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Peroxide-Induced Damage to Plasminogen Molecules.

A D Vasilyeva1, V S Ivanov2, L V Yurina2

  • 1Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russia. alexandra.d.vasilyeva@gmail.com.

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|December 30, 2021
PubMed
Summary
This summary is machine-generated.

Hydrogen peroxide oxidizes plasminogen, a key enzyme in clot dissolution. This study identifies specific amino acid targets and reveals that plasminogen oxidation reduces its fibrinolytic activity.

Keywords:
antioxidant methionineselectrophoresishydrogen peroxidemass spectrometryoxidationoxidation sitesplasminogen/plasmin

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Plasminogen is the precursor to plasmin, an enzyme crucial for fibrin clot breakdown.
  • Plasmin's activity is vital for various physiological processes, including wound healing and tissue remodeling.
  • Oxidative stress can impact protein structure and function, potentially affecting plasminogen's role.

Purpose of the Study:

  • To identify post-translational modifications in plasminogen induced by hydrogen peroxide.
  • To investigate the impact of plasminogen oxidation on its fibrinogenolytic activity.
  • To explore the potential antioxidant role of methionine residues in plasminogen.

Main Methods:

  • Gas chromatography-mass spectrometry (GC-MS) was employed to analyze plasminogen structure.
  • Plasminogen was treated with physiologically relevant concentrations of hydrogen peroxide.
  • Fibrinogenolytic activity assays were performed to assess plasmin function post-oxidation.

Main Results:

  • Methionine and tryptophan residues were identified as primary targets of oxidation in plasminogen.
  • Oxidation of plasminogen resulted in a dose-dependent decrease in fibrinogenolytic activity.
  • Formation of fibrinogen degradation products was observed, indicating reduced plasmin efficacy.

Conclusions:

  • Hydrogen peroxide induces specific oxidative modifications in plasminogen, targeting methionine and tryptophan residues.
  • Oxidized plasminogen exhibits diminished activity in degrading fibrinogen.
  • Methionine residues may play a protective, antioxidant role against plasminogen oxidative modification.