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Related Experiment Videos

Orphan selenoproteins.

R F Burk1, K E Hill

  • 1Department of Medicine and Clinical Nutrition Research Unit, Vanderbilt University School of Medicine, Nashville, TN 37232-2279, USA. raymond.burk@mcmail.vanderbilt.edu

Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology
|May 20, 1999
PubMed
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This study explores two "orphan" selenoproteins, Selenoprotein P and Selenoprotein W, which contain selenium. Their functions suggest roles in protecting against cellular oxidant injury, highlighting selenium

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • Selenoproteins incorporate selenium, with most synthesized via UGA codon decoding as selenocysteine.
  • Biochemical functions are known for nine of twelve characterized animal selenoproteins.
  • Two selenoproteins, Selenoprotein P and Selenoprotein W, remain functionally uncharacterized.

Purpose of the Study:

  • To discuss the characteristics and potential functions of two
  • orphan
  • selenoproteins: Selenoprotein P and Selenoprotein W.
  • To explore the role of selenocysteine's redox properties in protein function.
  • To predict the discovery of novel selenium-dependent proteins.

Main Methods:

  • Characterization of Selenoprotein P and Selenoprotein W.

Related Experiment Videos

  • Analysis of protein structure and cellular localization.
  • Investigation of binding partners (heparin, glutathione).
  • Correlation of plasma Selenoprotein P levels with protection against diquat-induced liver injury.

    • Main Results:

    • Selenoprotein P is an extracellular glycoprotein with multiple selenocysteines, binding heparin and associating with endothelial cells. Two isoforms exist.
    • Plasma Selenoprotein P concentration is linked to protection against diquat liver injury, indicating an antioxidant role.
    • Selenoprotein W is a small intracellular protein with one selenocysteine, binding glutathione and potentially involved in oxidant defense.

    Conclusions:

    • The identified selenoproteins, Selenoprotein P and Selenoprotein W, exhibit properties consistent with oxidant defense roles.
    • The unique thiol-redox capabilities of selenocysteine likely underpin these protective functions.
    • Further discoveries of proteins utilizing selenium's chemical properties are anticipated.