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Related Experiment Videos

Calreticulin binding affinity for glycosylated laminin

J M McDonnell1, G E Jones, T K White

  • 1Randall Institute, King's College, London WC2B 5RL, United Kingdom.

The Journal of Biological Chemistry
|April 5, 1996
PubMed
Summary

Calreticulin exhibits lectin-like properties, binding specifically to glycosylated laminin in a calcium-dependent manner. This interaction supports calreticulin's role in recognizing laminin within and on the cell surface.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Calreticulin, a molecular chaperone, possesses lectin-like properties, binding to immature carbohydrates on nascent glycoproteins.
  • Its structural similarity to calnexin suggests overlapping chaperone functions.
  • A cell surface form of calreticulin also demonstrates lectin-like activity, binding specific oligomannosides.

Purpose of the Study:

  • To investigate the interaction between calreticulin and laminin.
  • To confirm the lectin-like properties of calreticulin in binding to laminin.
  • To elucidate the role of calcium in this interaction.

Main Methods:

  • Surface plasmon resonance (SPR) was employed to analyze the binding kinetics and affinity.
  • Binding assays were performed using glycosylated and unglycosylated laminin, as well as bovine serum albumin.

Related Experiment Videos

  • The effect of calcium ions and EDTA on calreticulin-laminin interaction was assessed.

    • Main Results:

    • Calreticulin specifically bound to glycosylated laminin but not to unglycosylated laminin or bovine serum albumin.
    • The binding of calreticulin to glycosylated laminin was calcium-dependent and inhibited by EDTA.
    • Scatchard and kinetic analyses provided quantitative measures of the association constant and rate.

    Conclusions:

    • The study confirms the lectin-like properties of calreticulin.
    • Calreticulin plays a role in recognizing laminin, both intracellularly and on the cell surface.
    • Calcium ions are crucial for the specific binding of calreticulin to glycosylated laminin.