Fibrin glue

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Fibrin glue
Glued IOL Fig 9.jpg
Fibrin glue applied after drying the scleral bed in an intraocular lens operation
Combination of
Fibrinogen Glycoprotein
Thrombin Coagulation factor
Clinical data
Trade names Artiss, Evicel, Tisseel, others
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administration 		Topical
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KEGG

Fibrin glue (also called fibrin sealant) is a surgical formulation used to create a fibrin clot for hemostasis, cartilage repair surgeries or wound healing. It contains separately packaged human fibrinogen and human thrombin. [15] [16] [17] [18] [19] [20] [21] [22] [23] [24]

Contents

Medical uses

This glue is used as a supportive treatment in surgery (such as liver surgery) for the improvement of hemostasis where standard surgical techniques are insufficient or impractical. [13] [8]

It is also used for repairing dura mater tears and bronchial fistulas and for achieving hemostasis after spleen and liver trauma, [23] in "no sutures" corneal transplantation, pterygium excision with amniotic membrane or conjunctival autograft, and in eye trauma for corneal or conjunctival defects, [25] [26] [27] as well as for skin graft donor site wounds to reduce postoperative pain. [28]

It can also be used to treat pilonidal sinus disease but it is of unclear benefit as of 2017, due to insufficient research. [29]

Contraindications

The glue must not get into blood vessels, as this could lead to clotting in the form of thromboembolism or disseminated intravascular coagulation, or to anaphylaxis (a severe allergic reaction). [30]

Side effects

Possible adverse effects include bleeding disorder and allergic reactions such as flushing, stinging, generalised urticaria, angioedema, bronchospasm, and anaphylaxis. Other adverse effects in studies occurred in roughly equal proportions in treatment and placebo groups. [30]

Interactions

As fibrin glue contains proteins, it may be denatured by ethanol, iodine and heavy metals. These substances are frequently found in antiseptic solutions. [30]

Pharmacology

Mechanism of action

Thrombin is an enzyme that splits fibrinogen into fibrin monomers in 10 to 60 seconds, which aggregate to form a three-dimensional gel-like structure. Thrombin also activates factor XIII from the human body to factor XIIIa, which then cross-links the fibrin monomers to form a stable clot. Both these processes need calcium to work. As the wound heals, the clot is slowly degraded by the enzyme plasmin. [23] [30] [31]

Pharmacokinetics

In rabbit studies, only 1 to 2% of the applied thrombin dose reached the bloodstream. It reached highest blood plasma concentrations after 6 to 8 hours. [30]

Chemistry

Composition

Fibrin glue comes in two vials, respectively containing:

The two components are mixed immediately before application. [13] [32] The formulations also contain calcium salts. [30]

Formulations from different manufacturers may also contain aprotinin, fibronectin, plasminogen, and factor XIII. [33] [34]

Society and culture

A formulation with human thrombin was approved for medical use in the United States in March 2003, and in the European Union in October 2008. [13] [32] [35]

Related Research Articles

<span class="mw-page-title-main">Coagulation</span> Process of formation of blood clots

Coagulation, also known as clotting, is the process by which blood changes from a liquid to a gel, forming a blood clot. It results in hemostasis, the cessation of blood loss from a damaged vessel, followed by repair. The process of coagulation involves activation, adhesion and aggregation of platelets, as well as deposition and maturation of fibrin.

<span class="mw-page-title-main">Disseminated intravascular coagulation</span> Medical condition where blood clots block small blood vessels

Disseminated intravascular coagulation (DIC) is a condition in which blood clots form throughout the body, blocking small blood vessels. Symptoms may include chest pain, shortness of breath, leg pain, problems speaking, or problems moving parts of the body. As clotting factors and platelets are used up, bleeding may occur. This may include blood in the urine, blood in the stool, or bleeding into the skin. Complications may include organ failure.

