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Peroxynitrite induced fibrinogen site identification.

Yunjing Luo¹, Jianlong Shi¹, Jingjing Li¹

¹College of Life Science and Bioengineering, Beijing University of Technology, 100124 P.R. China.

Bio-Medical Materials and Engineering

|September 26, 2015

Summary

Peroxynitrite damages fibrinogen, a key protein in blood clots. This study identifies specific injury sites on fibrinogen, crucial for understanding thrombotic diseases.

Keywords:

Fibrinogen LC-MS/MS SDS-PAGE peroxynitrite tyrosine nitration

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Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

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Published on: November 30, 2018

Area of Science:

Biochemistry
Proteomics
Thrombosis Research

Background:

Peroxynitrite-induced fibrinogen nitration is linked to thrombotic diseases.
Limited information exists regarding specific fibrinogen injury sites from nitration.

Purpose of the Study:

To investigate structural changes and identify nitration sites in fibrinogen exposed to peroxynitrite.
To elucidate priority injury sites on fibrinogen using an improved in vivo-simulating method.

Main Methods:

Utilized an improved in vivo-simulating method to treat fibrinogen with peroxynitrite.
Employed SDS-PAGE to assess structural modifications, particularly on fibrinogen gamma (Fg) subunits.
Applied Liquid Chromatography-Mass Spectrometry/Mass Spectrometry (LC-MS/MS) for in-depth nitration site identification.

Main Results:

SDS-PAGE revealed that fibrinogen gamma subunits are susceptible to peroxynitrite-induced oxidative/nitrative modifications.
LC-MS/MS analysis identified specific priority nitration sites on the fibrinogen gamma chain (Fg I) at Y96, Y262, Y274, Y348, and Y363.
A large dataset confirmed these identified sites as primary targets of peroxynitrite attack.

Conclusions:

The study successfully identified key peroxynitrite-mediated nitration sites on fibrinogen.
These findings provide valuable data for biomedical studies related to fibrinogen modification and thrombotic disorders.
The identified sites offer potential targets for further research into the mechanisms of thrombosis.