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Kassinin Sale

(Synonyms: 肛褶蛙肽) 目录号 : GC31145

Kassinin是一种衍生自Kassina蛙的肽。Kassinin属于速激肽家族的神经肽。Kassinin分泌作为防御信号,并参与神经肽信号传导。

Kassinin Chemical Structure

Cas No.:63968-82-1

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产品描述

Kassinin is a peptide derived from the Kassina frog. It belongs to tachykinin family of neuropeptides. It is secreted as a defense response, and is involved in neuropeptide signalling.

Amino acid composition and sequence of Kassinin, a tachykinin dodecapeptide from the skin of the African frog Kassina senegalensis. Methanol extracts of the skin of the African amphibian Kassina senegalensis contain a dodecapeptide, Kassinin, belonging to the family of tachykinins or physalaemin-like peptides. Kassinin, like all other natural tachykinins, possesses the characteristic C-terminal tripeptide Gly-Leu-Met-NH2 and a phenylalanine residue in position 5 from the C-terminus. The amino acid sequence in the N-moiety of the molecule differs sharply from that of the other tachykinins[1].

[1]. Anastasi A, et al. Amino acid composition and sequence of kassinin, a tachykinin dodecapeptide from the skin of the African frog Kassina senegalensis. Experientia. 1977 Jul 15;33(7):857-8.

Chemical Properties

Cas No. 63968-82-1 SDF
别名 肛褶蛙肽
Canonical SMILES Asp-Val-Pro-Lys-Ser-Asp-Gln-Phe-Val-Gly-Leu-Met-NH2
分子式 C59H95N15O18S 分子量 1334.54
溶解度 Soluble in DMSO 储存条件 Store at -20°C
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1 mM 0.7493 mL 3.7466 mL 7.4932 mL
5 mM 0.1499 mL 0.7493 mL 1.4986 mL
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Research Update

Inhibitory effect of kassinin on salt intake induced by different natriorexigenic treatments in the rat

Pulse intracerebroventricular (i.c.v.) injection of kassinin, 100-500 ng/rat, potently inhibits salt intake induced by sodium depletion. The effect appears to be selective since the same doses of kassinin do not inhibit milk intake or solid food intake. When given by continuous i.c.v. infusion kassinin elicits a clear anti-natriorexic effect at doses of 1-10 ng/min/rat. Kassinin not only suppresses sodium depletion-induced salt appetite, but it also inhibits sodium intake induced by pulse i.c.v. injection of renin or by subcutaneous (s.c.) deoxycorticosterone. Finally it also suppresses the elevated need-free intake of 1.5% NaCl in multidepleted female rats, which is not mediated by the renin-angiotensin-aldosterone system. These findings show that kassinin exerts a general suppressive effect on salt intake, irrespective of the natriorexigenic treatment. The present study suggests that the kassinin-like peptides that are endogenous to the rat brain may be involved in the behavioral regulation of extracellular body fluids in the rat by inhibiting sodium intake.

Kassinin: stimulation of insulin and glucagon secretion in the rat

The effect of the newly discovered tachykinin dodecapeptide kassinin on endocrine pancreatic function was examined in the rat and compared to that of substance P, a neuropeptide which is structurally closely related to kassinin. Kassinin, injected iv in graded doses 10, 20, and 30 min before blood collection, significantly increased both plasma insulin and plasma glucagon in a dose-related fashion. The largest dose examined (10 micrograms) increased plasma insulin by 275% and plasma glucagon by 77%. In contrast, iv injections of equimolar doses of substance P did not affect either hormone. However, both kassinin and substance P increased plasma glucose levels in a dose-dependent fashion. Kassinin appears to have biological actions on the endocrine pancreas which clearly can be distinguished from those of substance P. Should kassinin be present in mammalian tissue and show a distribution similar to that of other neuropeptides, it may play a role in the physiological regulation of carbohydrate metabolism.

