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Related Experiment Videos

Calumenin interacts with serum amyloid P component.

H Vorum1, C Jacobsen, B Honoré

  • 1Department of Medical Biochemistry, Ole Worms Allé, Building 170, University of Aarhus, DK-8000, Aarhus C, Denmark.

FEBS Letters
|January 13, 2000
PubMed
Summary

Researchers identified serum amyloid P component (SAP) interacting with calumenin, a secreted protein. This discovery suggests calumenin

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Immunology

Background:

  • Human calumenin is a novel, secreted, Ca(2+)-binding protein belonging to the EF-hand protein family.
  • Previous studies identified calumenin and its association with cellular transformation.
  • The extracellular functions of calumenin remained largely unexplored.

Purpose of the Study:

  • To investigate the extracellular interactions and functions of human calumenin.
  • To identify proteins that interact with calumenin in a Ca(2+)-dependent manner.

Main Methods:

  • Immobilization of recombinant calumenin onto a column.
  • Affinity chromatography using placental tissue extract.
  • Protein identification via amino acid sequencing.
  • Interaction characterization using surface plasmon resonance.

Main Results:

  • A single protein was eluted from the calumenin column in the presence of Ca(2+).
  • Amino acid sequencing identified the interacting protein as serum amyloid P component (SAP).
  • Surface plasmon resonance confirmed and characterized the calumenin-SAP interaction.

Conclusions:

  • Calumenin interacts with serum amyloid P component (SAP) in a Ca(2+)-dependent manner.
  • Calumenin may play a role in the immunological defense system.
  • The interaction suggests a potential involvement of calumenin in amyloidosis and amyloid deposit formation.

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