<span class="mw-page-title-main">Fibrin</span> Fibrous protein involved in blood coagulation

Fibrin is a fibrous, non-globular protein involved in the clotting of blood. It is formed by the action of the protease thrombin on fibrinogen, which causes it to polymerize. The polymerized fibrin, together with platelets, forms a hemostatic plug or clot over a wound site.

<span class="mw-page-title-main">Fibrinogen</span> Soluble protein complex in blood plasma and involved in clot formation

Fibrinogen is a glycoprotein complex, produced in the liver, that circulates in the blood of all vertebrates. During tissue and vascular injury, it is converted enzymatically by thrombin to fibrin and then to a fibrin-based blood clot. Fibrin clots function primarily to occlude blood vessels to stop bleeding. Fibrin also binds and reduces the activity of thrombin. This activity, sometimes referred to as antithrombin I, limits clotting. Fibrin also mediates blood platelet and endothelial cell spreading, tissue fibroblast proliferation, capillary tube formation, and angiogenesis and thereby promotes revascularization and wound healing.

<span class="mw-page-title-main">Thrombin</span> Enzyme involved in blood coagulation in humans

Prothrombin is encoded in the human by the F2 gene. It is proteolytically cleaved during the clotting process by the prothrombinase enzyme complex to form thrombin.

Fibrinolysis is a process that prevents blood clots from growing and becoming problematic. Primary fibrinolysis is a normal body process, while secondary fibrinolysis is the breakdown of clots due to a medicine, a medical disorder, or some other cause.

<span class="mw-page-title-main">Thrombin time</span>

The thrombin time (TT), also known as the thrombin clotting time (TCT), is a blood test that measures the time it takes for a clot to form in the plasma of a blood sample containing anticoagulant, after an excess of thrombin has been added. It is used to diagnose blood coagulation disorders and to assess the effectiveness of fibrinolytic therapy. This test is repeated with pooled plasma from normal patients. The difference in time between the test and the 'normal' indicates an abnormality in the conversion of fibrinogen to fibrin, an insoluble protein.

<span class="mw-page-title-main">Batroxobin</span>

Batroxobin, also known as reptilase, is a snake venom enzyme with Venombin A activity produced by Bothrops atrox and Bothrops moojeni, venomous species of pit viper found east of the Andes in South America. It is a hemotoxin which acts as a serine protease similarly to thrombin, and has been the subject of many medical studies as a replacement of thrombin. Different enzymes, isolated from different species of Bothrops, have been called batroxobin, but unless stated otherwise, this article covers the batroxobin produced by B. moojeni, as this is the most studied variety.

Tachosil is an equine collagen sponge coated with the human plasma-derived coagulation factors fibrinogen and thrombin. It is used during surgery to stop local bleeding on internal organs (hemostasis). Tachosil reacts upon contact with blood, other body fluids or saline to form a clot that glues it to the tissue surface.

The dysfibrinogenemias consist of three types of fibrinogen disorders in which a critical blood clotting factor, fibrinogen, circulates at normal levels but is dysfunctional. Congenital dysfibrinogenemia is an inherited disorder in which one of the parental genes produces an abnormal fibrinogen. This fibrinogen interferes with normal blood clotting and/or lysis of blood clots. The condition therefore may cause pathological bleeding and/or thrombosis. Acquired dysfibrinogenemia is a non-hereditary disorder in which fibrinogen is dysfunctional due to the presence of liver disease, autoimmune disease, a plasma cell dyscrasias, or certain cancers. It is associated primarily with pathological bleeding. Hereditary fibrinogen Aα-Chain amyloidosis is a sub-category of congenital dysfibrinogenemia in which the dysfunctional fibrinogen does not cause bleeding or thrombosis but rather gradually accumulates in, and disrupts the function of, the kidney.

<span class="mw-page-title-main">Fibrinogen alpha chain</span> Protein-coding gene in the species Homo sapiens

Fibrinogen alpha chain is a protein that in humans is encoded by the FGA gene.

<span class="mw-page-title-main">Fibrinogen beta chain</span> Protein-coding gene in the species Homo sapiens

Fibrinogen beta chain, also known as FGB, is a gene found in humans and most other vertebrates with a similar system of blood coagulation.

