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Related Experiment Videos

Nucleolin is a calcium-binding protein.

James S C Gilchrist1, Bernard Abrenica, Patrick J DiMario

  • 1Department of Oral Biology and Physiology, Division of Stroke and Vascular Disease, University of Manitoba, Winnipeg, Manitoba, Canada.

Journal of Cellular Biochemistry
|April 12, 2002
PubMed
Summary
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Researchers identified a calcium-binding protein in rat liver nuclei, confirming it is nucleolin. This protein

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cell Biology

Background:

  • A prominent 110-kDa nuclear protein (p110) was purified from rat liver.
  • This protein exhibited characteristics of calcium (Ca2+) binding.

Purpose of the Study:

  • To identify the purified 110-kDa protein.
  • To characterize its calcium-binding properties and potential functions.

Main Methods:

  • Protein purification from rat liver nuclear extracts.
  • Stains-All staining, ruthenium red binding, and 45Ca2+ overlay assays.
  • Spin-dialysis for Ca2+ binding quantification.
  • N-terminal sequencing and 2D SDS-PAGE/IEF for protein identification and fragmentation analysis.
  • Immunostaining with anti-nucleolin antibody.

Related Experiment Videos

Main Results:

  • The purified 110-kDa protein (p110) demonstrated saturable Ca2+ binding (approx. 75 nmol Ca2+/mg protein, with half-maximal binding at 105 microM Ca2+).
  • p110 underwent autolytic fragmentation, but fragments retained Ca2+ binding capacity.
  • N-terminal sequencing and antibody staining confirmed p110 is nucleolin.
  • Autolysis selectively removed the basic C-terminal domain, leaving the acidic N-terminus responsible for Ca2+ binding.

Conclusions:

  • Rat liver nuclear nucleolin possesses annexin-like Ca2+-binding properties.
  • The acidic N-terminus of nucleolin is crucial for its Ca2+ binding.
  • Ca2+-dependent functions of nucleolin may involve chromatin structure regulation, potentially during apoptosis.