Rheological studies of the contractile force within platelet-fibrin clots: Effects of prostaglandin E1, dibutyryl-cAMP and dibutyryl-cGMP

Kuntamukkula, M.S.; McIntire, Larry V.; Moake, JL; Peterson, Dolores M.; Thompson, W. J.

doi:10.1016/0049-3848(78)90225-6

Cited by 12 publications

(5 citation statements)

References 15 publications

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“…Likewise, during the initial stages of tissue repair, cells exert a traction force on the fibrin matrix as they infiltrate the clot to recreate functional tissue at the site of injury. [1][2][3][4] In doing so, they both respond to and modify the mechanical cues presented by the fibrin matrix. Furthermore, the high shear stress engendered by blood flow can provoke thrombus rupture followed by vascular occlusion, depending on the mechanical properties of the constituent fibrin matrix.…”

Section: Introductionmentioning

confidence: 99%

Complex strain induced structural changes observed in fibrin assembled in human plasma

Portale¹,

Torbet

2018

Nanoscale

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The structure of the core scaffold of blood clots, the interlinked 3-dimensional network of fibrin fibers, is modified by mechanical forces generated by platelet driven clot retraction, wound repair and shear stress through blood flow. Here X-ray diffraction is used to investigate how uniaxial strain, ε (ε = extension/original length), alters fiber structure in highly aligned human plasma clots covalently cross-linked by Factor XIIIa. Three stretch sensitive axially repeating structures are identified. Firstly, the foundation structure with an initial ≈22 nm axial repeat stretches, fades then disappears at ε ≈ 0.40. A second, lengthened transitory structure emerges at the low strains (ε ≈ 0.20) believed to be developed by cells. Finally, a third shortened structure appears after relaxation. Simultaneously as strain progresses an increasing fraction of molecules become axially disordered. Weak off-axis diffraction maxima indicate the presence of lateral ordering up to ε = 0.40 that partially recovers after relaxation. The reappearance of both axial and lateral order on relaxation demonstrates a surprising resilience in structure. In view of the range and importance of fibrin's functions, this structural heterogeneity, triggered in vivo by cell traction or shear stress, is likely to be of clinical significance.

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Section: Introductionmentioning

confidence: 99%

Complex strain induced structural changes observed in fibrin assembled in human plasma

Portale¹,

Torbet

2018

Nanoscale

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“…Platelets bind and pull on the fibrin strands as soon as they assemble into a network (Kuntamukkula et al 1978), neutrophils and macrophages (Ciano et al 1986) attach to fibrin as they home to sites of injury to dispose of dead tissues and infectious agents that have breached the epidermal barrier, and fibroblasts first anchor to fibrin as they enter the wound site to rebuild the tissue (Brown et al 1993;Laurens et al 2006). Unlike the extracellular matrices and basement membranes formed by collagen, laminin and proteoglycans, which assemble slowly in an ordered manner dictated by the cells that secrete them, fibrin gels assemble rapidly by a modified polycondensation reaction ( Janmey 1982) from fibrinogen, an abundant constituent of blood plasma, as soon as the protease thrombin is activated in the clotting cascade and begins to remove the part of the fibrinogen polypeptides that prevent its spontaneous polymerization.…”

Section: Introductionmentioning

confidence: 99%

Fibrin gels and their clinical and bioengineering applications

Janmey

Winer

Weisel

2008

J. R. Soc. Interface.

553

461

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Fibrin gels, prepared from fibrinogen and thrombin, the key proteins involved in blood clotting, were among the first biomaterials used to prevent bleeding and promote wound healing. The unique polymerization mechanism of fibrin, which allows control of gelation times and network architecture by variation in reaction conditions, allows formation of a wide array of soft substrates under physiological conditions. Fibrin gels have been extensively studied rheologically in part because their nonlinear elasticity, characterized by soft compliance at small strains and impressive stiffening to resist larger deformations, appears essential for their function as haemostatic plugs and as matrices for cell migration and wound healing. The filaments forming a fibrin network are among the softest in nature, allowing them to deform to large extents and stiffen but not break. The biochemical and mechanical properties of fibrin have recently been exploited in numerous studies that suggest its potential for applications in medicine and bioengineering.

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“…FE simulations are corroborated by physiological calculations. From a physiological standpoint, it is known that fibrin clots retract normally in the presence of platelets [22][23][24][25][26][27]. However, in this study, the forces exerted by MMPs were representative of tensile forces within the elastic regime of fibrin when stretched.…”

Section: Extended Parametric Analysismentioning

confidence: 87%

Electromagnetically Induced Distortion of a Fibrin Matrix With Embedded Microparticles

Scogin

Yesudasan

Walker

et al. 2018

J. Mech. Med. Biol.

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Blood clots occur in the human body when they are required to prevent bleeding. In pathological states such as diabetes and sickle cell disease, blood clots can also form undesirably due to hypercoagulable plasma conditions. With the continued effort in developing fibrin therapies for potential life-saving solutions, more mechanical modeling is needed to understand the properties of fibrin structures with inclusions. In this study, a fibrin matrix embedded with magnetic micro particles (MMPs) was subjected to a magnetic field to determine the magnitude of the required force to create plastic deformation within the fibrin clot. Using finite element (FE) analysis, we estimated the magnetic force from an electromagnet at a sample space located approximately 3 cm away from the coil center. This electromagnetic force coupled with gravity was applied on a fibrin mechanical system with MMPs to calculate the stresses and displacements. Using appropriate coil parameters, it was determined that application of a magnetic field of 730 A/m on the fibrin surface was necessary to achieve an electromagnetic force of 36 nN (to engender plastic deformation).

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Rheological studies of the contractile force within platelet-fibrin clots: Effects of prostaglandin E1, dibutyryl-cAMP and dibutyryl-cGMP

Cited by 12 publications

References 15 publications

Complex strain induced structural changes observed in fibrin assembled in human plasma

Complex strain induced structural changes observed in fibrin assembled in human plasma

Fibrin gels and their clinical and bioengineering applications

Electromagnetically Induced Distortion of a Fibrin Matrix With Embedded Microparticles

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