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Related Experiment Videos

Specific binding proteins for selenium in rat tissues.

B P Sani1, J L Woodard, M C Pierson

  • 1Kettering-Meyer Laboratory, Southern Research Institute, Birmingham, AL 35255-5305.

Carcinogenesis
|February 1, 1988
PubMed
Summary
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Selenium (Se) acts like a hormone, binding to a specific cellular protein (SeBP) in tissues like the liver and intestine. This SeBP facilitates selenium

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Nutritional Science

Background:

  • Selenium (Se) is a vital micronutrient with documented anticancer properties.
  • The precise mechanisms underlying selenium's biological actions remain largely unknown.
  • Investigating potential receptor-mediated pathways, similar to steroid hormones and retinoids.

Purpose of the Study:

  • To elucidate the mechanism of selenium's action by identifying cellular receptors.
  • To characterize a specific selenium-binding protein (SeBP) and its role in selenium transport and function.
  • To explore the binding affinities of various selenium compounds to SeBP.

Main Methods:

  • Detection and characterization of a 2S cellular binding protein (SeBP) for Na2[75Se]O3 in rat tissues.

Related Experiment Videos

  • Assessment of SeBP levels in different organs (liver, intestine, heart, uterus, spleen).
  • Competitive binding assays using various unlabeled selenium compounds and other molecules.
  • Scatchard analysis to determine binding affinity (dissociation constant).
  • Isoelectric focusing for protein characterization.
  • Identification of plasma transport protein using immunoprecipitation and chromatography.

    • Main Results:

    • A specific SeBP was identified in rat tissues, with highest concentrations in liver and intestine.
    • Oral administration of Na2[75Se]O3 led to the formation of a [75Se]SeBP complex in tissues.
    • SeBP exhibits moderate-high affinity for sodium selenite (Kd = 1.1 x 10(-7) M).
    • Selenium dioxide and selenocystine demonstrated high binding affinity, while selenomethionine showed poor affinity.
    • Biological activity of selenocompounds correlated with their SeBP binding affinities.
    • Thiol inhibitors blocked Se interaction with SeBP.
    • Serum albumin was identified as the primary plasma transport protein for selenium.

    Conclusions:

    • Selenium's biological functions may be mediated by a specific intracellular binding protein (SeBP).
    • SeBP plays a crucial role in the intracellular transport and potential action of selenium.
    • Plasma transport of selenium is facilitated by serum albumin, while intracellular transport involves SeBP.