Plasmodium falciparum thioredoxins and glutaredoxins as central players in redox metabolism

Redox Rep. 2003;8(5):246-50. doi: 10.1179/135100003225002844.

Abstract

Over the last few years, an increasing number of different functions have been ascribed to small redox-active proteins like thioredoxins (Trx) and glutaredoxins (Grx). These functions include redox regulation of transcription and translation, antioxidant defence, involvement in protein folding and cellular signalling, and reduction of ribonucleotide reductase. In the malarial parasite Plasmodium falciparum, a classical Trx and a typical Grx have been described as well as a number of Trx- and Grx-like proteins including monothiol glutaredoxins. Furthermore, plasmoredoxin, a redox-active protein related to Trx, has been characterized; plasmoredoxin is unique for malarial parasites, therefore having great potential as diagnostic tool. In this minireview, we summarize the current knowledge on members of the thioredoxin superfamily and their function in the malarial parasite P. falciparum.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Forecasting
  • Glutaredoxins
  • Humans
  • Molecular Sequence Data
  • Oxidation-Reduction
  • Oxidoreductases*
  • Plasmodium falciparum / physiology*
  • Proteins / metabolism*
  • Protozoan Proteins / physiology*
  • Sequence Homology, Amino Acid
  • Thioredoxins / metabolism*

Substances

  • GLRX protein, human
  • Glutaredoxins
  • Proteins
  • Protozoan Proteins
  • Thioredoxins
  • Oxidoreductases