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Query: UNIPROT:P01185 (vasopressin)
 23,126 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effects of a novel vasopressin (AVP) fragment analog NC-1900 (pGlu-Asn-Ser-Pro-Arg-Gly-NH2 acetate) were studied on the performance of memory retention and retrieval in mice. NC-1900 of one time application of 1 hr after the acquired trial (electric shock) extended the latent period of passive avoidance task 21 days after the acquired trial. Though the extended response was also recognized with AVP4-9, the potency was approx. 1/1000 of NC-1900. The potentiation wasn't recognized with vasopressin. NC-1900 showed a significantly high correct answer after 21 days after the last trial in the search task. While, V1 antagonist Pmp1-Tyr (Me)2-AVP shortened the latent period of passive avoidance task. On the other hand, NC-1900 extended the reaction latency 21 days after the acquired trial by the application 1 hr before the retention trial. Though this improvement of memory retrieval was recognized with vasopressin and AVP4-9, the potency was 1/100-1/1000. NC-1900 improved the retrieval 24 h after the CO2 exposure. V1 antagonists Pmp1-Tyr-Me2-AVP or Deamino-Pen1, O-Me-Tyr2-AVP, and PMA had no effects on the retrieval 21 days after the acquired trial. These results suggest that NC-1900 may have the memory retention and retrieval potentiating action, and that phospholipase C-protein kinase C system may be involved in the former action, and the latter action not be involved.
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PMID:[The improvement of memory retention and retrieval of a novel vasopressin fragment analog NC-1900]. 1249 80

The mechanism by which NC-1900, a new pGlu-Asn-Cys(Cys)-Pro-Arg-Gly-NH(2) (AVP(4-9)) analog, improves spatial memory in rats using an eight-arm radial maze was examined. Even at very low doses (0.2 ng/kg for s.c., 1 microg/kg for p.o., 1 fg for i.c.v.) NC-1900 improved scopolamine-induced impairment of spatial memory. NC-1900 (1 ng/kg, s.c.) also improved impairment of spatial memory induced by pirenzepine, a muscarinic(1) (M(1)) receptor antagonist, and by KN-62, a Ca2+/calmodulin (CaM)-dependent protein kinase II inhibitor. [Pmp(1), Tyr(Me)(2)]-Arg(8)-vasopressin, a vasopressin(1A) (V(1A)) receptor antagonist, and nicardipine, L-type Ca2+ blocker, but not OPC-31260, a V(2) antagonist, suppressed the effect of NC-1900 on scopolamine-induced impairment of spatial memory. A microdialysis study showed that NC-1900 did not affect acetylcholine release in the ventral hippocampus (VH) of intact rats or of scopolamine-treated rats. NC-1900 (1 microM) increased [Ca2+](i) in the VH than in the dorsal hippocampus (DH). Pretreatment with nicardipine (1 microM) and Ca2+ -free conditions inhibited the NC-1900-induced [Ca2+](i) response in the VH. Whereas co-administration of NC-1900 (1 microM) and carbachol (500 microM) increased [Ca2+](i) in the VH. Moreover, nicardipine concentration-dependently inhibited the increase in [Ca2+](i) induced by the co-administration of NC-1900 and carbachol in the VH. These results suggest that NC-1900 activates the V(1A) receptor at the postsynaptic cholinergic nerve, and causes a transient influx of intracellular Ca2+ through L-type Ca2+ channels, to interact with the M(1) receptor. The activation of these Ca2+ -dependent processes induced by NC-1900 may be involved in the positive effect of NC-1900 on scopolamine-induced impairment of spatial memory.
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PMID:Ameliorative effect of NC-1900, a new AVP4-9 analog, through vasopressin V1A receptor on scopolamine-induced impairments of spatial memory in the eight-arm radial maze. 1264 91

