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Annual Review of Pharmacology and Toxicology, 1979
Opioid peptides are endogenous or synthetic peptides, with a spectrum of pharmacological activity similar to that of morphine and other narcotic agonist drugs. The designation opioid peptide can be made if (a) it produces morphine-like, naloxone reversible effects in several in vitro bioassay sys tems such as the guinea pig ileum (1), the cat ...
A, Beaumont, J, Hughes
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Opioid peptides are endogenous or synthetic peptides, with a spectrum of pharmacological activity similar to that of morphine and other narcotic agonist drugs. The designation opioid peptide can be made if (a) it produces morphine-like, naloxone reversible effects in several in vitro bioassay sys tems such as the guinea pig ileum (1), the cat ...
A, Beaumont, J, Hughes
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Cancer and Metastasis Reviews, 2004
Opioid and somatostatin systems are two main inhibitory systems in mammals implicated in a variety of processes from hormone secretion to the modulation of cell proliferation. Opioids and opioid receptors were found in a great diversity of primary human tumors and in various cancer cell lines.
Jakub, Fichna, Anna, Janecka
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Opioid and somatostatin systems are two main inhibitory systems in mammals implicated in a variety of processes from hormone secretion to the modulation of cell proliferation. Opioids and opioid receptors were found in a great diversity of primary human tumors and in various cancer cell lines.
Jakub, Fichna, Anna, Janecka
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Cyclization in Opioid Peptides
Current Drug Targets, 2013Endogenous opioid peptides have been studied extensively as potential therapeutics for the treatment of pain. The major problems of using natural opioid peptides as drug candidates are their poor receptor specificity, metabolic instability and inability to reach the brain after systemic administration.
Justyna, Piekielna +3 more
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Pigment Cell Research, 1996
Opioid peptides and other Tyr‐NH2‐terminal peptides are substrates in vitro for mushroom and sepia tyrosinase, giving rise to synthetic melanins retaining the peptide moiety (opiomelanins). The melanopeptides are characterized by a total solubility in hydrophylic solvents at neutral and basic pH. Opioid peptides (enkephalins, endorphins, and esorphins),
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Opioid peptides and other Tyr‐NH2‐terminal peptides are substrates in vitro for mushroom and sepia tyrosinase, giving rise to synthetic melanins retaining the peptide moiety (opiomelanins). The melanopeptides are characterized by a total solubility in hydrophylic solvents at neutral and basic pH. Opioid peptides (enkephalins, endorphins, and esorphins),
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1988
The discovery of endogenous opioids has begun an intricate saga involving multiple ligands and multiple receptors that form an extensive neuronal network in both the central and peripheral nervous systems. This intricacy is reflected in the complex pharmacology and diverse physiological effects of opioids in mammals.
Christopher J. Evans +2 more
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The discovery of endogenous opioids has begun an intricate saga involving multiple ligands and multiple receptors that form an extensive neuronal network in both the central and peripheral nervous systems. This intricacy is reflected in the complex pharmacology and diverse physiological effects of opioids in mammals.
Christopher J. Evans +2 more
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Biosynthesis of Opioid Peptides
1990The endogenous opioid peptides all contain the enkephalin sequence Tyr-Gly-Gly-Phe-Met and Tyr-Gly-Gly-Phe-Leu at their aminoterminus. Three distinct families of these peptides (endorphins, enkephalins and dynorphins) are present in different neuronal pathways within the central nervous system. Molecular genetics have shown that these three families of
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