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At least 19 recordsLinked to original sources
PubMed1980

Studies on the presence of vasopressin, oxytocin and vasotocin in the pineal gland, subcommissural organ and fetal pituitary gland: failure to demonstrate vasotocin in mammals.

The demonstration of vasotocin in the mammalian pineal gland, subcommissural organ and fetal pituitary gland by bioassay has led to hypotheses regarding the function of this hormone in various reproductive processes. Preliminary examinations of the pineal gland and subcommissural organ with a specific radioimmunoassay failed to show vasotocin immunoreactivity. The presence of vasotocin, vasopressin and oxytocin in the pineal gland, subcommissural organ and fetal neurohypophysis was therefore investigated, using three specific radioimmunoassays. Frog and chicken pituitary glands were used to validate the vasotocin radioimmunoassay. Direct measurements in diluted homogenates of pituitary glands from frogs, chickens, mid-term fetal sheep and near-term fetal seals revealed the presence of vasotocin only in the frog and chicken pituitary glands, while vasopressin and oxytocin were found in the two fetal pituitary homogenates. Vasopressin and ocytocin were measured in homogenates of rat and bovine pineal glands and in preparations of the subcommissural organ of rats and rabbits after extraction with Vycor glass powder, but no specific vasotocin immunoreactivity was observed. These results indicate a discrepancy between the reported biological activity of vasotocin in the pineal gland, subcommissural organ and fetal pituitary gland and the immunoreactivity of this material, which can at present only be explained by the presence of a peptide which is structurally closely related to, but not identical with, vasotocin.

Animals↗
PubMed1981

The vasotocin-like biological activity present in the bovine pineal is due to a compound different from vasotocin.

The vasotocin-like biological activity detected in an extract (E5 fraction) of bovine pineal gland was found not to be due to the presence of vasotocin, vasopressin or oxytocin. The data obtained by means of bio- and radioimmunoassays suggest that the peptide responsible for this biological activity, however, possess the same Pro-Arg-Gly(NH2) tripeptidic carboxy-terminal end as vasotocin.

Animals↗
PubMed2005

Altered plasma and pituitary arginine vasotocin and hypothalamic provasotocin expression in flounder (Platichthys flesus) following hypertonic challenge and distribution of vasotocin receptors within the kidney.

Plasma AVT concentration, pituitary AVT content, hypothalamic provasotocin mRNA expression and other osmoregulatory parameters were measured in euryhaline flounder 4, 8, and 24 h after the hypertonic challenge of transfer from fresh water (FW) to seawater (SW). Osmolality and the concentration of major plasma ions, sodium and chloride, were significantly higher in fish transferred to SW by comparison with time matched controls, an effect evident within 4 h. By comparison with time matched controls, pituitary store of AVT was lower while plasma AVT concentration was higher 8 and 24 h after transfer to SW. Higher provasotocin mRNA expression in the hypothalamus was also seen at 4 and 8 h in flounder transferred from FW to SW compared with time matched controls. The lower pituitary store and higher circulating levels imply substantial AVT secretion occurs in the early phase response to this hypertonic challenge. Changes in the regulation of AVT synthesis and secretion appeared quickly following movement to SW, consistent with the rapid osmoregulatory response, including reduced urine production that fish require to accommodate the dehydrative water losses and salt loading on exposure to the new hyperosmotic environment. qPCR measures of whole kidney vasotocin receptor mRNA expression indicated similar levels in SW and FW. Immunohistochemistry for the vasotocin receptor in flounder kidney showed localisation on the afferent and efferent arterioles of the glomerulus and on the capillary bed that extends from the efferent arteriole to the smooth muscle surrounding the collecting duct. Localisation of the vasotocin receptor was comparable in SW and FW fish.

Animals↗
PubMed1976

Specific antidiuretic effect of [Leu4, D-Arg8] vasotocin and [Mpr1, Leu4, D-Arg8] vasotocin. Comment on the idea of lipophilic properties and position 4.