Some analogues of arginine vasopressin (AVP) reportedly possess hypotensive properties, and two such peptides are Cys(1)-Tyr(2)-Phe(3)-Val(4)-Asn(5)-Cys(6)-Pro(7)- d-Arg(8)-Gly(9)-NH(2) (VD-AVP) and d(CH(2))(5)-Cys(1)- d-Tyr(Et)(2)-Arg(3)-Val(4)-Asn(5)-Cys(6)-Lys(7)-Lys(8)-ethylenediamine(9) (TA-LVP). In the present investigation we examined the effects of TA-LVP (0.3, 1.0 and 3.0 microg/kg/min), VD-AVP (0.3, 1.0 and 3.0 microg/kg/min) and AVP (1.0, 3.0, 10 ng/kg/min) on haemodynamics, blood volume (BV) and plasma troponin levels in anaesthetised rats. Infusion of TA-LVP significantly ( P<0.05) reduced blood pressure (-45+/-3%; n=8; mean +/- SEM), mean circulatory filling pressure ( P(mcf); -41+/-3%), and cardiac output (CO; -59+/-4%). The reduction in CO at a lower dose of TA-LVP was due to reduced venous tone, while at higher doses the reduction was predominantly the result of reduced BV (-35+/-4%). The large decrease in BV during the infusion of TA-LVP, substantially increased resistance to venous return (50+/-11%), which was the main contributor in reducing CO. Administration of AVP significantly increased blood pressure (41+/-4%) and arterial resistance (98+/-16%) without any impact on P(mcf) and BV, while significantly reducing CO (-26+/-5%). Infusion of VD-AVP did not produce hypotension, but produced a modest but significant reduction in CO (-18+/-5%) and insignificant but moderate increases in peripheral resistance (30+/-12%) and resistance to venous return (28+/-8%). Plasma troponin levels were not affected by any of the peptides. The hypotensive action of TA-LVP was due to a reduction in CO as a result of a reduced pre-load, while the pressor effect of AVP increased after-load sufficiently to impede flow, reducing CO. VD-AVP was devoid of any hypotensive effects, suggesting that V(2)-vasopressin receptors are most likely to play a limited role in the control of cardiac and vascular function in these animals.
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PMID:A comparison between haemodynamic effects of vasopressin analogues. 1552 9

Little is known about endoplasmic reticulum (ER) export signals, particularly those of members of the G-protein-coupled receptor family. We investigated the structural motifs involved in membrane export of the human pituitary vasopressin V1b/V3 receptor. A series of V3 receptors carrying deletions and point mutations were expressed in AtT20 corticotroph cells. We analyzed the export of these receptors by monitoring radioligand binding and by analysis of a V3 receptor tagged with both green fluorescent protein and Myc epitopes by a novel flow cytometry-based method. This novel method allowed us to quantify total and membrane-bound receptor expression. Receptors lacking the C terminus were not expressed at the cell surface, suggesting the presence of an export motif in this domain. The distal C terminus contains two di-acidic (DXE) ER export motifs; however, mutating both these motifs had no effect on the V3 receptor export. The proximal C terminus contains a di-leucine (345)LL(346) motif surrounded by the hydrophobic residues Phe(341), Asn(342), and Leu(350). The mutation of one or more of these five residues abolished up to 100% of the receptor export. In addition, these mutants colocalized with calnexin, demonstrating that they were retained in the ER. Finally, this motif was sufficient to confer export properties on a CD8alpha glycoprotein-V3 receptor chimera. In conclusion, we have identified a novel export motif, FN(X)(2)LL(X)(3)L, in the C terminus of the V3 receptor.
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PMID:A novel C-terminal motif is necessary for the export of the vasopressin V1b/V3 receptor to the plasma membrane. 1552 11

We designed and synthesized new photoactivatable linear vasopressin analogues containing benzophenone photophores. All compounds were monitored and purified using RP-HPLC and characterized by mass spectrometry. Affinity and selectivity were determined in CHO cells expressing either human V(1a), V(1b) or V(2) receptor subtypes. Within the series, compounds 6 (PhCH(2)CO-lBpa-Phe-Gln-Asn-Arg-Pro-Arg-Tyr(3I)-NH(2)) and 9 (PhCH(2)CO-dBpa-Phe-Gln-Asn-Arg-Pro-Arg-Tyr(3I)-NH(2)), containing a benzoylphenylalanine residue (Bpa), were selected and their antagonistic properties determined (K(inact) = 1.87 and 0.35 nM, respectively). The dissociation constant of the most potent candidate (compound 9) was further calculated from saturation experiments using the (125)I derivative (K(d) = 0.07 +/- 0.01 nM). Photolabeling experiments using radioactive compound 9 as a probe were specific and UV-dependent and allowed the identification of two bands at molecular masses around 85-90 kDa and 46 kDa, respectively, as previously described by Phalipou et al., using two photoreactive linear azidopeptide antagonists. The results suggest therefore that compound 9 is a potent new tool for the accurate mapping of the human V(1a) receptor antagonist binding site.
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PMID:Design of benzophenone-containing photoactivatable linear vasopressin antagonists: pharmacological and photoreactive properties. 1585 44