The fibrinolysis system is responsible for removing blood clots. Hyperfibrinolysis describes a situation with markedly enhanced fibrinolytic activity, resulting in increased, sometimes catastrophic bleeding. Hyperfibrinolysis can be caused by acquired or congenital reasons. Among the congenital conditions for hyperfibrinolysis, deficiency of alpha-2-antiplasmin or plasminogen activator inhibitor type 1 (PAI-1) are very rare. The affected individuals show a hemophilia-like bleeding phenotype. Acquired hyperfibrinolysis is found in liver disease, in patients with severe trauma, during major surgical procedures, and other conditions. A special situation with temporarily enhanced fibrinolysis is thrombolytic therapy with drugs which activate plasminogen, e.g. for use in acute ischemic events or in patients with stroke. In patients with severe trauma, hyperfibrinolysis is associated with poor outcome. Moreover, hyperfibrinolysis may be associated with blood brain barrier impairment, a plasmin-dependent effect due to an increased generation of bradykinin.

A fibrin scaffold is a network of protein that holds together and supports a variety of living tissues. It is produced naturally by the body after injury, but also can be engineered as a tissue substitute to speed healing. The scaffold consists of naturally occurring biomaterials composed of a cross-linked fibrin network and has a broad use in biomedical applications.

<span class="mw-page-title-main">Edoxaban</span> Anticoagulant medication

Edoxaban, sold under the brand name Lixiana among others, is an anticoagulant medication and a direct factor Xa inhibitor. It is taken by mouth.

Platelet-Poor Plasma (PPP) is blood plasma with very low number of platelets (< 10 X 103/μL). Traditionally, PPP was recommended for use in platelet aggregation studies to both adjust the platelet-rich plasma concentration, and to serve as a control. PPP may have elevated levels of fibrinogen, which has the ability to form a fibrin-rich clot once activated. Wound healing requires cell migration and attachment, which is facilitated by this fibrin clot.

Blood clotting tests are the tests used for diagnostics of the hemostasis system. Coagulometer is the medical laboratory analyzer used for testing of the hemostasis system. Modern coagulometers realize different methods of activation and observation of development of blood clots in blood or in blood plasma.

Venombin A is an enzyme. This enzyme catalyses the following chemical reaction

Congenital hypofibrinogenemia is a rare disorder in which one of the three genes responsible for producing fibrinogen, a critical blood clotting factor, is unable to make a functional fibrinogen glycoprotein because of an inherited mutation. In consequence, liver cells, the normal site of fibrinogen production, make small amounts of this critical coagulation protein, blood levels of fibrinogen are low, and individuals with the disorder may develop a coagulopathy, i.e. a diathesis or propensity to experience episodes of abnormal bleeding. However, individuals with congenital hypofibrinogenemia may also have episodes of abnormal blood clot formation, i.e. thrombosis. This seemingly paradoxical propensity to develop thrombosis in a disorder causing a decrease in a critical protein for blood clotting may be due to the function of fibrin to promote the lysis or disintegration of blood clots. Lower levels of fibrin may reduce the lysis of early fibrin strand depositions and thereby allow these depositions to develop into clots.

<span class="mw-page-title-main">Fibrinopeptide</span> Chemical compound

The fibrinopeptides, fibrinopeptide A (FpA) and fibrinopeptide B (FpB), are peptides which are located in the central region of the fibrous glycoprotein fibrinogen and are cleaved by the enzyme thrombin to convert fibrinogen into covalently-linked fibrin monomers. The N-terminal FpA is cleaved from the Aα chains of fibrinogen and FpB from the Bβ chains of fibrinogen, with FpA released before FpB. Subsequent to their formation, fibrin monomers are converted to cross-linked fibrin polymers by the action of thrombin-activated factor XIII, and these fibrin polymers form the backbone of a thrombus. Hence, the fibrinopeptides are sensitive markers of fibrinogenesis, thrombin activity, and coagulation.

