Clinician reported ease of use for a novel fibrin sealant patch for hemostasis: results from four randomized controlled trials

Corral, Mitra; Ferko, Nicole; Hollmann, S.; Hogan, Andrew J.; Jamous, N.; Batiller, Jonathan; Shen, Jim

doi:10.1185/03007995.2015.1128405

Cited by 8 publications

(7 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…First, THA, no matter of the product used, is highly appreciated by liver surgeons – as recently highlighted in a Dutch survey – in order to reduce intraoperative blood loss, TTH and potential bile leakage . A fibrin sealant patch is often preferred since it seems the friendliest tool to use . Second, the best results – all outcomes confounded – seem to be obtained with the carrier‐bound fibrin sealant, homemade or ready‐to‐use, that combines the effects of a matrix with active agents to trigger and accelerate coagulation.…”

Section: Discussionmentioning

confidence: 99%

An update on topical haemostatic agents in liver surgery: systematic review and meta analysis

Brustia

Granger

Scatton

2016

J Hepatobiliary Pancreat Sci

View full text Add to dashboard Cite

Mortality and morbidity in hepatic surgery are affected by blood loss and transfusion. Topical haemostatic agents (THA) are composed by a matrix and/or fibrin sealants, and their association known as "carrier-bound fibrin sealant" (CBFS): despite widely used for secondary haemostasis, the level of evidence remains low. To realize a meta-analysis on the results of CBFS on haemostasis and postoperative complications. Searches in PubMed, PubMed Central, Cochrane and Google Scholar using keywords: "topical_haemostasis" OR "haemostatic_agents" OR "sealant_patch" OR "fibrin_sealant" OR "collagen_sealant" AND "liver_surgery" OR "hepatic_surgery" OR "liver_transplantation". Randomized clinical trials, large retrospective cohort studies, case control studies evaluating THA on open/laparoscopic liver surgery and transplantation. From 1993 to 2016 were found 22 studies for qualitative synthesis and 13 for quantitative meta-analysis. The time to haemostasis was lower in the CBFS group (mean difference À2.33 min; P = 0.00001). The risk of receiving blood transfusion, developing collections and bile leak was not influenced by the use of CBFS (OR 0.75; P = 0.25), (OR 0.72; P = 0.52), (OR 0.74; P = 0.30) respectively. The use of CBFS in liver surgery significantly reduce the time to haemostasis, but does not decrease transfusion, postoperative collection and bile leak.

show abstract

Section: Discussionmentioning

confidence: 99%

An update on topical haemostatic agents in liver surgery: systematic review and meta analysis

Brustia

Granger

Scatton

2016

J Hepatobiliary Pancreat Sci

View full text Add to dashboard Cite

show abstract

“…Fibrin sealants formed by mixing fibrinogen and thrombin are widely used to stop bleeding (Corral et al 2016). Importantly, various commercially available fibrin sealants have diverse mechanical properties (Hickerson et al 2011) and glues with distinct structure and stiffness had different hemostatic efficacy (Fortelny et al 2011).…”

Section: 5 Fibrin Mechanical Properties and Their Structural Originsmentioning

confidence: 99%

Fibrin Formation, Structure and Properties

Weisel

Litvinov

2017

Subcellular Biochemistry

527

498

View full text Add to dashboard Cite

Fibrinogen and fibrin are essential for hemostasis and are major factors in thrombosis, wound healing, and several other biological functions and pathological conditions. The X-ray crystallographic structure of major parts of fibrin(ogen), together with computational reconstructions of missing portions and numerous biochemical and biophysical studies, have provided a wealth of data to interpret molecular mechanisms of fibrin formation, its organization, and properties. On cleavage of fibrinopeptides by thrombin, fibrinogen is converted to fibrin monomers, which interact via knobs exposed by fibrinopeptide removal in the central region, with holes always exposed at the ends of the molecules. The resulting half-staggered, double-stranded oligomers lengthen into protofibrils, which aggregate laterally to make fibers, which then branch to yield a three-dimensional network. Much is now known about the structural origins of clot mechanical properties, including changes in fiber orientation, stretching and buckling, and forced unfolding of molecular domains. Studies of congenital fibrinogen variants and post-translational modifications have increased our understanding of the structure and functions of fibrin(ogen). The fibrinolytic system, with the zymogen plasminogen binding to fibrin together with tissue-type plasminogen activator to promote activation to the active proteolytic enzyme, plasmin, results in digestion of fibrin at specific lysine residues. In spite of a great increase in our knowledge of all these interconnected processes, much about the molecular mechanisms of the biological functions of fibrin(ogen) remains unknown, including some basic aspects of clotting, fibrinolysis, and molecular origins of fibrin mechanical properties. Even less is known concerning more complex (patho)physiological implications of fibrinogen and fibrin.

show abstract

“…A viscoelastic fibrin clot is necessary to prevent blood loss and promote wound healing. In surgery, fibrin sealants are formed from concentrated (up to 60 mg/mL) Fg followed by application to a bleeding wound to achieve hemostasis . Fg might polymerize without proteolytic action, but the (patho)physiological implications of this phenomenon are unclear.…”

Section: Introductionmentioning

confidence: 99%

“…In surgery, fibrin sealants are formed from concentrated (up to 60 mg/mL) Fg followed by application to a bleeding wound to achieve hemostasis. 2 Fg might polymerize without proteolytic action, 3 but the (patho)physiological implications of this phenomenon are unclear. Due to various functions in blood clotting, Fg molecules are also involved in many intermolecular interactions and, therefore, the physical molecular characteristics of Fg are of paramount importance for biology and medicine.…”

Section: ■ Introductionmentioning

confidence: 99%

Conformational Flexibility and Self-Association of Fibrinogen in Concentrated Solutions

et al. 2017

View full text Add to dashboard Cite

We studied the hydrodynamic behavior of fibrinogen, a blood plasma protein involved in blood clotting, in a broad 0.3-60 mg/mL range of concentration and 5-42 °C temperature using pulsed-field gradient H NMR-diffusometry. Arrhenius plots revealed the activation energy for fibrinogen diffusion E = 21.3 kJ/mol at 1.4 mg/mL and 28.4 kJ/mol at 38 mg/mL. We found a dramatic slowdown in fibrinogen self-diffusion with concentration beginning at 1.7-3.4 mg/mL, which deviated from the standard hard-particle behavior, suggesting a remarkable intermolecular entanglement. This concentration dependence was observed regardless of the absence or presence of the GPRP peptide (inhibitor of fibrin polymerization), and also in samples free of fibrin oligomers. By contrast, diffusivity of fibrinogen variant I-9 with truncated C-terminal portions of the Aα chains was much less concentration-dependent, indicating the importance of intermolecular linkages formed by the αC regions. Theoretical models combined with all-atom molecular dynamics simulations revealed partially bent fibrinogen solution conformations that interpolate between a flexible chain and a rigid rod observed in the crystal. The results obtained illuminate the important role of the αC regions in modulating the fibrinogen molecular shape through formation of weak intermolecular linkages that control the bulk properties of fibrinogen solutions.

show abstract

Clinician reported ease of use for a novel fibrin sealant patch for hemostasis: results from four randomized controlled trials

Cited by 8 publications

References 35 publications

An update on topical haemostatic agents in liver surgery: systematic review and meta analysis

An update on topical haemostatic agents in liver surgery: systematic review and meta analysis

Fibrin Formation, Structure and Properties

Conformational Flexibility and Self-Association of Fibrinogen in Concentrated Solutions

Contact Info

Product

Resources

About