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Related Experiment Videos

Cellular transglutaminase has affinity for extracellular matrix.

H F Upchurch1, E Conway, M K Patterson

  • 1Samuel Roberts Noble Foundation, Inc., Ardmore, Oklahoma 73402.

In Vitro Cellular & Developmental Biology : Journal of the Tissue Culture Association
|November 1, 1987
PubMed
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Cellular transglutaminase (TGase) is an intracellular enzyme that binds to the extracellular matrix after cell membrane damage. This binding is linked to fibronectin and can be blocked by antibodies.

Area of Science:

  • Cell Biology
  • Biochemistry

Background:

  • Cellular transglutaminase (TGase) is primarily known as an intracellular enzyme.
  • Its localization and function outside the cell are less understood.

Purpose of the Study:

  • To investigate the extracellular localization and binding of cellular transglutaminase (TGase).
  • To determine the relationship between TGase, fibronectin, and the extracellular matrix.

Main Methods:

  • Immunofluorescence microscopy was used to visualize TGase in WI-38 cells.
  • Cell membrane perturbation was induced using Triton X-100 treatment.
  • Antibody blocking assays were performed using anti-fibronectin antibodies.

Main Results:

  • TGase was found to bind to the extracellular matrix following cell membrane perturbation.

Related Experiment Videos

  • TGase colocalized with fibronectin in the extracellular matrix.
  • Anti-fibronectin antibodies blocked the binding of TGase to the cell matrix.
  • Exogenous soluble TGase could bind to the extracellular matrix of fixed or untreated cells.

    • Conclusions:

    • Cellular transglutaminase (TGase) can be released and bind to the extracellular matrix.
    • Fibronectin plays a role in mediating TGase binding to the extracellular matrix.
    • The "particulate bound" form of TGase results from soluble enzyme binding to the extracellular matrix after cell rupture.