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Interaction of Fluorescent Gonadotropin-releasing Hormone with Receptors in Cultured Pituitary Cells. by Z. Naor; D. Atlas; R.N. Clayton; D.S. Forman; A. Amsterdam; K.J. Catt is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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A fluorescent derivative of the gonadotropin-releasing hormone (GnRH) agonist analog, [D-Lys6]GnRH, was synthesized for receptor studies and shown to be biologically active. The rhodamine-derivatized peptide (Rh-GnRH) retained 40% of the receptor binding activity of [D-Lys6]GnRH, and 50% of the luteinizing hormone-releasing activity assayed in cultured pituitary cells. The fluorescent analog was employed to visualize the distribution of GnRH receptors in cultured pituitary cells, using the technique of video-intensified fluorescence microscopy. The binding of Rh-GnRH was confined to the large gonadotrophs which comprised 15% of the cell population. The specificity of the binding was shown by the absence of significant fluorescence in the presence of a 100-fold excess of [D-Lys6]GnRH, or when Rh-GnRH was incubated with choriocarcinoma, neuroblastoma, or 3T3 cell lines devoid of GnRH receptors. The interaction of Rh-GnRH with living pituitary cells was characterized by an initial diffuse distribution, followed by the formation of polar aggregates that later appeared to be internalized. These observations emphasize the value of fluorescent derivatives of GnRH for elucidating the cours

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Author

Z. Naor; D. Atlas; R.N. Clayton; D.S. Forman; A. Amsterdam; K.J. Catt

Publisher

Elsevier BV

Published

1981

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)