References

  1. 1 2 "VeraSeal". Therapeutic Goods Administration (TGA). 12 November 2021. Retrieved 28 December 2021.
  2. ↑ "Updates to the Prescribing Medicines in Pregnancy database". Therapeutic Goods Administration (TGA). 12 May 2022. Retrieved 13 May 2022.
  3. ↑ "AusPAR: Human Fibrinogen / Human Thrombin". Therapeutic Goods Administration (TGA). 29 June 2022. Retrieved 17 July 2022.
  4. ↑ "Health product highlights 2021: Annexes of products approved in 2021". Health Canada . 3 August 2022. Retrieved 25 March 2024.
  5. ↑ "TachoSil sealant matrix - Summary of Product Characteristics (SmPC)". (emc). 31 January 2020. Archived from the original on 10 July 2020. Retrieved 10 July 2020.
  6. ↑ "Tisseel Ready to use Solutions for Sealant - Summary of Product Characteristics (SmPC)". (emc). 30 December 2019. Retrieved 10 July 2020.
  7. ↑ "Artiss Solutions for Sealant - Summary of Product Characteristics (SmPC)". (emc). 29 January 2019. Retrieved 10 July 2020.
  8. 1 2 "Evicel Fibrin Sealant (Human)". U.S. Food and Drug Administration (FDA). 22 July 2017.
  9. ↑ "Vistaseal". U.S. Food and Drug Administration (FDA). 1 October 2024. Retrieved 2 October 2024.
  10. ↑ "Artiss Fibrin Sealant- fibrinogen human, human thrombin solution". DailyMed. 9 June 2022. Retrieved 2 October 2024.
  11. ↑ "Tisseel Fibrin Sealant- fibrinogen human, human thrombin kit; Tisseel Fibrin Sealant- fibrinogen human, human thrombin solution". DailyMed. 26 December 2019. Retrieved 2 October 2024.
  12. ↑ "TachoSil". U.S. Food and Drug Administration. 1 October 2024. Retrieved 2 October 2024.
  13. 1 2 3 4 "Evicel EPAR". European Medicines Agency. 17 September 2018. Retrieved 12 June 2020.PD-icon.svg This article incorporates text from this source, which is in the public domain .
  14. ↑ "Veraseal EPAR". European Medicines Agency (EMA). 10 November 2017. Retrieved 13 September 2024.
  15. ↑ Irwin RM, Bonassar LJ, Cohen I, Matuska AM, Commins J, Cole B, et al. (8 November 2019). "The clot thickens: Autologous and allogeneic fibrin sealants are mechanically equivalent in an ex vivo model of cartilage repair". PLOS ONE. 14 (11): e0224756. Bibcode:2019PLoSO..1424756I. doi: 10.1371/journal.pone.0224756 . PMC   6839864 . PMID   31703078.
  16. ↑ Shah NV, Meislin R (December 2013). "Current state and use of biological adhesives in orthopedic surgery". Orthopedics. 36 (12): 945–956. doi:10.3928/01477447-20131120-09. PMID   24579215.
  17. ↑ Smith BL, Matuska AM, Greenwood VL, Gilat R, Wijdicks CA, Cole BJ (15 April 2022). "Autologous Fibrin Sealants Have Comparable Graft Fixation to an Allogeneic Sealant in a Biomechanical Cadaveric Model of Chondral Defect Repair". Arthroscopy, Sports Medicine, and Rehabilitation. 4 (3): e1075–e1082. doi:10.1016/j.asmr.2022.03.003. ISSN   2666-061X. PMC   9210474 . PMID   35747626. S2CID   248208731.
  18. 1 2 Atrah HI (April 1994). "Fibrin glue". BMJ. 308 (6934): 933–934. doi:10.1136/bmj.308.6934.933. PMC   2539755 . PMID   8173397.
