Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Arsenic binding proteins from human lymphoblastoid cells.

D B Menzel1, H K Hamadeh, E Lee

  • 1Department of Community and Environmental Medicine, University of California, Irvine 92697-1825, USA. menzel@uci.edu

Toxicology Letters
|April 30, 1999
PubMed
Summary

Researchers identified proteins that bind to toxic inorganic arsenic (AsIII) in human cells. These arsenic-binding proteins may play a role in arsenic toxicity and its biological actions.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

ES Series: Cancer Risk Assessment. 2. Physiological pharmacokinetic modeling.

Environmental science & technology·2009
Same author

Transgene integration into the same chromosome location can produce alleles that express at a predictable level, or alleles that are differentially silenced.

Genes & development·2000
Same author

Intactness of zona pellucida does not affect the secretion of a trypsin-like protease from mouse blastocyst.

Journal of Korean medical science·2000
Same author

Mater, a maternal effect gene required for early embryonic development in mice.

Nature genetics·2000
Same author

High-resolution transcript map of the region spanning D12S1629 and D12S312 at chromosome 12q13: triple A syndrome-linked region.

Genome research·2000
Same author

Effects of electric stimulation on bovine oocyte activation and embryo development in intracytoplasmic sperm injection procedure.

Journal of assisted reproduction and genetics·2000

Area of Science:

  • Toxicology
  • Molecular Biology
  • Biochemistry

Background:

  • Arsenic is a widespread contaminant in drinking water and food.
  • The precise mechanisms underlying inorganic arsenic toxicity remain largely unknown.
  • Understanding arsenic's molecular interactions is crucial for assessing health risks.

Purpose of the Study:

  • To isolate and identify proteins that bind to arsenite (AsIII), the toxic form of arsenic.
  • To investigate the induction of arsenic-binding proteins in human cells exposed to arsenite.
  • To explore the potential role of these proteins in arsenic's biological effects.

Main Methods:

  • Human lymphoblastoid cells were treated with arsenite (AsIII).
  • Proteins with high affinity for AsIII were isolated using a p-aminophenylarsine oxide affinity column.

Related Experiment Videos

  • Proteins were eluted using varying concentrations of 2-mercaptoethanol and identified by molecular weight and preliminary analysis.
  • Main Results:

    • At least four arsenic-binding proteins (50, 42, 38.5, and 19.5 kDa) were isolated.
    • Tubulin and actin were tentatively identified among the arsenic-binding proteins.
    • Heme oxygenase 1 was induced by AsIII but did not bind to the affinity column, indicating variable arsenic interactions.

    Conclusions:

    • Arsenite (AsIII) induces multiple proteins with varying affinities for arsenic in the +3 oxidation state.
    • These arsenic-binding proteins may act as high-affinity sites for AsIII.
    • The identified proteins could be involved in the toxic mechanisms of inorganic arsenic.