[Leu4, D-Arg8] vasotocin (I) and [Mpr1, Leu4, D-Arg8] vasotocin (II) possess a considerable and very specific antidiuretic effect. In I, the change of configuration in position 8 caused an increase of the magnitude of the antidiuretic effect. In I, the change of configuration in position 8 caused by two orders and a decrease of the magnitude of the pressor effect by one order. I and II are the first vasotocin analogues reported to have a relatively high and specific antidiuretic effect.

Animals↗
PubMed1977

Solid phase synthesis and some hormonal activities of 8-L-homoarginine-vasotocin and 1-deamino-8-L-homoarginine-vasotocin.

8-L-Homoarginine-vasotocin and its 1-deamino derivative were synthesized by the solid phase method. Both compounds possessed high activities in the uterus contraction and fowl depressor assays and showed higher pressor activities than the corresponding vasopressins. Homoarginine-vasotocin, unexpectedly, was a more potent antidiuretic agent than its deamino analogue.

Amino Acid Sequence↗
PubMed1988

Arginine vasotocin and a novel oxytocin-vasotocin-like material in plasma of human newborns.

Plasma of human adults contains an oxytocin, vasotocin-like (OT-VT) immunoreactive material that is estrogen responsive in both males and females and the levels of which are elevated during pregnancy. Although OT-VT is immunoreactive with an antiserum raised against synthetic arginine vasotocin (AVT), the elution profile of OT-VT by high-performance liquid chromatography (HPLC) is distinct from AVT, arginine vasopressin (AVP) or oxytocin (OT). Because the fetus is also exposed to high estrogen levels during pregnancy and AVT has been reported to be present in human fetal pituitaries, cord blood samples from 16 vaginally delivered human newborn infants were examined for evidence of OT-VT and AVT. Analysis of an extracted pool of cord blood plasma by HPLC revealed 4 peaks (I-IV) of AVT-like immunoreactivity. Peaks II and IV coeluted with synthetic AVP and OT, respectively, and were attributable to cross-reaction of the AVT antiserum with these peptides. Peak I was identified as AVT on the basis of its coelution with synthetic AVT. Peak III eluted in a manner identical with OT-VT. These results indicate that human newborn plasma contains at least three neurohypophysial peptides, AVP, OT and AVT. Additionally, newborn plasma contains an AVT-like immunoreactive material that is distinct from AVT, AVP and OT, but is identical with a novel OT-VT material observed in plasma of estrogen-primed adults. The physiological significance of AVT and OT-VT in newborn plasma remains to be determined.

Arginine Vasopressin↗
PubMed2005

Identification of roughskin newt medullary vasotocin target neurons with a fluorescent vasotocin conjugate.

Arginine8 vasotocin (AVT), a neurohypophyseal peptide in nonmammalian vertebrates, plays a key role in the regulation of social behaviors related to reproduction. In male roughskin newts (Taricha granulosa), AVT is an important facilitator of several reproductive behaviors, including courtship clasping of females. Although AVT is known to act in certain brain regions and AVT receptors have been localized to some extent, specific target neurons for this peptide have not been identified in any species. Internalization of a receptor-specific conjugate of AVT and the fluorescent dye Oregon green was used to identify AVT target cells in the medulla of male roughskin newts. Medullary neurons are of interest because they appear to mediate facilitation of clasping by AVT. Direct application of AVT-Oregon green to the fourth ventricular surface of the medulla in vivo resulted in conjugate internalization by a widespread population of medullary neurons, particularly in the medial reticular formation and nuclei of cranial nerves V, VII, VIII, IX, and X. Some fourth-ventricle ependymal cells were also labeled. Reticulospinal neurons, which play an important role in clasping, were identified by retrograde labeling with tetramethylrhodamine dextran amine. AVT-Oregon green was internalized by 72% of these neurons. These results show that AVT can directly affect a very large and diverse medullary neuronal population, which may underlie the peptide's role in multiple neuroendocrinological processes, including autonomic and behavioral regulation. Selectivity of the AVT action may arise through interactions between AVT and steroids such as corticosterone.

Animals↗
PubMed1988

Opposite effects of vasotocin and of a specific vasotocin antiserum on active sleep of kittens.

