Membrane and soluble forms of Fas (CD95) and Fas ligand in peripheral blood mononuclear cells and in plasma from human immunodeficiency virus-infected persons

J Infect Dis. 1998 Oct;178(4):1030-9. doi: 10.1086/515700.

Abstract

The expression of membrane-bound Fas ligand (FasL) and Fas in lymphocytes and monocytes and levels of soluble forms of FasL (sFasL) and Fas (sFas) in plasma from human immunodeficiency virus (HIV)-positive and -negative subjects was evaluated. Surface FasL was detectable on monocytes, but poorly so on lymphocytes, even in the presence of KB8301, a metalloproteinase inhibitor. Unexpectedly, monocytes of HIV-positive subjects expressed less FasL than those of HIV-negative volunteers. sFasL levels in plasma of HIV-positive persons were elevated and correlated with levels in plasma and with HIV RNA burden. sFas levels in plasma of HIV-positive subjects were also elevated and correlated with Fas expression in apoptotic lymphocytes. Finally, culture-induced lymphocyte apoptosis of HIV-positive subjects was enhanced by anti-Fas agonistic antibody but was not inhibited by anti-FasL blocking antibodies. These results suggest that significant dysregulation of both Fas and FasL occurs in HIV infection and contributes to increased sensitivity of lymphocytes to apoptosis.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Apoptosis*
  • Fas Ligand Protein
  • HIV Infections / immunology*
  • HIV-1 / immunology*
  • Humans
  • Leukocytes, Mononuclear / immunology*
  • Lymphocytes / immunology
  • Membrane Glycoproteins / blood*
  • Membrane Glycoproteins / genetics
  • Membrane Proteins / blood
  • Metalloendopeptidases / antagonists & inhibitors
  • Monocytes / immunology
  • Protease Inhibitors
  • RNA, Messenger / analysis
  • Signal Transduction
  • Solubility
  • fas Receptor / blood*

Substances

  • FASLG protein, human
  • Fas Ligand Protein
  • Membrane Glycoproteins
  • Membrane Proteins
  • Protease Inhibitors
  • RNA, Messenger
  • fas Receptor
  • Metalloendopeptidases