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Hypochlorite-Induced Damage of Plasminogen Molecules: Structural-Functional Disturbance.
A D Vasilyeva1, L V Yurina2, A N Shchegolikhin2
1Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, 119334, Moscow, Russia. alexandra.d.vasilyeva@gmail.com.
Doklady. Biochemistry and Biophysics
|November 27, 2019
Summary
Oxidative modifications in plasminogen were analyzed using mass spectrometry. Plasminogen exhibits high tolerance to oxidation due to its structure and methionine residues acting as reactive oxygen species traps.
Area of Science:
- Biochemistry
- Proteomics
- Molecular Biology
Background:
- Plasminogen is a key serine protease in intravascular thrombolysis.
- Understanding plasminogen's response to oxidative stress is crucial for its physiological role.
Purpose of the Study:
- To investigate the oxidative modifications of plasminogen under induced oxidation.
- To elucidate the structural changes and protective mechanisms of plasminogen against oxidation.
Main Methods:
- High-resolution mass spectrometry was employed to identify oxidative modifications.
- Fourier-transform infrared (FTIR) spectroscopy was used to analyze secondary structure changes.
Main Results:
- The study provides the first high-resolution mass spectrometry data on plasminogen oxidative modifications.
- Oxidation induced rearrangements in plasminogen's secondary structure.
- Plasminogen demonstrated significant tolerance to oxidative conditions.
Conclusions:
- The closed conformation and methionine residues acting as reactive oxygen species (ROS) traps contribute to plasminogen's oxidative tolerance.
- These findings offer insights into plasminogen's stability and function under oxidative stress.
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