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The oxidative modification of cellular fibrin-stabilizing factor.
M A Rosenfeld1, A N Shchegolikhin2, V B Leonova2
1Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, ul. Kosygina 4, Moscow, 119334, Russia. markrosenfeld@rambler.ru.
Doklady. Biochemistry and Biophysics
|May 20, 2016
Summary
Oxidative modification significantly reduces the enzymatic activity of cellular fibrin-stabilizing factor (cFXIII) and its activated form (FXIIIa). Protein structural changes observed suggest a role for regulatory subunits in antioxidant defense.
Area of Science:
- Biochemistry
- Protein Chemistry
- Oxidative Stress
Background:
- Cellular fibrin-stabilizing factor (cFXIII) plays a crucial role in hemostasis.
- The impact of oxidative modification on cFXIII activity and structure was previously unknown.
- Understanding these modifications is vital for comprehending protein function under oxidative stress.
Purpose of the Study:
- To investigate the effects of induced oxidative modification on cellular fibrin-stabilizing factor (cFXIII).
- To analyze the enzymatic activity and structural integrity of oxidized cFXIII and FXIIIa.
- To explore the potential antioxidant role of cFXIII regulatory subunits.
Main Methods:
- Electrophoresis analysis to assess enzyme activity.
- Fourier-transform infrared (FTIR) spectroscopy to study protein structure.
- Induced oxidation protocols for cFXIII and FXIIIa.
Main Results:
- Oxidized cFXIII showed significantly reduced enzymatic activity upon conversion to FXIIIa.
- FXIIIa subjected to oxidation was completely inactive.
- FTIR spectroscopy revealed substantial changes in the chemical and spatial structures of both cFXIII and FXIIIa post-oxidation.
Conclusions:
- Induced oxidation profoundly impairs the enzymatic function of cFXIII and FXIIIa.
- Oxidation leads to significant alterations in protein structure.
- Findings support the hypothesis that regulatory subunits (B) of plasma fibrin-stabilizing factor contribute to antioxidant defense.
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