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Experimental and Imaging Techniques for Examining Fibrin Clot Structures in Normal and Diseased States
Published on: April 1, 2015
Structural and functional changes of fibrinogen due to aging
Nikola Gligorijević1, Martina Zámorová Križáková2, Ana Penezić1
1Institute for the Application of Nuclear Energy (INEP), Department of Metabolism, University of Belgrade, Banatska 31b, 11000 Belgrade, Serbia.
Aging alters fibrinogen structure and function. Healthy aging increases fibrinogen glycosylation, impacting its clotting time, a key factor in blood coagulation.
Area of Science:
- Biochemistry
- Gerontology
- Hematology
Background:
- Coagulation is vital for hemostasis, influenced by various factors.
- Fibrinogen is a primary coagulation factor.
- Understanding aging's impact on fibrinogen is crucial for healthy longevity.
Purpose of the Study:
- To investigate the influence of aging on fibrinogen structure and function.
- To analyze age-related changes in fibrinogen glycosylation and its consequences.
Main Methods:
- Fibrinogen isolation from plasma of healthy individuals aged 21-83.
- Lectin microarray analysis to assess glycosylation patterns.
- Spectrofluorimetric analysis for structural insights.
- Functional assays to evaluate clotting properties.
Main Results:
- Aging significantly increased fibrinogen glycosylation, particularly high-mannose/hybrid N-glycans and complex N-glycans with increased galactose and N-acetylglucosamine.
- Fibrinogen structure became more densely packed with age, but advanced glycation end products did not increase.
- Fibrinogen from older individuals showed reduced clotting time, correlating positively with age.
- No significant age-related differences were observed in clotting speed, clot density, fiber diameter, or porosity.
Conclusions:
- Glycosylation changes in fibrinogen during healthy aging affect its structure and function, notably altering clotting time.
- These findings contribute to understanding protein dynamics in healthy aging and longevity mechanisms.
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