Protein degradation and apoptotic death in lymphocytes during Fiv infection: activation of the ubiquitin-proteasome proteolytic system

Exp Cell Res. 1999 May 1;248(2):381-90. doi: 10.1006/excr.1999.4410.

Abstract

The movement of a cell through the sequential phases of apoptosis is accompanied by a progressive decrease in cell size with loss in protein mass. In lymphocytes from Hiv-infected persons, protein loss during apoptosis is due to increased protein degradation rather than decreased synthesis. To identify and characterize the proteolytic enzymes or enzyme systems involved in this process, we studied several features of protein turnover in lymphocytes from peripheral blood and lymph nodes during the natural and experimental infection by feline immunodeficiency virus (Fiv). This animal model allowed us to integrate in vivo results with in vitro observations of protein damage. Here we report that protein breakdown in apoptotic cells is concomitant with the activation of the ATP and ubiquitin-dependent multicatalytic system (proteasome). We suggest that proteasome activation is part of the proteolytic cascade in the execution phases of apoptosis in AIDS.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Apoptosis
  • Cats
  • Cysteine Endopeptidases / metabolism*
  • Female
  • Half-Life
  • Immunodeficiency Virus, Feline / growth & development*
  • Lentivirus Infections / metabolism*
  • Lymph Nodes / metabolism*
  • Lymph Nodes / pathology
  • Lymphocytes / metabolism*
  • Lymphocytes / pathology
  • Male
  • Multienzyme Complexes / metabolism*
  • Proteasome Endopeptidase Complex
  • Proteins / metabolism
  • Ubiquitins / metabolism*

Substances

  • Multienzyme Complexes
  • Proteins
  • Ubiquitins
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex