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Brain Res Bull
2007 Mar 30;716:628-32. doi: 10.1016/j.brainresbull.2006.12.001.
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Xendorphin B1, a novel opioid-like peptide determined from a Xenopus laevis brain cDNA library, produces opioid antinociception after spinal administration in amphibians.
Stevens CW
,
Tóth G
,
Borsodi A
,
Benyhe S
.
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Prodynorphins (PDYNs) from the African clawed frog (Xenopus laevis), originally described as 'proxendorphins', are novel members of the family of opioid-like precursor polypeptides and were recently discovered based on polymerase chain reaction (PCR) isolates from a Xenopus brain cDNA library. This amphibian prodynorphin was found in two isoforms, (Xen)PDYN-A and (Xen)PDYN-B, consisting of 247 and 279 amino acids, respectively. Each prepropeptide contains five potential opioid-like peptides, collectively named xendorphins. One of these, xendorphin B1 ((Xen)PDYN-B sequence 96-111: YGGFIRKPDKYKFLNA), is a hexadecapeptide that displaced [3H]naloxone and the radiolabelled kappa opioid, [3H]dynorphin A (1-17), with nanomolar affinity from rat brain membranes. Using the acetic acid pain test, the present study examined the antinociceptive effects of spinally administered xendorphin B1 in amphibians. Xendorphin B1 produced a long-lasting and dose-dependent antinociceptive effect in the Northern grass frog (Rana pipiens) with an ED50 value of 44.5 nmol/frog. The antinociceptive effects of xendorphin B1 were significantly blocked by pretreatment with the non-selective opioid antagonist, naltrexone. This is the first report of the in vivo characterization of a non-mammalian prodynorphin-derived peptide and suggests that xendorphin peptides may play a role in the modulation of noxious information in vertebrates.
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17292806
???displayArticle.pmcLink???PMC1945180 ???displayArticle.link???Brain Res Bull ???displayArticle.grants???[+]
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