Type I interferons induce proteins susceptible to act as thyroid receptor (TR) corepressors and to signal the TR for destruction by the proteasome: possible etiology for unexplained chronic fatigue

Med Hypotheses. 2003 Feb;60(2):175-80. doi: 10.1016/s0306-9877(02)00353-5.

Abstract

In some patients complaining of chronic fatigue such as those suffering from the chronic fatigue syndrome (CFS), no underlying physical cause can be clearly identified and they typically present a normal thyroid function. Several studies indicate a dysregulation in the type I interferons (IFN-alpha/beta) pathway in CFS resulting in a sustained upregulation of 2('),5(')-oligoadenylate synthetases (2-5OAS). Likewise, patients treated with IFN-alpha/beta usually complain of severe fatigue as a limiting side effect. Beside the 2-5OAS, IFN-alpha/beta induce also the expression of three closely related proteins of unknown function termed the 2-5OAS-like (2-5OASL) proteins. The amino acid sequences of the 2-5OASL proteins display 96% identity with the partial sequence of the thyroid receptor interacting protein (TRIP) 14, further contain two typical thyroid hormone receptor (TR) coregulator domains and feature two ubiquitin C-terminal domains. From these observations, we raise the hypothesis that the 2-5OASL proteins are TRIPs capable of, respectively, repressing TR transactivation and/or signaling the receptor for destruction by the proteasome. Such molecular mechanisms could explain the development of a clinical hypothyroid state in presence of a normal thyroid function.

MeSH terms

  • 2',5'-Oligoadenylate Synthetase / metabolism
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Cysteine Endopeptidases / metabolism*
  • DNA-Binding Proteins / metabolism
  • Fatigue Syndrome, Chronic / etiology*
  • Humans
  • Interferon Type I / metabolism
  • Interferon Type I / physiology*
  • Models, Biological
  • Molecular Sequence Data
  • Multienzyme Complexes / metabolism*
  • Proteasome Endopeptidase Complex
  • Protein Binding
  • Protein Structure, Tertiary
  • Receptors, Thyroid Hormone / metabolism*
  • Sequence Homology, Amino Acid
  • Signal Transduction

Substances

  • DNA-Binding Proteins
  • Interferon Type I
  • Multienzyme Complexes
  • Receptors, Thyroid Hormone
  • OASL protein, human
  • 2',5'-Oligoadenylate Synthetase
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex