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Published on: April 1, 2015
Emerging insights of fibrinogen glycation in cardiovascular disorders: A review
K Ameera1, Garima Choraria2, Shaik Basha1
1Department of Biophysics, Manipal School of Life Sciences, Manipal Academy of Higher Education, Manipal - 576104, Karnataka, India.
Insights
Protein glycation alters fibrinogen, increasing its thrombotic potential and contributing to cardiovascular disease (CVD). Glycated fibrinogen promotes thrombosis, inflammation, and oxidative stress, highlighting its role in CVD pathophysiology.
Area of Science:
- Biochemistry
- Molecular Biology
- Cardiovascular Research
Background:
- Cardiovascular diseases (CVDs) are a leading cause of global mortality, driven by metabolic, vascular, and inflammatory factors.
- Protein glycation is increasingly recognized as a key molecular pathway implicated in the development of CVDs.
Purpose of the Study:
- To comprehensively review the biochemistry of protein glycation.
- To elucidate the molecular mechanisms by which glycated fibrinogen contributes to CVD.
- To summarize characterization techniques for glycated fibrinogen.
Main Methods:
- Literature review and synthesis of existing research on protein glycation and fibrinogen.
- Analysis of biochemical pathways and molecular mechanisms.
- Evaluation of characterization techniques for glycated proteins.
Main Results:
- Glycation alters fibrinogen structure and function, reducing polymerization and altering clot architecture.
- Glycated fibrinogen exhibits increased resistance to fibrinolysis and enhanced thrombotic potential.
- Glycated fibrinogen contributes to oxidative stress, systemic inflammation, and immune dysregulation.
Conclusions:
- Glycated fibrinogen is a significant mediator in the pathophysiology of cardiovascular diseases.
- Glycated fibrinogen holds potential as a biomarker for CVD risk assessment.
- Targeting glycated fibrinogen may offer therapeutic strategies for CVD.
Abstract:
Cardiovascular diseases (CVDs) are the most prevalent cause of morbidity and mortality worldwide, arising from a complex interplay of metabolic, vascular, and inflammatory processes. Protein glycation has emerged as one of the molecular pathways contributing to the development of cardiovascular disease. Fibrinogen is an important protein in hemostasis and thrombosis, and its structure and function are altered upon glycation. Glycated fibrinogen has a lower polymerisation potential, different clot architecture, and is more resistant to fibrinolysis, as well as having greater thrombotic potential. Glycated fibrinogen can also increase oxidative stress, systemic inflammation, and alter the immune response. This review comprehensively evaluates the biochemistry of glycation, the molecular mechanisms and the characterisation techniques used to study glycated fibrinogen. We provide a systematic summary of the role of glycated fibrinogen in promoting thrombosis, oxidative stress, inflammation, and immune disturbance, establishing that glycated fibrinogen will be an important mediator of the pathophysiology of CVDs and a potential biomarker for risk assessment and possibly therapeutic targeting.
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