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Related Experiment Videos

The enigma PAI-2. Gene expression, evolutionary and functional aspects

F Bachmann1

  • 1Department of Medicine, Hôpital Nestlé, University of Lausanne Medical Center, Switzerland.

Thrombosis and Haemostasis
|July 1, 1995
PubMed
Summary
This summary is machine-generated.

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Type-2 plasminogen activator inhibitor (PAI-2), a serpin, has intracellular and secreted forms. Its gene regulation and potential roles in cell protection and programmed cell death are under investigation.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Type-2 plasminogen activator inhibitor (PAI-2) is a member of the serpin superfamily, sharing homology with other protease inhibitors.
  • PAI-2 exists in two forms: a 47 kDa intracellular nonglycosylated form and a ~60 kDa secreted glycosylated form.

Purpose of the Study:

  • To investigate the structural and regulatory aspects of PAI-2.
  • To explore the potential physiological functions of PAI-2, including cytoprotective roles and involvement in programmed cell death.

Main Methods:

  • Analysis of PAI-2 homology with other protease inhibitors.
  • Characterization of PAI-2's intracellular and secreted forms.
  • Identification of response elements in the PAI-2 gene promoter region.

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Main Results:

  • PAI-2 exhibits significant homology with leukocyte elastase inhibitor, placental thrombin inhibitor, and squamous cell carcinoma antigen.
  • The absence of a signal peptide in the PAI-2 gene correlates with its predominantly intracellular localization.
  • The PAI-2 promoter contains response elements for constitutive expression, phorbol esters, retinoic acid, cAMP, and glucocorticoids, including two AP-1 sites.

Conclusions:

  • PAI-2's gene expression is tightly regulated by various signaling pathways.
  • The precise physiological function of PAI-2 remains to be fully elucidated.
  • PAI-2 may play a role in cytoprotection and programmed cell death.