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

The nonapeptide vasopressin is synthetized as part of a longer common precursor polypeptide, together with its carrier protein neurophysin and a glycopeptide of unknown function. The gene for this common precursor has been isolated and sequenced and shown to comprise three exons encoding, respectively, the protein domains approximately corresponding to the N-terminal leader peptide and hormone, to most of the neurophysin, and to the glycopeptide. In the Brattleboro rat, the hereditary hypothalamic diabetes insipidus, characteristic of this strain, has been shown to be caused by a single nucleotide deletion in the vasopressin gene. This leads to the much reduced synthesis of a mutant vasopressin precursor, whose C terminus is quite unlike that in wild-type rats and which does not appear to be correctly processed in vivo.
 ...
PMID:Biosynthesis of vasopressin. 243 69

The nonapeptide hormone oxytocin-like arginine-vasopressin (AVP) is synthesized as part of a larger precursor polypeptide. The precursor also includes the neurophysin molecule with which the hormone is associated in the neurosecretory granules of the hypothalamo-pituitary tract. A protein of molecular weight (Mr) approximately 20,000 has been isolated from supraoptic nuclei of rat hypothalami which, after tryptic cleavage, released a neurophysin-like molecule of Mr approximately 10,000 and an oligopeptide related to oxytocin. This result was complemented by in vitro translation of bovine hypothalamic mRNA. Among the primary translation products a single polypeptide of Mr approximately 16,500 was shown to contain antigenic determinants recognized by specific antisera against bovine neurophysin I and oxytocin. Here we report the amino acid sequence of the bovine oxytocin-neurophysin I (OT-NpI) precursor which was derived from sequence analysis of the cloned cDNA. As is the case for the bovine arginine-vasopressin-neurophysin II (AVP-NpII) precursor, the signal sequence of the OT-NpI precursor is immediately followed by the nonapeptide hormone which is connected to neurophysin I by a Gly-Lys-Arg sequence. A striking feature of the nucleic acid sequence is the 197-nucleotide long perfect homology with the AVP-NpII precursor mRNA sequence encoding the conserved middle part of neurophysins I and II.
 ...
PMID:Deduced amino acid sequence from the bovine oxytocin-neurophysin I precursor cDNA. 668 26

Annetocin is a structurally and functionally oxytocin-related peptide isolated from the earthworm Eisenia foetida. We present the characterization of the annetocin cDNA. Sequence analyses of the deduced precursor polypeptide revealed that the annetocin precursor is composed of three segments: a signal peptide, an annetocin sequence flanked by a Gly C-terminal amidation signal and a Lys-Arg dibasic processing site, and a neurophysin domain, similar to other oxytocin family precursors. The proannetocin showed 37.4-45.8% amino acid homology to other prohormones. In the neurophysin domain, 14 cysteines and amino acid residues essential for association of a neurophysin with a vasopressin/oxytocin superfamily peptide were conserved, suggesting that the Eisenia neurophysin can bind to annetocin. Furthermore, in situ hybridization experiments demonstrated that the annetocin gene is expressed exclusively in neurons of the central nervous system predicted to be involved in regulation of reproductive behavior. These findings confirm that annetocin is a member of the vasopressin/oxytocin superfamily. This is the first identification of the cDNA encoding the precursor of an invertebrate oxytocin-related peptide and also the first report of the identification of an annelid vasopressin/oxytocin-related precursor.
 ...
PMID:Evidence for conservation of the vasopressin/oxytocin superfamily in Annelida. 1002 77

The cyclic nonapeptides, oxytocin and vasopressin, are neurohypophysial hormones that regulate many significant physiological processes related especially to reproduction and osmoregulation. In this study, we characterized an oxytocin-related peptide cDNA from a urochordate, Styela plicata, thought to be a sister group to vertebrates. Sequence analysis of the deduced precursor polypeptide revealed that the precursor is composed of three segments: a signal peptide, an oxytocin-like sequence flanked by a Gly C-terminal amidation signal and a Lys-Arg dibasic processing site, and a neurophysin domain, similar to other oxytocin/vasopressin family precursors. However, unlike other members of this family, the tunicate oxytocin-like peptide (CYISDCPNSRFWST-NH2) is a tetradecapeptide. We termed this peptide Styela oxytocin-related peptide (SOP). Furthermore, analyses of mass spectrometry, in situ hybridization, and immunohistochemistry demonstrated production of mature SOP in the cerebral ganglion. To elucidate the physiological action of SOP, we kept the tunicate for 2 d under the three different concentrations of seawater, 60, 100, and 130%, and measured the expression levels of SOP mRNA in the cerebral ganglion. The greatest expression of SOP mRNA was observed in the 60% seawater. In 60% seawater, but not in 100 or 130%, the tunicate mostly closed the atrial and branchial siphons. Therefore, we investigated the contractile effects of SOP on the siphons in vitro. SOP caused contractions in both siphons in a dose-dependent manner. Taken together, these results suggest that SOP acts to prevent the influx of a low concentration of seawater into the body and thus play an important role in osmoregulation.
 ...
PMID:Unique form and osmoregulatory function of a neurohypophysial hormone in a urochordate. 1858 15

cDNA clones corresponding to the vasotocin precursor polypeptide were isolated from a chicken hypothalamic library and sequenced. The derived amino-acid sequence indicates a precursor of comparable structural organization to that described for members of the vasotocin/vasopressin gene family from other species. Unlike in mammals the C-terminal glycopeptide moiety appears not be cleaved off from the neurophysin. Subsequent screening of a chicken genomic library permitted an analysis also of the vasotocin gene structure and exonic composition. The 5'region upstream of the first exon was sequenced and revealed an unusual pattern of 49 repetitive -YYCYCYAAAYY- motifs, together with a polyadenyl region supporting a bend in the DNA, and a long pyrimidine-rich sequence. Three AP2-like elements, identified in the mammalian vasopressin gene, were also observed in the immediate upstream region. There was no obvious homology to the promoter regions of the known oxytocin genes, nor to any other sequence deposited in available databases, nor to other known cis-elements.
 ...
PMID:The chicken vasotocin gene. 2155 35

Stress stimuli, including diseases, disturb homeostasis of the body and enhance secretion of various hypothalamus, pituitary and adrenal gland hormones. One of the main hypothalamic hormones secreted in stress conditions is arginine vasopressin (AVP). Vasopressin concentration in the blood reflects the severity of disease and disorders of blood volume. Measurement of vasopressin is difficult and subjected to considerable laboratory error because of the short half-life in serum and its instability in withdrawn blood samples. This hormone and copeptin are peptides produced during the cleavage of a larger precursor polypeptide: pre-provasopressin. Both peptides are formed in equimolar amounts. Copeptin is a more stable peptide, measurement of which can be performed with higher accuracy. This paper presents the importance of copeptin as a marker of stress, with particular emphasis on the neonatal period, analyzing the impact of gestational age and the route of delivery. Its potential application for assessing the degree of hydration in the adaptation period is also discussed.
...
PMID:[Copeptin - stable C-terminal fragment of pre-provasopressin as a new stress marker in newborns]. 2620 85