Abstract
The opioid peptide β-endorphin is released from the pituitary into the blood under physical or emotional stress; its target tissues, however, are unknown1. We report here the specific binding of human β-endorphin to both terminal complexes of human complement: the cytolytic, membrane-derived C5b–9(m) complex and the cytolytically inactive, serum-derived SC5b–9 complex. Binding is through the carboxy-terminus of β-endorphin rather than the amino-terminus, which is implicated in binding to opiate receptors. It is conceivable that the binding of β-endorphin to complement has physiological relevance in the adaptation of the immune system to stress.
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Schweigerer, L., Bhakdi, S. & Teschemacher, H. Specific non-opiate binding sites for human β-endorphin on the terminal complex of human complement. Nature 296, 572–574 (1982). https://doi.org/10.1038/296572a0
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DOI: https://doi.org/10.1038/296572a0