The effects of intracerebroventricularly administered synthetic arginine vasotocin (AVT) or undiluted AVT, vasopressin (AVP) and oxytocin (OT) antisera on active sleep (AS) of newborn kittens have been investigated in comparison with rabbit serum control. In contrast to AVP and OT antisera, AVT antiserum has produced opposite effects on AS as AVT itself. Since after 10 microliter of undiluted AVT antiserum the percentage of AS did not decrease under 20% and even after 100 microliter AS did not decrease under 5%, it is concluded that, at least during perinatal life, AVT could be considered as a neuromodulator with AS-promoting effect.

Animals↗
PubMed1989

Vasotocin increases quiet sleep and suppresses active sleep in newborn cats. Opposite effects after vasotocin immunoneutralization.

One picogram of synthetic arginine vasotocin (AVT) administered into the lateral ventricle of newborn cats aged 7-9 days, increased the amount of quiet sleep and markedly decreased the amount of active sleep. Ten pg AVT completely suppressed active sleep during the recording time of 3 hr. The increase in the quiet sleep occurred within 5-7 min and lasted for the entire recording time of 3 hr. An undiluted specific AVT antiserum (10 microliters) administered into the lateral ventricle, induced opposite effects suppressing quiet sleep and increasing active sleep. It is concluded that in newborn cats both AVT and the AVT antiserum induce the same hypnogenic effects as in the adult cats.

Animals↗
PubMedDate not supplied

Fluorescent vasotocin conjugate for identification of the target cells for brain actions of vasotocin.

The effects of neuropeptides on the brain are a major focus of neuroendocrine research, and little progress has been made in the identification of the target neurons for many neuropeptides. Arginine8-vasotocin (AVT) is a neurohypophyseal peptide present in nonmammalian vertebrates that controls many neural and behavioral functions. Here we describe synthesis and functional characterization of an AVT-Oregon green conjugate 1 (AVT-OG 1) that can be used in vivo to identify AVT target neurons. Application of AVT-OG 1 to the brainstem of an amphibian produces rapid, endosome-like internalization together with typical AVT-like neurophysiological effects. Thus, preparation of AVT-OG 1, which preserves the peptide's neurophysiological effects, is useful as a fluorescent marker for AVT target neurons. Consequently, AVT-OG 1 conjugate will have considerable utility for analyzing the neural actions of AVT in the intact brain.

Animals↗
PubMed1989

Identification of vasotocin-like immunoreactivity in chromaffin cells of the frog adrenal gland: effect of vasotocin on corticosteroid secretion.

The presence of neurohypophyseal nonapeptides in the adrenal gland of nonmammalian vertebrates and the possible action of these regulatory peptides on corticosteroid secretion have never been investigated. We have applied the indirect immunofluorescence technique to examine whether vasotocin (AVT) and/or mesotocin (MT) are located in frog adrenal (interrenal) tissue. Using antisera against AVT and tyrosine hydroxylase, we found that all chromaffin cells contain an AVT-like peptide. Labeling of consecutive sections with phenylethanolamine-N-methyltransferase or AVT antibodies showed that both noradrenaline- and adrenaline-storing cells contain AVT-like immunoreactivity. In contrast no labeling of frog adrenal slices was observed using a MT antiserum. At the ultrastructural level, the immunogold technique revealed that the AVT-immunoreactive peptide is sequestered in chromaffin granules with varying electron densities. Filtration of frog adrenal tissue extracts on Sep-Pak C-18 cartridges showed that the elution profile of the AVT-like peptide was similar to that of synthetic AVT. The apparent concentration of AVT in the adrenal was 2.7 ng/g tissue. Since chromaffin cells represent approximately one third of all interrenal cells, the actual concentration of AVT in chromaffin tissue was about 8 ng/g tissue. The role of AVT in the regulation of frog adrenal steroidogenesis was studied in vitro using perifused frog interrenal slices. Graded doses of AVT (10(-10)-10(-7) M) induced a dose-dependent stimulation of both corticosterone and aldosterone secretion. The other neurohypophyseal peptides (vasopressin, oxytocin, and MT) were also able to enhance corticosteroid secretion, but AVT was by far the most potent stimulator of steroidogenesis. Prolonged administration (4 h) of AVT induced a rapid increase in corticosterone and aldosterone output, followed by a gradual decline of corticosteroid secretion. These results show that an AVT-like peptide is stored in chromaffin granules of frog adrenal gland. Our data also indicate that synthetic AVT is a potent stimulator of corticosteroid secretion by frog interrenal cells. Since in amphibians adrenocortical and chromaffin cells are intimately intermingled, these results suggest that AVT produced by chromaffin cells may regulate corticosteroid release locally, through a cell to cell mode of communication.

