to the piglets w10 min after intrarenal arterial bolus injection of losartan Ross et al 2010, Tsoukas et al 2011. However, the cyclic hexapeptide sequence in UII carboxyl-terminus, which is responsible for its biological activity, is highly conserved between species (Itoh et al 1987, Conlon et al 1990, Coulouarn et al 1998, Douglas et al 2004. Hence, it is unlikely that the physiological function of UII is dependent on its source .…”

Section: Discussionmentioning

confidence: 99%

Pressor and renal regional hemodynamic effects of urotensin II in neonatal pigs

Soni¹,

Adebiyi²

2013

Journal of Endocrinology

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Renal expression of the peptide hormone urotensin II (UII) and its receptor (UTR) are dependent on kidney maturation and anatomical regions. However, renal regional hemodynamic effects of UII in neonates are unclear. Here, we investigated regional hemodynamic responses to acute intrarenal arterial administration of UII in newborn pigs. Western immunoblotting and immunofluorescence confirmed UTR expression and membrane localization in newborn pig renal afferent arterioles and afferent arteriolar smooth muscle cells respectively. Intrarenal arterial bolus injections of human UII (hUII; 1-100 ng/kg) resulted in a dose-dependent decrease in total renal blood flow (RBF) and an increase in mean arterial pressure (MAP) and renal vascular resistance (RVR) in newborn pigs. Moreover, hUII dose dependently reduced cortical blood flow (CBF) but increased medullary blood flow (MBF) in the piglets. hUII-induced MAP elevation and hemodynamic changes were inhibited by urantide, a UTR antagonist, but not losartan, a type 1 angiotensin II receptor antagonist. U-73122, a phospholipase C (PLC) inhibitor, and 2-aminoethoxydiphenyl borate, an inositol 1,4,5 trisphosphate (IP 3 ) receptor antagonist, attenuated hUII-induced MAP and RVR elevations, RBF and CBF reductions, but not MBF increase. These findings indicate that intrarenal arterial administration of hUII elevates blood pressure and induces region-selective renal hemodynamic changes in newborn pigs. Our data also suggest that the PLC/IP 3 signaling pathway contributes to hUII-induced alterations in MAP, RBF, RVR, and CBF but not MBF in newborn pigs.

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“…The amino acid sequence of UII has been determined in dogfish (Conlon et al, 1992a), flounder (Conlon et al, 1990), frog (Conlon et al, 1992b), and pig (Mori et al, 1999) confirming that the peptide is generated through cleavage at the Arg…”

Section: E Structure Of the Urotensin II And Urotensin Ii-related Pementioning

confidence: 92%