  19. ↑ Thompson DF, Letassy NA, Thompson GD (December 1988). "Fibrin glue: a review of its preparation, efficacy, and adverse effects as a topical hemostat". Drug Intelligence & Clinical Pharmacy. 22 (12): 946–952. doi: 10.1177/106002808802201203 . PMID   2468466. S2CID   37017252.
  20. ↑ "Fibrin Glue for Anal Fistula - Digestive Disorders / Gastroenterology". MedHelp.
  21. ↑ Shinohara K, Kobayashi E, Yoshida T, Toyama N, Kiyozaki H, Fujimura A, et al. (1998). "Effect of fibrin glue on small and large bowel anastomoses in the rat". European Surgical Research. 30 (1): 8–12. doi:10.1159/000008552. PMID   9493689. S2CID   46792418.
  22. ↑ Spotnitz WD, Mintz PD, Avery N, Bithell TC, Kaul S, Nolan SP (August 1987). "Fibrin glue from stored human plasma. An inexpensive and efficient method for local blood bank preparation". The American Surgeon. 53 (8): 460–462. PMID   2440358.
  23. 1 2 3 Saxena S, Jain P, Shukla J (2003). "Preparation of two component Fibrin Glue and its clinical evaluation in skin grafts and flaps". Indian J Plast Surg. 36 (1): 14–17. doi: 10.1055/s-0043-1778572 .
  24. ↑ Mücke T, Wolff KD (2009). "Performing microvascular anastomosis with fibrin glue--faster, easier, and more reliable?". Microsurgery. 29 (1): 80–81. doi:10.1002/micr.20556. PMID   18946885. S2CID   31854904.
  25. ↑ Narendran N, Mohamed S, Shah S (July 2007). "No sutures corneal grafting--a novel use of overlay sutures and fibrin glue in Deep Anterior Lamellar Keratoplasty". Contact Lens & Anterior Eye. 30 (3): 207–209. doi:10.1016/j.clae.2007.02.007. PMID   17379570.
  26. ↑ Dal Pizzol MM, Roggia MF, Kwitko S, Marinho DR, Rymer S (2009). "[Use of fibrin glue in ocular surgery]" [Use of fibrin glue in ocular surgery]. Arquivos Brasileiros de Oftalmologia (in Portuguese). 72 (3): 308–312. doi: 10.1590/s0004-27492009000300006 . hdl: 10183/37501 . PMID   19668958.
  27. ↑ "Fibrin Sealant Fibrin Gluing Haemostasis autologous". vivostat.com.
  28. ↑ Sinha S, Schreiner AJ, Biernaskie J, Nickerson D, Gabriel VA (November 2017). "Treating pain on skin graft donor sites: Review and clinical recommendations". The Journal of Trauma and Acute Care Surgery. 83 (5): 954–964. doi:10.1097/TA.0000000000001615. PMID   28598907. S2CID   44520644.
  29. ↑ Lund J, Tou S, Doleman B, Williams JP (January 2017). "Fibrin glue for pilonidal sinus disease". The Cochrane Database of Systematic Reviews. 1 (1): CD011923. doi:10.1002/14651858.CD011923.pub2. PMC   6464784 . PMID   28085995.
  30. 1 2 3 4 5 6 "Evicel: EPAR – Product Information" (PDF). European Medicines Agency. 12 June 2020.
  31. ↑ Spotnitz WD (April 2010). "Fibrin sealant: past, present, and future: a brief review". World Journal of Surgery. 34 (4): 632–634. doi:10.1007/s00268-009-0252-7. PMID   19820991. S2CID   20760524.
  32. 1 2 "Evicel Fibrin Sealant (Human)- fibrinogen human and thrombin human kit". DailyMed. 17 December 2019. Retrieved 12 June 2020.
  33. ↑ "Tisseel". Swedish official drug catalog.
  34. ↑ KEGG drug: Factor XIII with fibrinogen. Accessed 9 July 2020.
  35. ↑ "Evicel". U.S. Food and Drug Administration (FDA). 5 June 2017. Archived from the original on 22 July 2017. Retrieved 12 June 2020.
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