| Autor: |
Seizinger, B. R., Liebisch, D. C., Gramsch, C., Herz, A., Weber, E., Evans, C. J., Esch, F. S., Böhlen, P. |
| Zdroj: |
Nature; January 1985, Vol. 313 Issue: 5997 p57-59, 3p |
| Abstrakt: |
Biologically active peptide hormones and neurotransmitters have been shown to be enzymatically liberated from larger, inactive precursor molecules by tissue-specific post-translational processing, particularly at the typical cleavage signals of paired basic residues1,2. Subsequent N-terminal or C-terminal modifications may be of importance in regulating the biological activities of these peptides (for review see ref. 3). C-terminal α-amidation is considered to be essential for the biological function of several non opioid peptides4,5. Here we present the isolation and structure of a novel C-terminally amidated opioid peptide, amidorphin, from bovine adrenal medulla. Amidorphin and the recently isolated octapeptide metorphamide6(adrenorphin7) are the only endogenous opioid peptides in mammals known to possess a C-terminal amide group. The amino acid sequence of amidorphin corresponds to the sequence 104–129 of bovine proenkephalin A (refs 8, 9). Very high concentrations of amidorphin were detected in bovine adrenal medulla and in a further endocrinological system, the hypothalamic–neurohypophyseal axis. Amidorphin may there fore be considered to be a major gene product of the opioid peptide precursor proenkephalin A in these endocrine tissues. |
| Databáze: |
Supplemental Index |
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