Adrenal Cortex↗
PubMed1995

Sequence analysis of vasotocin cDNAs of the lamprey, Lampetra japonica, and the hagfish, Eptatretus burgeri: evolution of cyclostome vasotocin precursors.

We determined the nucleotide sequences of cDNAs encoding precursors of vasotocin (VT) from two cyclostomes, the lamprey Lampetra japonica and the hagfish Eptatretus burgeri, for estimation of their phylogenetic relationships. Although only 47% similarity was found between the VT cDNAs, the predicted VT precursors of the lamprey and the hagfish were both composed of a single peptide, VT, Gly-Lys-Arg and a neurophysin, as has been shown for precursors of vasopressin (VP) family hormones, including VP, VT and molluscan conopressin. The central region of the lamprey neurophysin was very similar to those of previously characterized gnathostome neurophysins. Conspicuously, all the positions of 14 Cys residues were conserved in the lamprey neurophysin. The C-terminal region did not have a distinctive Leu-rich core segment, which is always found in the glycopeptide (copeptin) moiety of VP precursors. In contrast, the hagfish neurophysin showed at least two insertions and one deletion in the conserved central region including 14 Cys residues, but contained a potential N-linked glycosylation site and had a high proportion of Leu residues in the C-terminal region, like the neurophysin of another hagfish, Eptatretus stouti. The evolutionary relationships of the precursors of VP family hormones among the lamprey, hagfish, gnathostomes and a mollusc were estimated by a maximum likelihood method. The phylogenetic tree with the highest bootstrap probability showed that the lamprey VT precursor is more closely related to the gnathostome VT and VP precursors than to the hagfish VT precursors.

Amino Acid Sequence↗
PubMed1997

Neuroanatomical distribution of vasotocin in a urodele amphibian (Taricha granulosa) revealed by immunohistochemical and in situ hybridization techniques.

Immunohistochemical and in situ hybridization techniques were used to investigate the neuroanatomical distribution of arginine vasotocin-like systems in the roughskin newt (Taricha granulosa). Vasotocin-like-immunoreactive neuronal cell bodies were identified that, based on topographical position, most likely, are homologous to groups of vasopressin-immunoreactive neuronal cell bodies described in mammals, including those in the bed nucleus of the stria terminalis, medial amygdala, basal septal region, magnocellular basal forebrain-including the horizontal limb of the diagonal band of Broca, paraventricular and supraoptic nuclei, suprachiasmatic nucleus, and dorsomedial hypothalamic nucleus. Several additional vasotocin-like-immunoreactive cell groups were observed in the forebrain and brainstem regions; these observations are compared with previous studies of vasotocin- and vasopressin-like systems in vertebrates. Arginine vasotocin-like-immunoreactive fibers and presumed terminals also were widely distributed with high densities in the basal limbic forebrain, the ventral preoptic and hypothalamic regions, and the brainstem ventromedial tegmentum. Based on in situ hybridization studies with synthetic oligonucleotide probes for vasotocin and the related neuropeptide mesotocin, as well as double-labeling studies with combined immunohistochemistry and in situ hybridization, we conclude that the vasotocin immunohistochemical procedures used identify vasotocin-like, but not mesotocin-like, elements in the brain of T. granulosa. The distribution of arginine vasotocin-like systems in T. granulosa is greater than the distribution previously reported for any other single vertebrate species; however, it is consistent with an emerging pattern of distribution of vasotocin- and vasopressin-like peptides in vertebrates. Complexity in the vasotocinergic system adds further support to the conclusion that this peptide regulates multiple neurophysiological and neuroendocrinological functions.

Animals↗