Kassina senegalensis skin tachykinins: molecular cloning of kassinin and (Thr2, Ile9)-kassinin biosynthetic precursor cDNAs and comparative bioactivity of mature tachykinins on the smooth muscle of rat urinary bladder

Tachykinins are among the most widely-studied families of regulatory peptides characterized by a highly-conserved C-terminal -Phe-X-Gly-Leu-Met.amide motif, which also constitutes the essential bioactive core. The amphibian skin has proved to be a rich source of these peptides with physalaemin from the skin of Physalaemus fuscomaculatus representing the archetypal aromatic tachykinin (X=Tyr or Phe) and kassinin from the skin of Kassina senegalensis representing the archetypal aliphatic tachykinin in which X=Val or Ile. Despite the primary structures of both mature peptides having been known for at least 30 years, neither the structures nor organizations of their biosynthetic precursors have been reported. Here we report the structure and organization of the biosynthetic precursor of kassinin deduced from cDNA cloned from a skin secretion library. In addition, a second precursor cDNA encoding the novel kassinin analog (Thr(2), Ile(9))-kassinin was identified as was the predicted mature peptide in skin secretion. Both transcripts exhibited a high degree of nucleotide sequence similarity and of open-reading frame translated amino acid sequences of putative precursor proteins. The translated preprotachykinins each consisted of 80 amino acid residues encoding single copies of either kassinin or its site-substituted analog. Synthetic replicates of each kassinin were found to be active on rat urinary bladder smooth muscle at nanomolar concentrations. The structural organization of both preprotachykinins differs from that previously reported for those of Odorrana grahami skin indicating a spectrum of diversity akin to that established for amphibian skin preprobradykinins.

Parallel bioassay of physalaemin and kassinin, a tachykinin dodecapeptide from the skin of the African frog Kassina senegalensis

1. Kassinin, a tachykinin dodecapeptide isolated from the skin of the African frog Kassina senegalensis was submitted to parallel bioassay with physalaemin, eledoisin and substance P, three major representatives of the tachykinin peptide family. Bioassay was carried out on blood pressure, salivary secretion and isolated or in situ smooth muscle preparations. 2. As expected, kassinin possessed the entire spectrum of biological activity peculiar to the tachykinins. However, among the examined tachykinins kassinin was the poorest stimulant of salivary secretion and the weakest hypotensive agent, while displaying very powerful stimulant effects on different smooth muscle preparations, especially on isolated preparations of urinary bladder. 3. Kassinin differed from the other tachykinins also for its more gradual and sustained action on several in situ and isolated preparations. The peptide most similar to kassinin in its spectrum of activity was eledoisin. 4. Emphasis is laid on the possibility to dissociate the effects of the tachykinins on different target systems through changes in the N-moiety of the tachykinin molecule.

Effect of kassinin, neurokinin A and neurokinin B on drinking behaviour in the pigeon

Intracerebroventricular (i.c.v.) injection of kassinin produced a prompt and copious drinking response at doses of 10-1000 ng/pigeon, in the absence of other behavioural alterations or of changes in core temperature. Neurokinin A and B evoked drinking, but they were respectively 10 and 100 times less potent than kassinin. Intraperitoneal injection of kassinin elicited drinking, but at doses about 1000 X larger than the i.c.v. ones. The angiotensin antagonist [Sar1, Leu8]angiotensin II did not reduce drinking induced by i.c.v. kassinin, suggesting that its effect is not due to interaction with the central renin-angiotensin system. Moreover, the effect is apparently independent of the mechanisms controlling hypovolaemic and hyperosmotic thirst since exact additivity was found in the dipsogenic response when i.c.v. kassinin was administered in the presence of a hypovolaemic (subcutaneous (s.c.), polyethylene glycol) or hyperosmotic (s.c. hypertonic NaCl) dipsogenic stimulus. The present findings show that kassinin, neurokinin A and B share with the tachykinins already tested (eledoisin, physalaemin, substance P) a common dipsogenic action in pigeons. However, marked differences exist in their dipsogenic potency. This order of potency, eledoisin = kassinin = physalaemin greater than neurokinin A = substance P greater than neurokinin B, is not consistent with the tachykinin receptor subtypes so far proposed.