A synthetic thiol molecule releasing N-acetyl-l-cysteine and cysteamine drives early up-regulation of immunoproteasome subunits in the lymph nodes of mice infected with LP-BM5 leukemia retrovirus

Biochim Biophys Acta Mol Basis Dis. 2024 Jan;1870(1):166918. doi: 10.1016/j.bbadis.2023.166918. Epub 2023 Oct 12.

Abstract

Thiol molecules have been recently re-considered as drug candidates in viral infections because of their ability to induce redox changes which interfere with virus life cycle and modulate the host immune response. Little is known about the molecular mechanisms of their immunomodulatory properties. Here we show that I-152, a thiol molecule metabolized to release N-acetyl-l-cysteine and cysteamine and acting as a pro-glutathione agent, causes early up-regulation of immunoproteasome subunits in the lymph nodes of murine leukemia virus infected mice. This evidence suggests that the immunoproteasome may be modulated by thiol-based compounds with important implications in understanding redox-controlled immunoregulation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylcysteine / metabolism
  • Acetylcysteine / pharmacology
  • Animals
  • Cysteamine / pharmacology
  • Leukemia*
  • Lymph Nodes / pathology
  • Mice
  • Murine Acquired Immunodeficiency Syndrome* / pathology
  • Retroviridae / metabolism
  • Sulfhydryl Compounds
  • Up-Regulation

Substances

  • Acetylcysteine
  • Cysteamine
  • Sulfhydryl Compounds