Primary structure and pharmacological activity of a nonapeptide related to neuromedin U isolated from chicken intestine

O’Harte, Finbarr; Bockman, Charles S.; Zeng, Wanyun; Abel, Peter W.; Harvey, Steven; Conlon, J. Michael

doi:10.1016/0196-9781(91)90138-f

Cited by 45 publications

(21 citation statements)

References 11 publications

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“…The frog peptide was approximately 10.9 times more potent on a molar basis when compared with porcine NmU-8. The latter peptide produced similar EC 50 values to those reported previously (16 Ϯ 5 nM (22); 46 Ϯ 8 nM (38)). In addition, the IC 50 value obtained for inhibition of monoradioiodinated rat NmU binding to rat uterine membrane preparations (60 nM) was of a similar magnitude to that previously reported (35)).…”

Section: Discussionsupporting

confidence: 76%

“…Frog skin NmU-23 has the same number of amino acid residues within its sequence as rat NmU-23; however, the two analogs differ in that the frog peptide is attenuated by two N-terminal amino acid residues, whereas two amino acid deletions have apparently occurred within the central domain of the rat peptide (17,18). Most members of the NmU family have a putative dibasic or monobasic amino acid residue cleavage site at positions 16 and 17, which in some species leads to the endogenous generation of an N-terminally truncated molecular variant containing the C-terminal active core of the peptide (15,22,38). Frog NmU-23 and rat NmU-23 are unique in that they lack this putative site, and therefore it is probable that they exist only as the elongated form.…”

Section: Discussionmentioning

confidence: 99%

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Isolation, Structural Characterization, and Bioactivity of a Novel Neuromedin U Analog from the Defensive Skin Secretion of the Australasian Tree Frog, Litoria caerulea

Salmon¹,

Johnsen²,

Bienert³

et al. 2000

Journal of Biological Chemistry

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We report the isolation of a novel bioactive peptide, neuromedin U-23 (NmU-23), from the defensive skin secretion of the Australasian tree frog, Litoria caerulea. The primary structure of the peptide was established by a combination of microsequencing, mass spectroscopy and site-directed antiserum immunoreactivity as SDEEVQVPGGVISNGYFLFRPRN-amide (M r 2580.6). A synthetic replicate of frog NmU-23 displaced monoradioiodinated rat NmU-23 from uterine membranes in a dose-dependent fashion indistinguishable from nonisotopically labeled rat NmU-23. In a rat uterine smooth muscle strip preparation, synthetic frog NmU-23 produced dose-dependent contractions identical to porcine NmU-25. However, in a preparation of human urinary bladder muscle strip, the synthetic frog peptide was more potent than porcine NmU-25 in eliciting contraction and produced desensitization of the preparation to the latter peptide. This report demonstrates that the defensive skin secretion of a frog contains a novel peptide exhibiting a high degree of primary structural similarity to the endogenous vertebrate peptide, NmU, and that this frog skin analog displays biological activity in mammalian tissues.

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Section: Discussionsupporting

confidence: 76%

Section: Discussionmentioning

confidence: 99%

Isolation, Structural Characterization, and Bioactivity of a Novel Neuromedin U Analog from the Defensive Skin Secretion of the Australasian Tree Frog, Litoria caerulea

Salmon¹,

Johnsen²,

Bienert³

et al. 2000

Journal of Biological Chemistry

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“…NmU is usually present in different species as peptides 8 or 25 amino acids long (NmU-8 and NmU-25, respectively), although other forms also exist (1)(2)(3)(4). These forms are generated from a longer precursor protein, cleaved by as-yet-unknown proteases (5 ).…”

Section: Structurementioning

confidence: 99%

“…The human and rat precursor protein is 174 amino acids long and includes a 34 -amino acid signal peptide, indicating it is secreted. The existence of alternative forms was predicted from the study of putative proteolytic sites along the NmU precursor sequence, which revealed a second peptide derived from the neuromedin U (NMU) 3 gene, termed proNMU 104 -136 . This longer form has shown activity that affects feeding behavior, body weight, and metabolic activity in mice (6 ).…”

