Abstract
Hemostasis is an orchestrated and tightly regulated process. Damaged endothelium interacts with VWF and platelets to form a platelet plug. Coagulation factors are then activated on the surface of injured endothelium and platelets and create a fibrin mesh. Fibrinolysis is activated to dissolve the platelet plug and return the endothelium to its typical structure.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Kumar V, Abbas AK, Aster JC. Chapter 4: Hemodynamic disorders, thromboembolic disease, and shock in Robbins & Cotran Pathologic Basis of Disease. 10th ed. Philadelphia, PA: Elsevier/Saunders; 2020. p. 115–38.
Barash PG, Cullen BF, Stoelting RK, Cahalan M, Stock M. Clinical anesthesia. Philadelphia, PA: Lippincott Williams & Wilkins; 2009. ISBN-10/ASIN: 0781787637, ISBN-13/EAN: 9780781787635
van der Meijden PEJ, Heemskerk JWM. Platelet biology and functions: new concepts and clinical perspectives. Nat Rev Cardiol. 2019;16(3):166–79. https://doi.org/10.1038/s41569-018-0110-0.
Lenting PJ, Christophe OD, Denis CV. Von Willebrand factor biosynthesis, secretion, and clearance: connecting the far ends. Blood. 2015;125(13):2019–28. https://doi.org/10.1182/blood-2014-06-528406.
Nieswandt B, Watson SP. Platelet-collagen interaction: is GPVI the central receptor? Blood. 2003;102(2):449–61. https://doi.org/10.1182/blood-2002-12-3882.
Broos K, Feys HB, De Meyer SF, Vanhoorelbeke K, Deckmyn H. Platelets at work in primary hemostasis. Blood Rev. 2011;25(4):155–67. https://doi.org/10.1016/j.blre.2011.03.002.
Macfarlane RG. An enzyme cascade in the blood clotting mechanism, and its function as a biochemical amplifier [23]. Nature. 1964;202(4931):498–9. https://doi.org/10.1038/202498a0.
Davie EW, Ratnoff OD. Waterfall sequence for intrinsic blood clotting. Science (80-). 1964;145(3638):1310–2. https://doi.org/10.1126/science.145.3638.1310.
O’Donnell JS, O’Sullivan JM, Preston RJS. Advances in understanding the molecular mechanisms that maintain normal haemostasis. Br J Haematol. 2019;186(1):24–36. https://doi.org/10.1111/bjh.15872.
Maas C, Renne T. Coagulation factor XII in thrombosis and inflammation. Blood. 2018;131(17):1903–9. https://doi.org/10.1182/blood-2017-04-569111.
Chapin JC, Hajjar KA. Fibrinolysis and the control of blood coagulation. Blood Rev. 2015;29(1):17–24. https://doi.org/10.1016/j.blre.2014.09.003.
Weitz JI, Fredenburgh JC, Eikelboom JW. A test in context: D-Dimer. J Am Coll Cardiol. 2017;70(19):2411–20. https://doi.org/10.1016/j.jacc.2017.09.024.
Kruithof EKO, Tran-Hang C, Bachmann F. The fast-acting inhibitor of tissue type plasminogen activator in plasma is also the primary plasma inhibitor of urokinase. Thromb Haemost. 1986;55(1):65–9. https://doi.org/10.1055/s-0038-1661449.
Åstedt B, Lindoff C, Lecander I. Significance of the plasminogen activator inhibitor of placental type (PAI-2) in pregnancy. In: Seminars in thrombosis and hemostasis, vol. 24. Thieme Medical Publishers Inc; 1998. p. 431–5. https://doi.org/10.1055/s-2007-996035.
Aoki N, Moroi M, Matsuda M, Tachiya K. The behavior of α2 plasmin inhibitor in fibrinolytic states. J Clin Invest. 1977;60(2):361–9. https://doi.org/10.1172/JCI108784.
Sakata Y, Aoki N. Significance of cross-linking of α2-plasmin inhibitor to fibrin in inhibition of fibrinolysis and in hemostasis. J Clin Invest. 1982;69(3):536–42. https://doi.org/10.1172/JCI110479.
Foley JH, Kim PY, Mutch NJ, Gils A. Insights into thrombin activatable fibrinolysis inhibitor function and regulation. J Thromb Haemost. 2013;11(Suppl. 1):306–15. https://doi.org/10.1111/jth.12216.
Mast AE. Tissue factor pathway inhibitor: multiple anti-coagulant activities for a single protein. Arterioscler Thromb Vasc Biol. 2016;36(1):9–14. https://doi.org/10.1161/ATVBAHA.115.305996.
Dahlbäck B, Villoutreix BO. Regulation of blood coagulation by the protein C anti-coagulant pathway: Novel insights into structure-function relationships and molecular recognition. Arterioscler Thromb Vasc Biol. 2005;25(7):1311–20. https://doi.org/10.1161/01.ATV.0000168421.13467.82.
Perry DJ. Antithrombin and its inherited deficiencies. Blood Rev. 1994;8(1):37–55. https://doi.org/10.1016/0268-960X(94)90006-X.
Jin L, Abrahams JP, Skinner R, Petitou M, Pike RN, Carrell RW. The anti-coagulant activation of antithrombin by heparin. Proc Natl Acad Sci U S A. 1997;94(26):14683–8. https://doi.org/10.1073/pnas.94.26.14683.
Alshaikhli A, Rokkam VR, Hemophilia B. [Updated 2020 Aug 14]. In: StatPearls [Internet]. Treasure Island (FL): StatPearls Publishing; 2020 Jan-. Available from: https://www.ncbi.nlm.nih.gov/books/NBK560792/.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2022 The Author(s), under exclusive license to Springer Nature Singapore Pte Ltd.
About this chapter
Cite this chapter
Ramanan, S.V., Rajan, J., Rajan, S. (2022). The Coagulation Cascade. In: Prabhakar, H., S Tandon, M., Kapoor, I., Mahajan, C. (eds) Transfusion Practice in Clinical Neurosciences. Springer, Singapore. https://doi.org/10.1007/978-981-19-0954-2_25
Download citation
DOI: https://doi.org/10.1007/978-981-19-0954-2_25
Published:
Publisher Name: Springer, Singapore
Print ISBN: 978-981-19-0953-5
Online ISBN: 978-981-19-0954-2
eBook Packages: MedicineMedicine (R0)