Neuromedin U octapeptide alters ion transport in porcine jejunum

Brown, David R.; Quito, Francis L.

doi:10.1016/0014-2999(88)90415-3

Cited by 73 publications

(46 citation statements)

References 6 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The functions of PRXa peptides known thus far in the vertebrates include activation of ion transport and contractile activity in intestine and arterial musculature via the NMUR (40,41,42). In invertebrates, functions for many of the PRXamide peptides remain uncertain, biological activity having been inferred from standard assays for visceral muscle contraction.…”

Section: Drosophila Gpcrs In the Nmur Group Are Activated By Prxa Pepmentioning

confidence: 99%

Identification of G protein-coupled receptors for Drosophila PRXamide peptides, CCAP, corazonin, and AKH supports a theory of ligand-receptor coevolution

Park

Kim

Adams

2002

Proc. Natl. Acad. Sci. U.S.A.

353

273

View full text Add to dashboard Cite

G-protein coupled receptors (GPCRs) are ancient, ubiquitous sensors vital to environmental and physiological signaling throughout organismal life. With the publication of the Drosophila genome, numerous “orphan” GPCRs have become available for functional analysis. Here we characterize two groups of GPCRs predicted as receptors for peptides with a C-terminal amino acid sequence motif consisting of −PRXamide (PRXa). Assuming ligand-receptor coevolution, two alternative hypotheses were constructed and tested. The insect PRXa peptides are evolutionarily related to the vertebrate peptide neuromedin U (NMU), or are related to arginine vasopressin (AVP), both of which have PRXa motifs. Seven Drosophila GPCRs related to receptors for NMU and AVP were cloned and expressed in Xenopus oocytes for functional analysis. Four Drosophila GPCRs in the NMU group (CG11475, CG8795, CG9918, CG8784) are activated by insect PRXa pyrokinins, (−FXPRXamide), Cap2b-like peptides (−FPRXamide), or ecdysis triggering hormones (−PRXamide). Three Drosophila GPCRs in the vasopressin receptor group respond to crustacean cardioactive peptide (CCAP), corazonin, or adipokinetic hormone (AKH), none of which are PRXa peptides. These findings support a theory of coevolution for NMU and Drosophila PRXa peptides and their respective receptors

show abstract

Section: Drosophila Gpcrs In the Nmur Group Are Activated By Prxa Pepmentioning

confidence: 99%

Identification of G protein-coupled receptors for Drosophila PRXamide peptides, CCAP, corazonin, and AKH supports a theory of ligand-receptor coevolution

Park

Kim

Adams

2002

Proc. Natl. Acad. Sci. U.S.A.

353

273

View full text Add to dashboard Cite

show abstract

“…Neuromedin U-8 was found to be ineffective in producing contractions of the guinea-pig ileum or porcine jejunum (Minamino et al, 1985;Brown & Quito, 1988) while it affected markedly intestinal ion transport (Brown & Quito, 1988) and splanchnic circulation (Sumi et al, 1987). On the basis of these results, it could be hypothesized that neuromedin U-8 is not a motor transmitter in the gut, being selectively involved in other functions.…”

Section: Discussionmentioning

confidence: 98%

“…In both studies, neuromedin U-25 was more potent than neuromedin U-8, indicating that the C-terminal sequence is probably responsible for the biological activity, whose expression is facilitated in the extended form of the peptide. More recently, Brown & Quito (1988) found that neuromedin U-8 affects ion transport in porcine jejunal mucosa via a neural mechanism while having no effect on motility of pig isolated jejunal muscle. The absence of a motor response to neuromedins U-8 and U-25 was also described by Minamino et al (1985) in the guinea-pig isolated ileum.…”

Section: Introductionmentioning

confidence: 99%

Motor response of the human isolated small intestine and urinary bladder to porcine neuromedin U‐8

Maggi

Patacchini

Giuliani

et al. 1990

British J Pharmacology

View full text Add to dashboard Cite

1Porcine neuromedin U-8 produced a concentration (0.3 nM-1 pM)-dependent contraction of the longitudinal muscle of the human isolated ileum, which was unaffected by either atropine (1 pM) or tetrodotoxin (1 pM). 2 By contrast, neuromedin U-8 had only a weak effect on the circular muscle of the human isolated ileum. 3 Neuromedin U-8 also produced a concentration-dependent contraction of mucosa-free muscle strips from the dome of the human isolated urinary bladder, its action being unaffected by either atropine or tetrodotoxin. 4 These findings indicate that neuromedin U-8 exerts a direct contractile effect on smooth muscle of the human intestinal and urinary tract.

show abstract

“…NmU-8 and NmU-25 cause potent and selective reduction of splanchnic blood flow in the dog and rat (26,27), and NmU-8 alters ion transport in porcine jejunum by a noncholinergic, neuronal mechanism (28). A variety of motor responses have been reported to be mediated by NmU in the gastrointestinal tract of several different species (28,29) and between longitudinal and circular muscle of particular tissues (30). NmU may also exert a direct and indirect effect on the regulation of growth, structure, and function of the adrenal cortex (31)(32)(33).…”

mentioning

confidence: 99%

“…NmU peptides have been shown to be potent stimulators of uterine smooth muscle contraction in vitro (15) and to exert a marked hypertensive effect in rats when administered systemically (25). NmU-8 and NmU-25 cause potent and selective reduction of splanchnic blood flow in the dog and rat (26,27), and NmU-8 alters ion transport in porcine jejunum by a noncholinergic, neuronal mechanism (28). A variety of motor responses have been reported to be mediated by NmU in the gastrointestinal tract of several different species (28,29) and between longitudinal and circular muscle of particular tissues (30).…”

mentioning

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

View full text Add to dashboard Cite

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.

show abstract

Neuromedin U octapeptide alters ion transport in porcine jejunum

Cited by 73 publications

References 6 publications

Identification of G protein-coupled receptors for Drosophila PRXamide peptides, CCAP, corazonin, and AKH supports a theory of ligand-receptor coevolution

Identification of G protein-coupled receptors for Drosophila PRXamide peptides, CCAP, corazonin, and AKH supports a theory of ligand-receptor coevolution

Motor response of the human isolated small intestine and urinary bladder to porcine neuromedin U‐8

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

Contact Info

Product

Resources

About