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Receptor-binding properties of the peptides corresponding to the ACTH-like sequence of human pro-interleukin-1 alpha

V P Zav'yalov1, V A Maiorov, N G Safonova

  • 1Institute of Immunology, Moscow Region, Chekhov District, Russia.

Immunology Letters
|May 1, 1995
PubMed

The octapeptide Gly-Lys-Val-Leu-Lys-Lys-Arg-Arg (termed leukocorticotropin, LCT) corresponding to the ACTH-like sequence 81-88 of human pro-interleukin-1 alpha and its derivative Tyr-Gly-Lys-Val-Leu-Lys-Lys-Arg-Arg were synthesized. The 125I-labeled Tyr-LCT specifically interacts with one type of receptor on the surface of murine splenocytes (Kd = (1.45 +/- 0.04) x 10(-8) M, the number of binding sites is equal to 4500) and with two types of receptors on the surface of murine peritoneal macrophages (Kd1 = (5.9 +/- 1.0) x 10(-9) M and Kd2 = (2.6 +/- 2.2) x 10(-7) M). LCT and Tyr-LCT significantly increase the adenylate cyclase activity of murine peritoneal macrophages. The receptor binding and adenylate cyclase stimulation activity of LCT and Tyr-LCT are inhibited by ACTH (13-24).

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