Novel C-Terminally amidated opioid peptide in human phaeochromocytoma tumour

Hisayuki Matsuo, Atsuro Miyata, Kensaku Mizuno

Research output: Contribution to journalArticlepeer-review

63 Citations (Scopus)


As has often been observed in hypothalamic releasing factors and gastrointestinal hormones, the carboxy-terminal amide structure is a unique feature of peptides exhibiting hormonal or physiological activities. Although a variety of opioid peptides have hitherto been identified1-8, such a C-terminal amidated species has never before been discovered in mammals. Here we present the first identification of a novel opioid octapeptide with a C-terminal amide structure, henceforth designated as 'adrenorphin', in human phaeochromocytoma tumour derived from adrenal medulla. The complete amino acid sequence of adrenorphin was determined by microsequencing and corresponds to the sequence of the first eight amino acids of peptide E which is derived from proenkephalin A. Adrenorphin has also been identified chromatographically in normal human and bovine adrenal medulla. Adrenorphin exhibits potent opioid activity in guinea pig ileum assay, suggesting a specialized physiological function.

Original languageEnglish
Pages (from-to)721-723
Number of pages3
Issue number5936
Publication statusPublished - 1983 Dec 1
Externally publishedYes

ASJC Scopus subject areas

  • General


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