Isolation and structure of a novel C-terminally amidated opioid peptide, amidorphin, from bovine adrenal medulla

@article{Seizinger1985IsolationAS,
  title={Isolation and structure of a novel C-terminally amidated opioid peptide, amidorphin, from bovine adrenal medulla},
  author={Bernd R. Seizinger and D. C. Liebisch and Ch. Gramsch and Albert Herz and Eckard Weber and Christopher J Evans and F S Esch and Peter Böhlen},
  journal={Nature},
  year={1985},
  volume={313},
  pages={57-59}
}
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… 
Novel Opioid Peptide Amidorphin: Characterization and Distribution of Amidorphin‐Like Immunoreactivity in Bovine, Ovine, and Porcine Brain, Pituitary, and Adrenal Medulla
TLDR
Findings are indicative of a tissue‐specific processing of the proenkephalin A precursor, leading predominantly to authentic amidorphin in the adrenal medulla and further processing to smaller C‐terminal fragments in the brain and pituitary.
Measurement of Opioid Peptides in Biologic Fluids by Radioimmunoassay
TLDR
During the past decade, a large family of peptides with opioid activity have attracted interest as alleged neurotransmitters, as neurohormones, and as hormones, particularly within the hypothalamic — pituitary — adrenal axis.
Generation of a novel monoclonal antibody that recognizes the alpha (α)-amidated isoform of a valine residue
TLDR
P18C5 mAb-immunoreactivity exhibited a wide distribution along the neuroaxis of the rat brain, particularly in brain areas that did not cross-match with the neuronal distribution of known valine amide neuropeptides (α-MSH, adrenorphin, secretin, UCN1-2).
Identification of functionally important dipeptide in sequences of atypical opioid peptides
TLDR
In tests on ileum preparations of guinea pig and mouse vas deference in vitro, Tyr-Pro was devoid of opioid activity, which proved its indirect influence on opioid receptors.
Five Decades of Research on Opioid Peptides: Current Knowledge and Unanswered Questions
TLDR
The opioid peptides play complex and overlapping roles in a variety of systems, including reward pathways, and an important direction for research is the delineation of the role of individual peptides.
Distribution Pattern of Metorphamide Compared with Other Opioid Peptides from Proenkephalin and Prodynorphin in the Bovine Brain
TLDR
The results from this study suggest that the amounts of metorphamide in the bovine brain are sufficient to make this peptide a candidate for a physiologically significant endogenous μ opioid receptor ligand.
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References

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Novel C-terminally amidated opioid peptide in human phaeochromocytoma tumour
TLDR
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 is presented.
Metorphamide: isolation, structure, and biologic activity of an amidated opioid octapeptide from bovine brain.
  • E. Weber, F. Esch, C. Evans
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1983
TLDR
A synthetic replicate of metorphamide as well as several synthetic analogs were tested for opioid activity in several bioassays and binding assays, and metorphamia was found to have a high mu-binding activity.
Predominance of the amino-terminal octapeptide fragment of dynorphin in rat brain regions
TLDR
It is reported that dynorphin1–8, an amino-terminal fragment, which has only ∼3% of the opioid potency of dynorphIn–17, is present in up to 10-fold higher concentrations in brain than dynorphhi1–17 immunoreactivity, suggesting a close biosynthetic relationship between α-neo-endorphin and dynorph in–8.
Mechanism of C-terminal amide formation by pituitary enzymes
TLDR
Porcine pituitary contains an enzyme with the ability to convert peptides that terminate in glycine to the corresponding des-glycine peptide amide, and its mechanism of action involves dehydrogenation and hydrolysis of the glycine-containing substrate.
Identification in pituitary tissue of a peptide alpha-amidation activity that acts on glycine-extended peptides and requires molecular oxygen, copper, and ascorbic acid.
An enzymatic activity capable of producing an alpha-amidated peptide product from its glycine-extended precursor has been identified in secretory granules of rat anterior, intermediate, and neural
Specific non-opiate binding sites for human β-endorphin on the terminal complex of human complement
TLDR
This work reports the specific binding of human β-endorphin to both terminal complexes of human complement: the cytolytic, membrane-derived C5b–9(m) complex and the cy tolytically inactive, serum-derived SC5b-9 complex.
Isolation and Amino-acid Sequence of β-LPH from Sheep Pituitary Glands
TLDR
In the course of investigating a simplified procedure for the isolation of ACTH from sheep pituitary glands, a lipotropic peptide is obtained which is chemically distinct from ACTH and other known adenohypophyseal hormones.
Probable precursors of [Leu]enkephalin and [Met]enkephalin in adrenal medulla: peptides of 3-5 kilodaltons.
Adrenal chromaffin granules contain at least 10 peptides, ranging in size from 3 to 5 kilodaltons, that yield, upon digestion with trypsin, peptides that show specific binding to opiate receptors.
Cloning and sequence analysis of cDNA for bovine adrenal preproenkephalin
TLDR
The nucleotide sequence of cloned cDNA for preproenkephalin from bovine adrenal medulla indicates that the precursor protein contains four copies of Met-enke PHalin, a previously undetected opioid peptide.
Binding Characteristics of a Monoclonal β‐Endorphin Antibody Recognizing the N‐Terminus of Opioid Peptides
TLDR
Data indicate that for the binding to this antibody a tyrosine residue in position 61 is essential, and it thus recognizes a site that is of functional significance for many naturally occurring opioid peptides.
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