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Opioid and nonopioid components independently contribute to the mechanism of action of tramadol, an 'atypical' opioid analgesic.
TLDR
The results suggest that tramadol-induced antinociception is mediated by opioid (mu) and nonopioid (inhibition of monoamine uptake) mechanisms, and is consistent with the clinical experience of a wide separation between analgesia and typical opioid side effects.
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Serotonin and norepinephrine uptake inhibiting activity of centrally acting analgesics: structural determinants and role in antinociception.
TLDR
Investigation of a diverse group of opioids revealed that structurally identifiable subgroups inhibited the neuronal reuptake of these monoamines, suggesting a broader role for the combination of mu opioid affinity and 5-hydroxytryptamine uptake inhibition in the activity of other antinociceptive agents.
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Complementary and synergistic antinociceptive interaction between the enantiomers of tramadol.
TLDR
A rational explanation for the coexistence of dual components to tramadol-induced antinociception appears to be related to the different, but complementary and interactive, pharmacologies of its enantiomers and might form the basis for understanding its clinical profile.
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Molecular cloning and characterization of the human voltage-gated calcium channel alpha(2)delta-4 subunit.
TLDR
It is revealed that the alpha(2)delta-4 subunit has limited distribution in special cell types of the pituitary, adrenal gland, colon, and fetal liver and may play a distinct physiological role in select endocrine tissues remains to be demonstrated.
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Identification and biological evaluation of 4-(3-trifluoromethylpyridin-2-yl)piperazine-1-carboxylic acid (5-trifluoromethylpyridin-2-yl)amide, a high affinity TRPV1 (VR1) vanilloid receptor…
High throughput screening using the recombinant human TRPV1 receptor was used to identify a series of pyridinylpiperazine ureas (3) as TRPV1 vanilloid receptor ligands. Exploration of the…
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Molecular cloning and functional expression of the human sodium channel beta1B subunit, a novel splicing variant of the beta1 subunit.
TLDR
Functional studies in oocytes demonstrate that the human beta1B subunit increases the ionic current when coexpressed with the tetrodotoxin sensitive channel, NaV1.2, without significantly changing voltage dependent kinetics and steady-state properties, thus distinguishing it from the humanbeta1 and rat beta1A subunits.
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JNJ-20788560 [9-(8-Azabicyclo[3.2.1]oct-3-ylidene)-9H-xanthene-3-carboxylic Acid Diethylamide], a Selective Delta Opioid Receptor Agonist, Is a Potent and Efficacious Antihyperalgesic Agent That Does…
TLDR
Findings strongly recommend δ-opioid agonists such as JNJ-20788560 for the relief of inflammatory hyperalgesia.
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Molecular cloning and functional expression of the human sodium channel β1B subunit, a novel splicing variant of the β1 subunit
TLDR
Functional studies in oocytes demonstrate that the human β1B subunit increases the ionic current when coexpressed with the tetrodotoxin sensitive channel, NaV1.2, without significantly changing voltage dependent kinetics and steady-state properties, thus distinguishing it from the humanβ1 and rat β1A subunits.
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Oral activity of the growth hormone releasing peptide His-D-Trp-Ala-Trp-D-Phe-Lys-NH2 in rats, dogs and monkeys.
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The Novel, Orally Active, Delta Opioid RWJ-394674 Is Biotransformed to the Potent Mu Opioid RWJ-413216
TLDR
RWJ-394674 is a delta opioid receptor agonist that appears to augment its antinociceptive effect through biotransformation to a novel mu opioid receptor-selective agonist.
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