| Company Name: |
Nanjing Yuanpeptide Biotech Co.，Ltd.
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18168071971 |
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support@yuan-peptide.com |
| Products Intro: |
Product Name:vasotocin
Purity:95% HPLC 98% HPLC 99% HPLC Package:10mg;20mg;50mg;100mg;1g;5g;20g
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| Product Name: | Vasotocin | | Synonyms: | Vasotocin;113-80-4/74927-14-3 | | CAS: | | | MF: | | | MW: | 0 | | EINECS: | | | Product Categories: | | | Mol File: | Mol File | ![Vasotocin Structure]() |
| | Vasotocin Chemical Properties |
| | Vasotocin Usage And Synthesis |
| Discovery | Vasotocin was chemically synthesized in 1958 as an
analog of neurohypophysial hormones containing a ring
of oxytocin (OT) and a side chain of vasopressin (VP).
Subsequently, VT has been isolated from various vertebrate species. All nonmammalian vertebrates have VT
as a VP family peptide. Because cyclostomes contain only
VT, the VT gene is considered to be an ancestral gene for
all vertebrate neurohypophysial hormones. | | Structure | The intramolecular ring structure is identical to that of
OT while the eighth aa residue in the C-terminal extension is arginine. Therefore, VT is a basic VP
family peptide. The C-terminus of VT is amidated. In
anuran amphibians, two types of C-terminally extended
peptides called hydrins have been found. Mr 1050. VT is freely soluble in water, with increased
stability under acidic conditions using acetic acid.
 | | Gene, mRNA, and precursor | From cartilaginous fish to birds, the VT gene is located
on the same chromosome with the respective OT-family
genes in a tail-to-head orientation. The existence of
cis-regulatory elements that mediate neuron-specific
expression was suggested for the pufferfish fugu.
Similar to VP precursors, VT precursors are composed
of a signal peptide, a mature peptide, processing and amidation motifs, neurophysin, and copeptin moieties. The copeptins of tetrapods
and cartilaginous fish are considered to be glycopeptides
while no glycosylation site is found in teleosts and
cyclostomes. | | Receptors | Currently, four specific receptors have been identified
in nonmammalian vertebrates. Of these, V2bR (further
subdivided to V2b,c,dR; see “Neurohypophysial hormone family”) is a newly discovered receptor and is
either a pseudogene or has disappeared in mammals
while the other three receptors (V1aR, V1bR, and
V2aR) are orthologous to mammalian VP receptors. Specifically, only in birds, VT receptors have been named differently as VT1R (V2bR), VT2R (V1bR), VT3R (mesotocin
receptor, MTR), and VT4R (V1aR). V2aR has not been
found in birds and cartilaginous fish while the existence
of V1bR in teleosts has not been proven. In teleosts, further duplications of receptors have been found. Similar to mammalian VP receptors, V1aR and V1bR
couple to Ca2+ signaling pathways while V2aR couples
to the adenylate cyclase pathway. V2bRs, including
chicken VT1R, are structurally related to the conventional
V2 receptor (V2aR), but couple to Ca2+ signaling
pathways. | | Agonist and antagonists | Only a few studies have tested the selectivity and
potency of agonists and antagonists to the nonmammalian receptors. The following antagonists for mammalian
receptors have been used: V1a antagonists, OPC-21268,
SR-49059, d(CH2)5[Tyr(Me)2
]AVP (Manning compound);
V1b antagonist, SSR-149415; V2a antagonists: OPC-31260, d(CH2)5[D-Ile2
,Ile4
,Ala-NH2]AVP. | | Synthesis and release | In birds, the synthesis and release of VT are increased
by water deprivation, drinking hypertonic saline, and
hemorrhage. The involvement of a transcription factor,
TonEBP, is implicated in enhanced VT synthesis after salt
loading. Osmotic manipulation increases the synthesis
and release of VT in reptiles, amphibians, many teleosts,
and sharks. In birds, plasma VT levels transiently
increase at the time of oviposition and decrease within
30min after egg laying, which is correlated with increases
in uterine contractility. Direct and indirect regulation of
VT synthesis by androgen and estrogen is shown in the
sexually dimorphic BNST and amygdala. VT release from
the neurohypophysis is stimulated by steroid hormones
and other hormones, including angiotensin II and urotensin I. Brain VT content is high in aggressive stickleback
males that take care of eggs. | | Biological functions | VT is important for osmoregulation and ionoregulation in vertebrate groups from fish to birds. The antidiuretic effect is particularly important in terrestrial
species. VT is also implicated in cardiovascular and
glycogenolytic effects, circadian and seasonal biology,
uterine contraction, stress response, and social and reproductive behaviors. | | Description | VT is a vasopressin-family peptide of all nonmammalian
vertebrates; roles in body fluid homeostasis, reproduction,
behavior, and stress response have been implicated. |
| | Vasotocin Preparation Products And Raw materials |
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