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Related Experiment Videos

Binding and processing of multimeric vitronectin by vascular endothelial cells

W Völker1, S Hess, P Vischer

  • 1Institute of Arteriosclerosis Research, University of Münster, Germany.

The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society
|December 1, 1993
PubMed
Summary

Multimeric vitronectin (VNmult) specifically binds to endothelial cells and is transported through them to the extracellular matrix. This process, mediated by heparin, highlights vitronectin

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Area of Science:

  • Biochemistry and Cell Biology
  • Extracellular Matrix Research
  • Glycoprotein Interactions

Background:

  • Vitronectin (VN) is a multifunctional adhesive glycoprotein.
  • VN transitions from a plasma form to a multimeric, heparin-binding form (VNmult).
  • The biological roles of VNmult, particularly its interactions with endothelial cells, require detailed investigation.

Purpose of the Study:

  • To investigate the interaction of multimeric vitronectin (VNmult) with porcine endothelial cells.
  • To elucidate the cellular uptake and trafficking pathways of VNmult.
  • To understand the role of heparin in VNmult binding and cell association.

Main Methods:

  • Time-dependent binding assays using radiolabeled VNmult.
  • Competition assays with heparin and plasma VN.

Related Experiment Videos

  • Cytochemical studies using VN-gold conjugates with electron and light microscopy.
  • Analysis of VNmult localization within endothelial cells and the extracellular matrix.

    • Main Results:

    • VNmult directly binds to the luminal face of endothelial cells in a time-dependent manner, a process inhibited by heparin.
    • Plasma VN shows minimal binding compared to VNmult.
    • At 37°C, VNmult is translocated through endothelial cells to the extracellular matrix, involving endocytosis, lysosomal compartments, and proteoglycans.
    • VNmult binding is reversible by heparin at 4°C, indicating specific cell-surface interactions.

    Conclusions:

    • VNmult exhibits specific binding and active transport across endothelial cells.
    • This pathway facilitates the routing of VNmult from circulation to extravascular spaces.
    • VNmult likely plays crucial adhesive and regulatory roles in these spaces, including roles in plasminogen activation and immune defense.