Novel C-Terminally amidated opioid peptide in human phaeochromocytoma tumour

Hisayuki Matsuo, Atsuro Miyata, Kensaku Mizuno

研究成果: Article査読

63 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)721-723
ページ数3
ジャーナルNature
305
5936
DOI
出版ステータスPublished - 1983 12 1
外部発表はい

ASJC Scopus subject areas

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