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Dynorphin-(1-13), an extraordinarily potent opioid peptide.
Open accessAbstract
We describe the opioid properties of a tridecapeptide, the sequence of which corresponds to the NH2-terminal sequence of dynorphin, a novel porcine pituitary endorphin. It contains [Leu]enkephalin. In the guinea pig ileum longitudinal muscle preparation it is about 700 times more potent than [Leu]enkephalin. Its effects in this tissue are blocked completely by naloxone, but the apparent affinity of naloxone is 1/13th that for blockade of [Leu]enkephalin or normorphine. In the mouse vas deferens, this peptide is 3 times more potent than [Leu]enkephalin. Well-washed rat brain membranes degrade the peptide rapidly, suggesting the presence of a membrane-bound degradative enzyme. The peptide displays considerable immunoreactivity in assays with antisera that have been used for the immunohistochemical localization of [Leu]enkephalin. The remarkable enhancement of the potency of [Leu]enkephalin by the COOH-terminal extension -Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-OH suggests new interpretations concerning the structure of opiate receptors and the function of the enkephalin pentapeptides.
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“This system is comprised of three types of opioid receptors: μ (MOR), δ (DOR), and κ (KOR); and their endogenous ligands, endorphin, enkephalin and dynorphin (Hughes et al 1975; Birdsall and Hulme 1976; Goldstein et al 1979; Evans et al 1992; Kieffer et al 1992; Chen et al 1993; Yasuda et al 1993).”
From The behavioral, anatomical and pharmacological parallels between social attachment, love and addiction (2012) · cites this paper as Goldstein et al 1979
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“Dynorphin is a potent endogenous ligand for the κ -opioid receptor (23, 24).”
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Metadata
- Authors
- Goldstein, A., Tachibana, S., Lowney, L. I., Hunkapiller, M., & Hood, L.
- Affiliations
- California Institute of Technology (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1979-12
- Volume
- 76
- Issue
- 12
- Pages
- 6666-6670
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC411929
- OpenAlex
- W2033680879
- Cited by
- 882
- References
- 18
- Citations by year
- 2026: 8 · 2025: 9 · 2024: 8 · 2023: 14 · 2022: 10 · 2021: 14 · 2020: 23 · 2019: 13 · 2018: 8 · 2017: 9 · 2016: 6 · 2015: 8 · 2014: 16 · 2013: 23 · 2012: 18
- FWCI
- 24.93
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuropeptides and Animal Physiology
- Life Sciences › Neuroscience › Endocrine and Autonomic Systems › Neuroendocrine regulation and behavior
- Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
- Keywords
- dynorphin A(1-13), opioid peptides, leu-enkephalin, enkephalin, naloxone, opioid receptors, vas deferens, peptide degradation, immunoreactivity
- MeSH terms
- Amino Acid Sequence, Animals, Biological Assay, Dose-Response Relationship, Drug, Endorphins, Guinea Pigs, Ileum, Radioligand Assay, Receptors, Opioid, Structure-Activity Relationship, Swine, Rats
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