Abstract
Studies of luteinizing hormone-releasing hormone (LHRH) have revealed several structural requirements for its biological activity1. Shortening of the decapeptide leads to loss of activity; positions 1, 6 and 10 are regarded as important in that they have a high affinity for the hormone receptor, and positions 2 and 3 (His-Trp) are thought to comprise the active centre of the molecule (replacement of His or Trp produces the most effective antagonists). Using a potent agonist analogue of the decapeptide, Glu-His-Trp-Ser-Tyr-D-Lys-Leu-Arg-Pro-NHEt, coupled to ferritin, we have demonstrated previously the binding, aggregation and internalization of bound hormone using dissociated pituitary cells2. Similar processes occur for other biologically active peptides, for example, insulin3 and epidermal growth factor (EGF)4. Using a pure antagonist in the simpler LHRH system we now show that the N-terminal portion of the molecule is important for receptor aggregation and that dimerization of occupied LHRH receptors is a necessary early stage in the release of luteinizing hormone.
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Gregory, H., Taylor, C. & Hopkins, C. Luteinizing hormone release from dissociated pituitary cells by dimerization of occupied LHRH receptors. Nature 300, 269–271 (1982). https://doi.org/10.1038/300269a0
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DOI: https://doi.org/10.1038/300269a0
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