Strain enhancement of elastic modulus in fine fibrin clots. 1988

M D Bale, and J D Ferry
Department of Chemistry, University of Wisconsin, Madison.

Fine fibrin clots, prepared at pH 8.5, ionic strength 0.45, with minimal lateral aggregation of protofibrils, and ligated (cross-linked) by factor XIIIa, were subjected to constant static shear strain (gamma) with superposed small oscillating strains. The incremental shear modulus (dynamic storage modulus) measured in the oscillating deformations was strain-independent at small static strains (up to about 0.1) and approximately equal to the static modulus. At higher static strains, it increased rapidly, up by a factor of 5 to 8 at gamma = 0.35. Comparison with earlier data on unligated clots showed that the enhancement of stiffness was independent of ligation except at very high strains. The enhancement is attributed to additional forced contacts between network fibers as the strands are bent and oriented. When the static strain was maintained for up to one day, in a clot ligated by factor XIIIa the enhanced incremental modulus remained constant or decreased slightly, and after removal of stress the clot returned almost to its original shape. This contrasts with the behavior of unligated clots, where most of the enhancement was progressively lost as the incremental modulus fell toward its small-strain value, and there was a substantial permanent deformation after the removal of stress. The latter behavior has been attributed to gradual severance of network strands at high strains, followed by their rejoining in relaxed configurations, but leaving some structural damage that is only very slowly recovered in the resting state. Ligation of protofibrils evidently eliminates the possibility of strand rupture.

UI MeSH Term Description Entries
D004548 Elasticity Resistance and recovery from distortion of shape.
D005337 Fibrin A protein derived from FIBRINOGEN in the presence of THROMBIN, which forms part of the blood clot. Antithrombin I
D005340 Fibrinogen Plasma glycoprotein clotted by thrombin, composed of a dimer of three non-identical pairs of polypeptide chains (alpha, beta, gamma) held together by disulfide bonds. Fibrinogen clotting is a sol-gel change involving complex molecular arrangements: whereas fibrinogen is cleaved by thrombin to form polypeptides A and B, the proteolytic action of other enzymes yields different fibrinogen degradation products. Coagulation Factor I,Factor I,Blood Coagulation Factor I,gamma-Fibrinogen,Factor I, Coagulation,gamma Fibrinogen
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D001696 Biomechanical Phenomena The properties, processes, and behavior of biological systems under the action of mechanical forces. Biomechanics,Kinematics,Biomechanic Phenomena,Mechanobiological Phenomena,Biomechanic,Biomechanic Phenomenas,Phenomena, Biomechanic,Phenomena, Biomechanical,Phenomena, Mechanobiological,Phenomenas, Biomechanic
D013927 Thrombosis Formation and development of a thrombus or blood clot in BLOOD VESSELS. Atherothrombosis,Thrombus,Blood Clot,Blood Clots,Thromboses

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