Abstract
During the past decade, a large family of peptides with opioid activity has been described. These peptides, also termed endorphins (an acronym for endogenous morphine) have attracted interest as alleged neurotransmitters, as neurohormones, and as hormones, particularly within the hypothalamic — pituitary — adrenal axis. These compounds have chemical homology in the NH2 terminal sequence Tyr-Gly-Gly-Phe-(Met or Leu), which forms the part of the molecule which is critical for opioid activity, and chemical heterogeneity in the COOH terminal sequences, which may contribute to receptor affinity and selectivity of interaction between opiate receptor types. A rather bewildering chemical complexity among these peptides is due to the fact that they derive from three distinct prohormones, each with a unique distribution in different cell types and neuronal pathways: proopiomelanocortin (with ß-endorphin), proenkephalin A (with seven enkephalin core sequences), and proenkephalin B (with three different dynorphin peptides); (Table 1 see also Sect. B).
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Nyberg, F., Christensson-Nylander, I., Terenius, L. (1987). Measurement of Opioid Peptides in Biologic Fluids by Radioimmunoassay. In: Patrono, C., Peskar, B.A. (eds) Radioimmunoassay in Basic and Clinical Pharmacology. Handbook of Experimental Pharmacology, vol 82. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71809-0_10
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