Specific nonopiate receptors for beta-endorphin.
Iodinated beta H-[2-D-alanine]endorphin exhibits specific binding to cultured human lymphocytes. The binding is inhibited by low concentrations of beta-endorphin and its D-alanine derivative, but is not affected by opiate agonists and antagonists, or by enkephalin analogs, beta-lipotropin, adrenocorticotrophic hormone, or alpha-melanocyte-stimulating hormone; this suggests the existence of a specific, non-opiate binding site (receptor) for beta-endorphin. The carboxy-terminal region of beta-endorphin is essential for this binding activity, since alpha-endorphin is not active. beta-Endorphin may be a circulating hormone with peripheral physiological effects that are not primarily mediated through interactions with opiate or enkephalin receptors.
D000595:Amino Acid Sequence; D002478:Cells, Cultured; D004723:Endorphins / Q000097:blood / Q000378:metabolism*; D006801:Humans; D008213:Lymphocyte Activation; D008214:Lymphocytes / Q000378:metabolism*; D011955:Receptors, Drug / Q000378:metabolism*; D011957:Receptors, Opioid / Q000378:metabolism; D013312:Stress, Physiological / Q000378:metabolism; D013329:Structure-Activity Relationship
D004723:Endorphins; D011955:Receptors, Drug; D011957:Receptors, Opioid