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Related Experiment Videos

Osteonectin in matrix remodeling. A plasminogen-osteonectin-collagen complex

R J Kelm1, N A Swords, T Orfeo

  • 1University of Vermont, Department of Biochemistry, College of Medicine, Burlington 05405.

The Journal of Biological Chemistry
|December 2, 1994
PubMed
Summary

Osteonectin, a glycoprotein, binds to plasminogen and influences its activation. Bone osteonectin anchors plasminogen to collagen, suggesting a role in matrix proteolysis.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Extracellular Matrix Research

Background:

  • Osteonectin is an adhesive glycoprotein produced by osteoblasts, endothelial cells, and megakaryocytes.
  • Bone-derived and platelet-derived osteonectins exhibit distinct properties and affinities for collagen.
  • Both forms of osteonectin interact with plasminogen.

Purpose of the Study:

  • To investigate the binding characteristics of osteonectin and plasminogen.
  • To determine the influence of osteonectin on plasminogen activation.
  • To explore the role of bone osteonectin in anchoring plasminogen to collagen matrices.

Main Methods:

  • Equilibrium binding measurements using total internal reflection fluorescence spectroscopy.
  • Assays to measure plasmin generation rates.

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  • Inhibition studies using alpha 2-antiplasmin and epsilon-aminocaproic acid.

    • Main Results:

    • Osteonectin binds to plasminogen with specific affinities (Kd(app) for bone: 4.7 x 10(-8) M; for platelet: 1.2 x 10(-7) M).
    • Osteonectin enhances plasmin generation by tissue-type plasminogen activator.
    • Bone osteonectin facilitates plasminogen binding to collagen (Kd = 1.30 x 10(-7) M), an interaction inhibited by epsilon-aminocaproic acid.

    Conclusions:

    • Osteonectin interacts with plasminogen, potentially via its kringle 1 region.
    • Bone osteonectin anchors plasminogen to collagen matrices, unlike platelet osteonectin.
    • Osteonectin may regulate extracellular matrix proteolysis through its interactions with plasminogen and collagen.