Study of Immunosuppressive Activity of a Synthetic Decapeptide Corresponding to an ACTH-Like Sequence of Human Immunoglobulin G1

E. V. Navolotskaya, T. A. Zargarova, T. N. Lepikhova, V. I. Turobov, R. I. Nurieva, N. V. Malkova, V. M. Lipkin, V. P. Zav'yalov

Research output: Contribution to journalReview articlepeer-review

5 Scopus citations

Abstract

The synthetic ACTH-like decapeptide H-Val-Lys-Lys-Pro-Gly- Ser-Ser-Val-Lys-Val-OH, corresponding to amino acid residues 11-20 of the variable part of the human IgG1 heavy chain (referred to as immunocortin) was found to have an immunosuppressive effect on cells in vitro: it inhibits blast transformation of mouse thymocytes and reduces spontaneous motility of mouse peritoneal macrophages as well as their bactericidal activity against the virulent bacterial strain Salmonella typhimurium 415. Tritium-labeled immunocortin binds with high affinity to ACTH receptors on thymocytes and macrophages (Kd 2.1 and 2.5 nM, respectively) and activates adenylate cyclase in these cells. Thus, the interaction of immunocortin with the target cell includes the following main steps: binding to the receptor, activation of adenylate cyclase, and elevation of the intracellular content of cAMP.

Original languageEnglish (US)
Pages (from-to)758-764
Number of pages7
JournalBiochemistry (Moscow)
Volume64
Issue number7
StatePublished - Jul 1999
Externally publishedYes

Keywords

  • Adenylate cyclase
  • Adrenocorticotropic hormone (ACTH)
  • Immune system
  • Immunoglobulin G (IgG)
  • Peptides
  • Peritoneal macrophages
  • Receptors
  • Thymocytes

ASJC Scopus subject areas

  • Biochemistry

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