Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01185 (vasopressin)
 23,126 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Several neuropeptides are suspected to act on the control of hydric balance in leeches. One of these peptides, a peptide immunoreactive to an antibody against oxytocin, was previously characterized from the central nervous system of the leech Erpobdella octoculata [Salzet, M., Wattez, C., Verger-Bocquet, M., Beauvillain, J.-C. & Malecha, J. (1993) Brain Res. 601, 173-184]. This paper reports the isolation from the central nervous system of E. octoculata of another peptide of the oxytocin/vasopressin family; a lysine-vasopressin-like molecule. Its purification was performed by reverse-phase high-performance liquid chromatography combined with both dot immunobinding assay and enzyme-linked immunosorbent assay for lysine-vasopressin. The amino acid sequence was established by Edman degradation and confirmed by electrospray-mass-spectrometry measurement. The nonapeptide obtained corresponded to the lysine-conopressin previously isolated from the venom of the mollusc Conus geographus [Cruz, L. L., de Santos, V., Zafaralla, G. C., Ramilo, C. A., Zeikus, R., Gray, W. R. & Olivera, B. M. (1987) J. Biol. Chem. 262, 15821-15824]. In leeches, synthetic lysine-conopressin exerts a diuretic effect which can be compared to that of the arginine-vasopressin-like peptide isolated in the Insect Locusta migratoria [Proux, J., Miller, C. A., Li, J. P., Carney, R. L., Girardie, A., Delaage, M. & Schooley, D. A. (1987) Biochem. Biophys. Res. Commun. 149, 180-186].
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PMID:Isolation, structural characterization and biological function of a lysine-conopressin in the central nervous system of the pharyngobdellid leech Erpobdella octoculata. 822 46

Purification of a material immunoreactive to an antiserum against the C-terminal part of the oxytocin (Pro-Leu-Gly-amide) and present in the central nervous system of the Pharyngobdellid leech Erpobdella octoculata was performed by reversed-phase high performance liquid chromatography combined with both enzyme-linked immunosorbent and dot immunobinding assays for oxytocin. The amino acid sequence of the purified peptide (Ile-Pro-Glu-Pro-Tyr-Val-Trp-Asp) was established by Edman degradation and confirmed by electrospray mass spectrometry measurement. When injected in leeches, purified or synthetic peptides exert an anti-diuretic effect, the most effective ranged between 10 pmol and 1 nmol. They provoked an uptake of water 1-2 h post-injection. Furthermore, electrophysiological experiments conducted in the leech Hirudo medicinalis revealed an inhibition of the potency of Na+ conductances of leech skin by this peptide. Immunocytochemical studies with an antiserum against synthetic oxytocin-like molecule provided the cytological basis for existence of a neuropeptide, since large amounts of immunoreactive neurons were detected in the central nervous systems of E. octoculata. The purified molecule is both different to peptides of the oxytocin/vasopressin family and is a novel neuropeptide in the animal kingdom. It was named the leech osmoregulator factor (LORF). An identification of the proteins immunoreactive to an antiserum against oxytocin performed at the level of both central nervous systems extracts and in vitro central nervous system-translated RNA products indicated that in the two cases, a single protein was detected. These proteins with a molecular masses of, respectively, approximately 34 kDa (homodimer of 17 kDa) for the central nervous systems extracts and approximately 19 kDa for in vitro central nervous system-translated RNA products were not recognized by the antiserum against MSEL- and VLDV-neurophysin (proteins associated to oxytocin and vasopressin), confirming that LORF did not belong to the oxytocin/vasopressin family.
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PMID:Structural characterization of a novel neuropeptide from the central nervous system of the leech Erpobdella octoculata. The leech osmoregulator factor. 863 63

Annetocin is an earthworm oxytocin-related peptide that we previously isolated from the whole body of a lumbricid earthworm Eisenia foetida. We have reported that annetocin induces egg-laying-like behaviors in E. foetida and a gnathobdellid leech, Whitmania pigra, when it is injected into the respective animals. The present study was undertaken to probe physiological functions of invertebrate oxytocin-vasopressin-superfamily peptides with special reference to reproductive and osmoregulatory events in which vertebrate peptides of this superfamily are involved. Annetocin, Lys-conopressin (a leech vasopressin-related peptide) and two analog peptides, [Tyr(3)]-annetocin ((3)Y-annetocin) and [Phe(3)]-annetocin ((3)F-annetocin), were compared for their activities to induce egg-laying-like behavior and to change body weight as a measure of water balance in the leech W. pigra. Injection of annetocin, Lys-conopressin, and (3)F-annetocin caused both egg-laying-like behavior and reduction of body weight in the animals, but (3)Y-annetocin induced neither. Furthermore, leeches in the non-breeding season responded to peptides less conspicuously than those in the breeding season. Such a concomitant induction of egg-laying-like behavior and body-weight reduction suggests that these two phenomena are unitary and might be accounted for by the fact that egg-laying in leeches and earthworms is accompanied by secretion of a large quantity of mucus, which should significantly contribute to body-weight loss. J. Exp. Zool. 284:401-406, 1999.
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PMID:Possible functions of oxytocin/vasopressin-superfamily peptides in annelids with special reference to reproduction and osmoregulation. 1045 17

An increase in intracellular cyclic AMP concentration stimulates transepithelial Na(+) transport across the skin of the leech Hirudo medicinalis, but it is unclear how cytosolic cyclic AMP levels are elevated in vivo. In search of this external stimulus, we performed Ussing chamber experiments to test several peptide hormones and neurotransmitters for their effect on Na(+) transport across leech dorsal integument. Although all the peptide hormones under investigation significantly affected ion transport across leech integument, none of them mimicked the effect of an experimental rise in intracellular cyclic AMP level. The invertebrate peptides conopressin and angiotensin II amide inhibited short-circuit-current- (I(sc)) and amiloride-sensitive Na(+) transport (I(amil)), although to slightly different degrees. The vertebrate peptide hormones 8-arginine-vasopressin and 8-lysine-vasopressin both produced an inhibition of I(amil) comparable with that caused by angiotensin II amide. However, 8-lysine-vasopressin reduced I(sc), whereas 8-arginine-vasopressin induced a moderate increase in I(sc). The neurotransmitter dopamine, which occurs in the leech central nervous system in relatively large amounts, and its precursor l-dopamine both induced large decreases in I(sc) and I(amil). However, the reactions evoked by the catecholamines showed no pronounced similarity to the effects of intracellular cyclic AMP. Two other neurotransmitters known to occur in leeches, serotonin (5-hydroxytryptamine) and gamma-n-aminobutyric acid (GABA), had no influence on transepithelial ion transport in leech skin.
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PMID:Regulation of Na(+) transport across leech skin by peptide hormones and neurotransmitters. 1127 12