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Ranatensin

● Preclinical
Ranatensin
Also known as: Rana Tachykinin, Frog Skin Tachykinin
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Quick Summary

Ranatensin is an 11-residue tachykinin peptide isolated from the skin of the North American frog Rana pipiens. It belongs to the same tachykinin family as substance P and physalaemin, sharing the conserved C-terminal Phe-X-Gly-Leu-Met-NH2 sequence.

Neuropeptide / Tachykinin Preclinical
Ranatensin is an 11-residue tachykinin peptide isolated from the skin of the North American frog Rana pipiens. It belongs to the same tachykinin family as substance P and physalaemin, sharing the conserved C-terminal Phe-X-Gly-Leu-Met-NH2 sequence. Ranatensin activates NK1 receptors and has been used as a pharmacological tool in tachykinin receptor research, helping to define the structural requirements for receptor binding.
Storage Stability
Lyophilized
1–2 years (-20°C)
Reconstituted
~30 days (2–8°C)
Room temp
Avoid

Mechanism of Action

Tachykinin Receptor Activation

Ranatensin activates NK1 receptors with similar potency to substance P. Gq coupling activates phospholipase C, generating IP3 and DAG, which mobilize intracellular calcium and activate PKC. The NK1 activation produces vasodilation, smooth muscle contraction in the gastrointestinal tract, and modulation of pain signaling in the spinal cord.

Structural Pharmacology

The N-terminal pyroglutamic acid (pGlu) of ranatensin confers resistance to aminopeptidase degradation. Structure-activity studies using ranatensin analogs identified the relative contributions of the N-terminus versus the conserved C-terminal sequence to receptor affinity and subtype selectivity.


Research Summary

Tachykinin SAR Studies

Preclinical

Ranatensin was an important tool in early structure-activity relationship (SAR) studies of tachykinins. Systematic substitutions of individual residues identified position 7 (Phe) and position 11 (Met-NH2) as critical determinants of NK1 receptor binding. These studies guided the development of selective NK1 antagonists with therapeutic applications.

Comparison with Eledoisin

Preclinical

Parallel pharmacological characterization of ranatensin and eledoisin in different tissue preparations showed differing potency ratios, providing early evidence for tachykinin receptor multiplicity. These comparative data helped establish the existence of distinct NK1 and NK2 receptor subtypes.


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Research Protocols

GoalDoseFrequencyRoute
NK1 receptor pharmacology1-1000 nMSingleOrgan bath / binding
Smooth muscle contraction10-100 nMSingleIsolated tissue

Research tool only. No therapeutic applications.


Interactions

Synergy
Substance P
Both NK1 agonists; complementary pharmacological tools
Synergy
Related amphibian tachykinin; used in comparative studies

Safety Profile

Ranatensin produces vasodilation and smooth muscle contraction; no therapeutic use. Research use only in in vitro and animal models.


References

  • [1]Anastasi A et al. (1968). Structure and pharmacological actions of ranatensin, a peptide isolated from the skin of Rana pipiens. Experientia, 24(8), 771-773.
  • [2]Nawa H et al. (1983). Substance P: regional distribution and comparisons with other tachykinins. Biochemical and Biophysical Research Communications, 114(3), 1103-1112.
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Verified Scientific Data Last audited:
Data Sources & External References
Source: peer-reviewed literature  ·  Domain: ascendpeptide.org

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