Journal of Biological Chemistry · 1979 · 367 citations · 14 references
MedicineBiochemistryPharmacologyNeurochemistryNeuropharmacologySignal TransductionAnalgesic PharmacologyNeurochemical PharmacologyNeuropeptide PharmacologyNeurotransmitter ReceptorsOpioid AnalgesicsOpioid PharmacologyAdenylate Cyclase RegulationAdenylate Cyclase SignalingAdenylyl Cyclase RegulationEndogenous OpioidsGluten ProteinsOpioid Peptide PharmacologyOpioid Receptor BindingReversible Inhibition
Peptides with opioid activity are found in pepsin hydrolysates of wheat gluten and alpha-casein. The opioid activity of these peptides was demonstrated by use of the following bioassays: 1) naloxone-reversible inhibition of adenylate cyclase in homogenates of neuroblastoma X-glioma hybrid cells; 2) naloxone-reversible inhibition of electrically stimulated contractions of the mouse vas deferens; 3) displacement of [3H]dihydromorphine and [3H-Tyr, dAla2]met-enkephalin amide from rat brain membranes. Substances which stimulate adenylate cyclase and increase the contractions of the mouse vas deferens but do not bind to opiate receptors are also isolated from gluten hydrolysates. It is suggested that peptides derived from some food proteins may be of physiological importance.
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Identification of two related pentapeptides from the brain with potent opiate agonist activity
Joel W. Hughes, Terry Smith, H. W. Kosterlitz et al. · Nature · 1975 · 3.8K citations
C fragment of lipotropin has a high affinity for brain opiate receptors
A.F. Bradbury, D.G. Smyth, Christopher R. Snell et al. · Nature · 1976 · 486 citations