The permeability of fibrin network developed in human plasma

Gelder, James M. van; Nair, C H; Dhall, D.P.

doi:10.1097/00001721-199506000-00001

Cited by 5 publications

(6 citation statements)

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“…Higher j values for the translucent than for the opaque gels are in agreement with the positive correlation reported between fibrin turbidity and gel porosity/permeability [28]. In turn, this porosity/permeability was suggested to predominantly depend on the arrangement of the fibers [29]. Moreover, FXIII content, larger for the translucent than for the opaque gels, could also contribute to the different permeability values estimated in both gels.…”

Section: Discussionsupporting

confidence: 85%

Influencing biophysical properties of fibrin with buffer solutions

et al. 2010

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Fibrin has been proposed as cell scaffold for numerous tissue engineering applications. While most of the studies have focused on fibrinogen and thrombin, other components of fibrin can also affect its properties. The present study aimed to evaluate the effects of buffer solution composition on fibrin biophysical properties. Fibrin scaffolds were synthesized with different calcium, chloride, and factor XIII (FXIII) final concentrations. Light transmission was determined as a relative, semi-quantitative estimator of fiber structure differences, and two compositions, resulting in translucent and opaque gels, were tested for mechanical and biological properties. Gels were seeded with mouse mesenchymal cells, C3H10T1/2, or bovine bone marrow-derived mesenchymal stromal cells and cultured up to 10 or 24 days, before cell number, morphology and distribution were evaluated. Calcium increased gel opacity (i.e., fiber thickness), while chloride and FXIII decreased it. Opaque gels displayed a fluid-like viscous behavior while translucent gels showed improved elastic properties. Both compositions supported survival of both cell types with opaque gels leading to better proliferation, but significant scaffold shrinkage after 17 days of culture. These results demonstrated that calcium, chloride, and FXIII modulate the biophysical properties of fibrin, and can be used to adjust mechanical and biological properties for tissue engineering applications.

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Section: Discussionsupporting

confidence: 85%

Influencing biophysical properties of fibrin with buffer solutions

et al. 2010

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“…Thrombogenic activity near the wound can also trigger an inflammatory response of endothelium [21] leading to the sequestration and aggregation of neutrophils, which, when activated by local mediators such as platelet-activating factor, platelet-derived growth factor, and XO, can undergo adhesion, degranulation, and subsequent respiratory burst that are deleterious to the vessel endothelium. Since P-188 is known to enhance fibrin network permeability [10,22] and is an inhibitor of neutrophil chemotaxis in vitro [11], it can keep capillaries patent and maintain blood flow within them. More recently, P-188 has been shown to bind to blood platelets [23].…”

Section: Discussionmentioning

confidence: 99%

“…Poloxamer-188 (P-188) is a nonionic block copolymer surfactant of polyoxyethylene and polyoxypropylene commonly found in artificial blood substitutes as an additive. P-188 increases whole blood clot permeability and fibrinolysis in vitro [10]. In addition to these potentially beneficial hemorheological effects, P-188 also inhibits leukocyte chemotaxis, adhesion, and migration [11][12][13].…”

Section: Introductionmentioning

confidence: 99%

Poloxamer-188 Improves Capillary Blood Flow and Tissue Viability in a Cutaneous Burn Wound

Baskaran¹,

Toner²,

Yarmush³

et al. 2001

Journal of Surgical Research

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“…In contrast, even though the fibrin Caracas II clots are also made up of thin fibers, the large pores that are present lead to higher than normal permeation rates. This observation highlights the importance of determining the ultrastructure of clot networks, in addition to permeation values, in order to adequately explain clot porosity (36,44).…”

Section: Localization Of ␣C Domains On Fibrinogen Caracas II Mole-mentioning

confidence: 82%

The Ultrastructure of Fibrinogen Caracas II Molecules, Fibers, and Clots

Woodhead

Nagaswami

Matsuda

et al. 1996

Journal of Biological Chemistry

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Fibrinogen Caracas II is an abnormal fibrinogen involving the mutation of A alpha serine 434 to N-glycosylated asparagine. Some effects of this mutation on the ultrastructure of fibrinogen Caracas II molecules, fibers, and clots were investigated by electron microscopy. Electron microscopy of rotary shadowed individual molecules indicated that most of the alphaC domains of fibrinogen Caracas II do not interact with each other or with the central domain, in contrast to control fibrinogen. Negatively contrasted Caracas II fibers were thinner and less ordered than control fibers, and many free fiber ends were observed. Scanning electron microscopy of whole clots revealed the presence of large pores bounded by local fiber networks made up of thin fibers. Permeation experiments also indicated that the average pore diameter was larger than that of control clots. The viscoelastic properties of the Caracas II clot, as measured by a torsion pendulum, were similar to those of control clots. Both the normal stiffness and increased permeability of the Caracas II clots are consistent with the observation that subjects with this dysfibrinogenemia are asymptomatic.

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The permeability of fibrin network developed in human plasma

Cited by 5 publications

References 0 publications

Influencing biophysical properties of fibrin with buffer solutions

Influencing biophysical properties of fibrin with buffer solutions

Poloxamer-188 Improves Capillary Blood Flow and Tissue Viability in a Cutaneous Burn Wound

The Ultrastructure of Fibrinogen Caracas II Molecules, Fibers, and Clots

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