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  • The thioredoxin system in retroviral infection and apoptosis
  • Masutani H; Ueda S; Yodoi J
  • Cell Death Differ 2005[Aug]; 12 Suppl 1 (): 991-8
  • Human thioredoxin (TRX) was first identified in human T-cell leukemia virus type I (HTLV-I)-positive T-cell lines and is associated with the pathophysiology of retroviral infections. TRX is a vital component of the thiol-reducing system and regulates various cellular function (redox regulation). Members of the TRX system regulate apoptosis through a wide variety of mechanisms. A family of thioredoxin-dependent peroxidases (peroxiredoxins) protects against apoptosis by scavenging hydrogen peroxide. Thioredoxin 2 is a critical regulator of cytochrome c release and mitochondrial apoptosis; transmembrane thioredoxin-related molecule (TMX) has a protective role in endoplasmic reticulum (ER) stress-induced apoptosis. TRX interacts with apoptosis signal-regulating kinase 1 (ASK1) and is a sensor of oxidative stress. Thioredoxin binding protein-2/vitamin D(3) upregulated protein 1 is a growth suppressor and its expression is suppressed in HTLV-I-transformed cells. Studies of these molecules of the TRX system provide novel insights into the apoptosis associated with retroviral diseases.
  • |*Apoptosis[MESH]
  • |*Oxidative Stress[MESH]
  • |Animals[MESH]
  • |Glutathione/metabolism[MESH]
  • |HIV Infections/metabolism[MESH]
  • |HTLV-I Infections/metabolism[MESH]
  • |Humans[MESH]
  • |MAP Kinase Kinase Kinase 5/metabolism[MESH]
  • |Membrane Proteins/metabolism[MESH]
  • |Peroxidases/metabolism[MESH]
  • |Peroxiredoxins[MESH]
  • |Retroviridae Infections/enzymology/*metabolism/pathology[MESH]
  • |Thioredoxins/*metabolism[MESH]

  • *{{pmid15818395}}
    *<b>[ The thioredoxin system in retroviral infection and apoptosis ]</b> Cell Death Differ 2005; 12 Suppl 1() ; 991-8 Masutani H; Ueda S; Yodoi J


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    Cell Death Differ

    991 .12 Suppl 1 2005