Effect of Mechanical Strain on the Degradation of Fibrin Gel and Its Rheology
ORAL
Abstract
Fibrin plays an essential role in forming the structural support of a blood clot. Fibrin network
formation is promoted by the enzyme thrombin, which activates fibrinogen to become
self-assembling fibrin monomers, whereas the enzyme plasmin disintegrates fibrin polymers and is necessary
for the removal of clots. Within the body, clots frequently experience various forms of
mechanical strains. Therefore, understanding how mechanical strains, such as stretching and
compression, affect the degradation of fibrin is important. The goal of our study is to explore the
rheological consequence of stretching and compressing fibrin gels when subjected to plasmin
degradation. Our rheological measurements show that the shear storage modulus of a fibrin gel
incubated with plasmin when stretched by 20% decreases about 1.5 times faster than that of a
relaxed gel, but the compressed gels, also of 20% strain, degrade 0.6 times slower. Understanding
the origin of these findings would advance our understanding of how an enzyme’s activity can be
altered by mechanical strain of its substrate and provide insight into homeostatic control of blood-clotting.
formation is promoted by the enzyme thrombin, which activates fibrinogen to become
self-assembling fibrin monomers, whereas the enzyme plasmin disintegrates fibrin polymers and is necessary
for the removal of clots. Within the body, clots frequently experience various forms of
mechanical strains. Therefore, understanding how mechanical strains, such as stretching and
compression, affect the degradation of fibrin is important. The goal of our study is to explore the
rheological consequence of stretching and compressing fibrin gels when subjected to plasmin
degradation. Our rheological measurements show that the shear storage modulus of a fibrin gel
incubated with plasmin when stretched by 20% decreases about 1.5 times faster than that of a
relaxed gel, but the compressed gels, also of 20% strain, degrade 0.6 times slower. Understanding
the origin of these findings would advance our understanding of how an enzyme’s activity can be
altered by mechanical strain of its substrate and provide insight into homeostatic control of blood-clotting.
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Presenters
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Thomas T Dutta
Brown University
Authors
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Thomas T Dutta
Brown University
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Paul Mollenkopf
University of Pennsylvania
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Xuechen Shi
University of Pennsylvania
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Jay X Tang
Brown University
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Paul A Janmey
University of Pennsylvania