The pro-enkephalin A derivative, peptide E, is centrally processed to active fragments

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Abstract

Recent evidence has indicated that all known opioid peptides are derived from one of 3 large precursor proteins, pro-opiomelanocortin, proenkephalin A, and proenkephalin B. The isolation and characterization of enkephalin-related peptides, derived from proenkephalin A, such as peptide E, BAM 22P, and BAM12P resulted from the discovery of enkephalin-like immunoreactivity within the adrenal medulla. Previous studies in our laboratory on the pro-opiomelanocortin derived peptide, β-endorphin, has shown that the presence of pairs of basic amino acids along this high molecular weight precursor leads to specific enzymatic cleavages by membrane bound enzymes into active peptide fragments. Based on the studies we chose to investigate if the proenkephalin A derivative, peptide E, is also processed centrally to active fragments.

Original languageEnglish (US)
Pages (from-to)577-581
Number of pages5
JournalProceedings of the Western Pharmacology Society
VolumeVOL. 27
StatePublished - 1984

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Pro-Opiomelanocortin
Enkephalins
Endorphins
Basic Amino Acids
Peptides
Peptide Fragments
Adrenal Medulla
Protein Precursors
Opioid Peptides
Molecular Weight
Membranes
peptide E (adrenal medulla)
proenkephalin
Enzymes
BAM 22P

ASJC Scopus subject areas

  • Pharmacology

Cite this

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title = "The pro-enkephalin A derivative, peptide E, is centrally processed to active fragments",
abstract = "Recent evidence has indicated that all known opioid peptides are derived from one of 3 large precursor proteins, pro-opiomelanocortin, proenkephalin A, and proenkephalin B. The isolation and characterization of enkephalin-related peptides, derived from proenkephalin A, such as peptide E, BAM 22P, and BAM12P resulted from the discovery of enkephalin-like immunoreactivity within the adrenal medulla. Previous studies in our laboratory on the pro-opiomelanocortin derived peptide, β-endorphin, has shown that the presence of pairs of basic amino acids along this high molecular weight precursor leads to specific enzymatic cleavages by membrane bound enzymes into active peptide fragments. Based on the studies we chose to investigate if the proenkephalin A derivative, peptide E, is also processed centrally to active fragments.",
author = "Davis, {Thomas P} and Frank Porreca and A. Dray",
year = "1984",
language = "English (US)",
volume = "VOL. 27",
pages = "577--581",
journal = "Proceedings of the Western Pharmacology Society",
issn = "0083-8969",
publisher = "Western Pharmacology Society",

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T1 - The pro-enkephalin A derivative, peptide E, is centrally processed to active fragments

AU - Davis, Thomas P

AU - Porreca, Frank

AU - Dray, A.

PY - 1984

Y1 - 1984

N2 - Recent evidence has indicated that all known opioid peptides are derived from one of 3 large precursor proteins, pro-opiomelanocortin, proenkephalin A, and proenkephalin B. The isolation and characterization of enkephalin-related peptides, derived from proenkephalin A, such as peptide E, BAM 22P, and BAM12P resulted from the discovery of enkephalin-like immunoreactivity within the adrenal medulla. Previous studies in our laboratory on the pro-opiomelanocortin derived peptide, β-endorphin, has shown that the presence of pairs of basic amino acids along this high molecular weight precursor leads to specific enzymatic cleavages by membrane bound enzymes into active peptide fragments. Based on the studies we chose to investigate if the proenkephalin A derivative, peptide E, is also processed centrally to active fragments.

AB - Recent evidence has indicated that all known opioid peptides are derived from one of 3 large precursor proteins, pro-opiomelanocortin, proenkephalin A, and proenkephalin B. The isolation and characterization of enkephalin-related peptides, derived from proenkephalin A, such as peptide E, BAM 22P, and BAM12P resulted from the discovery of enkephalin-like immunoreactivity within the adrenal medulla. Previous studies in our laboratory on the pro-opiomelanocortin derived peptide, β-endorphin, has shown that the presence of pairs of basic amino acids along this high molecular weight precursor leads to specific enzymatic cleavages by membrane bound enzymes into active peptide fragments. Based on the studies we chose to investigate if the proenkephalin A derivative, peptide E, is also processed centrally to active fragments.

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