An unusual crustacean cardioactive peptide (CCAP) from the pericardial organs of the shore crab Carcinus maenas has been purified to homogeneity by a two-step reversed-phase HPLC procedure. Manual microsequencing using the 4-(N,N-dimethylamino)azobenzene 4'-isothiocyanate/phenylisothiocyanate double-coupling technique and automated gas-phase sequencing of the oxidized peptide revealed that CCAP is a nonapeptide (M(r) 957) of the sequence Pro-Phe-[unk]Cys-Asn-Ala-Phe-Thr-Gly-Cys-NH(2). We have confirmed the sequence by chemical synthesis of the C-terminally amidated and nonamidated forms of the peptide. The presence of the amide group was indicated by lack of susceptibility to carboxypeptidase A and Y treatment and was confirmed by the observation that the native CCAP comigrated with the amidated synthetic peptide on HPLC. Native and synthetic CCAP displayed high accelerating activity on a semi-isolated crab heart preparation, whereas the nonamidated synthetic peptide was of much lower potency. The effect of CCAP was both inoand chronotropic. The two pericardial organs of one animal yielded 30-40 pmol of extractable CCAP. Its sequence does not resemble that of any known neuropeptide. However, a "mirror-image" similarity to vasopressin is conspicuous.
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PMID:Unusual cardioactive peptide (CCAP) from pericardial organs of the shore crab Carcinus maenas. 1659 3

The vasopressin-regulated urea transporter (UT)-A1 is a transmembrane protein with two glycosylated forms of 97 and 117 kDa; both are derived from a single 88-kDa core protein. However, the precise molecular sites and the function for UT-A1 N-glycosylation are not known. In this study, we compared Madin-Darby canine kidney cells stably expressing wild-type (WT) UT-A1 to Madin-Darby canine kidney cell lines stably expressing mutant UT-A1 lacking one (A1m1, A1m2) or both glycosylation sites (m1m2). Site-directed mutagenesis revealed that UT-A1 has two glycosylation sites at Asn-279 and -742. Urea flux is stimulated by 10 nM vasopressin (AVP) or 10 microM forskolin (FSK) in WT cells. In contrast, m1m2 cells have a delayed and significantly reduced maximal urea flux. A 15-min treatment with AVP and FSK significantly increased UT-A1 cell surface expression in WT but not in m1m2 cells, as measured by biotinylation. We confirmed this finding using immunostaining. Membrane fractionation of the plasma membrane, Golgi, and endoplasmic reticulum revealed that AVP or FSK treatment increases UT-A1 abundance in both Golgi and plasma membrane compartments in WT but not in m1m2 cells. Pulse-chase experiments showed that UT-A1 half-life is reduced in m1m2 cells compared with WT cells. Our results suggest that mutation of the N-linked glycosylation sites reduces urea flux by reducing UT-A1 half-life and decreasing its accumulation in the apical plasma membrane. In vivo, inner medullary collecting duct cells may regulate urea uptake by altering UT-A1 glycosylation in response to AVP stimulation.
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PMID:Loss of N-linked glycosylation reduces urea transporter UT-A1 response to vasopressin. 1684 33