Section: Structurementioning

confidence: 99%

Neuromedin U: A Multifunctional Neuropeptide with Pleiotropic Roles

2015

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BACKGROUND Neuromedin U (NmU) belongs to the neuromedin family, comprising a series of neuropeptides involved in the gut–brain axis and including neuromedins B and C (bombesin-like), K (neurokinin B), L (neurokinin A or neurotensin), N, S, and U. CONTENT Although initially isolated from porcine spinal cord on the basis of their ability to induce uterine smooth muscle contraction, these peptides have now been found to be expressed in several different tissues and have been ascribed numerous functions, from appetite regulation and energy balance control to muscle contraction and tumor progression. NmU has been detected in several species to date, particularly in mammals (pig, rat, rabbit, dog, guinea pig, human), but also in amphibian, avian, and fish species. The NmU sequence is highly conserved across different species, indicating that this peptide is ancient and plays an important biological role. Here, we summarize the main structural and functional characteristics of NmU and describe its many roles, highlighting the jack-of-all-trades nature of this neuropeptide. SUMMARY NmU involvement in key processes has outlined the possibility that this neuropeptide could be a novel target for the treatment of obesity and cancer, among other disorders. Although the potential for NmU as a therapeutic target is obvious, the multiple functions of this molecule should be taken into account when designing an approach to targeting NmU and/or its receptors.

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“…Neuromedin U (NMU) is a highly conserved brain-gut peptide that was first isolated from the porcine spinal cord (Minamino et al 1985) and later from the brain, spinal cord, and intestine of other species (Domin et al 1986, 1989, O'Harte et al 1991, Austin et al 1995. Thus far, the only known physiological role of NMU is contraction of smooth muscles in blood vessels, the uterus, and the gastrointestinal tract (Minamino et al 1985).…”

Section: Introductionmentioning

confidence: 99%

Comparison of feeding suppression by the anorexigenic hormones neuromedin U and neuromedin S in rats

Nakahara

Katayama

Maruyama³

et al. 2010

Journal of Endocrinology

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We compared the central mechanisms of feeding suppression by the anorexigenic hormones neuromedin U (NMU) and neuromedin S (NMS) in rats. I.c.v. injection of either NMU or NMS dose dependently decreased 3-h food intake during the first quarter of a dark period. Pretreatment involving i.c.v. injection of a specific anti-NMS IgG blocked the suppression of food intake induced by i.c.v.-and i.p.-injected leptin, but anti-NMU IgG elicited no blockade. Quantitative PCR analysis revealed that i.c.v. injection of NMU or NMS caused a dose-dependent increase in CRH and proopiomelanocortin mRNA expression in the paraventricular nucleus (PVN) and arcuate nucleus (Arc) respectively. In tissue cultures of the Arc, secretion of a-melanocyte-stimulating hormone was stimulated by NMU and NMS, with more potent stimulation by NMS. The time-course curves of the increase in neuronal firing rate in Arc slices in response to NMU and NMS showed almost the same pattern, with a peak 10-15 min after treatment, whereas the time-course curves for the PVN slices differed between NMU and NMS. These results suggest that NMS and NMU may share anorexigenic effects, depending on physiological conditions.

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Primary structure and pharmacological activity of a nonapeptide related to neuromedin U isolated from chicken intestine

Cited by 45 publications

References 11 publications

Isolation, Structural Characterization, and Bioactivity of a Novel Neuromedin U Analog from the Defensive Skin Secretion of the Australasian Tree Frog, Litoria caerulea

Isolation, Structural Characterization, and Bioactivity of a Novel Neuromedin U Analog from the Defensive Skin Secretion of the Australasian Tree Frog, Litoria caerulea

Neuromedin U: A Multifunctional Neuropeptide with Pleiotropic Roles

Comparison of feeding suppression by the anorexigenic hormones neuromedin U and neuromedin S in rats

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