As a hormone, vasopressin binds to three distinct receptors: V1a and V1b receptors, which induce phospholipase-Cbeta (PLCbeta) activation and Ca2+ mobilization; and V2 receptors, which are coupled to adenylyl cyclase. V1a and V1b receptors are also present in neurons. In particular, hypoglossal (XII) and facial (VII) motoneurons are excited following vasopressin-V1a receptor binding. The aim of the present study was double: (i) to determine whether V1b receptors contribute to the excitatory effect of vasopressin in XII and VII motoneurons; and (ii) to establish whether the action of vasopressin on motoneurons is mediated by Ca2+ signalling. Patch-clamp recordings were performed in brainstem slices of young rats. Vasopressin depolarized the membrane or generated an inward current. By contrast, [1-deamino-4-cyclohexylalanine] arginine vasopressin (d[Cha4]AVP), a V1b agonist, had no effect. The action of vasopressin was suppressed by Phaa-D-Tyr(Et)-Phe-Gln-Asn-Lys-Pro-Arg-NH2, a V1a antagonist, but not by SSR149415, a V1b antagonist. Thus, the vasopressin-induced excitation of brainstem motoneurons was exclusively mediated by V1a receptors. Light microscopic autoradiography failed to detect V1b binding sites in the facial nucleus. In motoneurons loaded with GTP-gamma-S, a non-hydrolysable analogue of GTP, the effect of vasopressin was suppressed, indicating that neuronal V1a receptors are G-protein-coupled. Intracellular Ca2+ chelation suppressed a Ca2+-activated potassium current, but did not affect the vasopressin-evoked current. H7 and GF109203, inhibitors of protein kinase C, were without effect on the vasopressin-induced excitation. U73122 and D609, PLCbeta inhibitors, were also without effect. Thus, excitation of brainstem motoneurons by V1a receptor activation is probably mediated by a second messenger distinct from that associated with peripheral V1a receptors.
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PMID:The vasopressin-induced excitation of hypoglossal and facial motoneurons in young rats is mediated by V1a but not V1b receptors, and is independent of intracellular calcium signalling. 1700 20

In vitro experiments demonstrated the neuroprotective effect of dipeptide pGlu-Asn-NH2, which corresponded to the N-terminal fragment of the major vasopressin metabolite AVP(4-9). The dipeptide in concentrations of 10(-5)-10(-7) M prevented death of HT-22 immortalized hippocampal neurons under conditions of oxidative stress and protected PC-12 rat pheochromocytoma cells from neurotoxic compound 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine. pGlu-Asn-NH2 in a concentration of 10(-6) M increased the content of endogenous neuroprotective substances, neurotrophin NGF and heat shock protein HSP70 in HT-22 cells. Our results indicate that this dipeptide can be used for the therapy of Parkinson's disease.
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PMID:Neuroprotective effect of dipeptide AVP(4-5)-NH2 is associated with nerve growth factor and heat shock protein HSP70. 1864 9

The myoactive neuropeptide NGIWYamide was originally isolated from the holothurian (sea cucumber) Apostichopus japonicus but there is evidence that NGIWYamide-like peptides also occur in other echinoderms. Here we report the discovery of a gene in the sea urchin Strongylocentrotus purpuratus that encodes two copies of an NGIWYamide-like peptide: Asn-Gly-Phe-Phe-Phe-(NH(2)) or NGFFFamide. Interestingly, the C-terminal region of the NGFFFamide precursor shares sequence similarity with neurophysins, carrier proteins hitherto uniquely associated with precursors of vasopressin/oxytocin-like neuropeptides. Thus, the NGFFFamide precursor is the first neurophysin-containing neuropeptide precursor to be discovered that does not contain a vasopressin/oxytocin-like peptide. However, it remains to be determined whether neurophysin acts as a carrier protein for NGFFFamide. The S. purpuratus genome also contains a gene encoding a precursor comprising a neurophysin polypeptide and 'echinotocin' (CFISNCPKGamide) - the first vasopressin/oxytocin-like peptide to be identified in an echinoderm. Therefore, in S. purpuratus there are two genes encoding precursors that have a neurophysin domain but which encode neuropeptides that are structurally unrelated. Furthermore, both NGFFFamide and echinotocin cause contraction of tube foot and oesophagus preparations from the sea urchin Echinus esculentus, consistent with the myoactivity of NGIWYamide in sea cucumbers and the myoactivity of vasopressin/oxytocin-like peptides in other animal phyla. Presumably the NGFFFamide precursor acquired its neurophysin domain following partial or complete duplication of a gene encoding a vasopressin/oxytocin-like peptide, but it remains to be determined when in evolutionary history this occurred.
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PMID:NGFFFamide and echinotocin: structurally unrelated myoactive neuropeptides derived from neurophysin-containing precursors in sea urchins. 1932 39


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