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199406, Санкт-Петербург, ул.Гаванская, д. 49, корп.2

ISSN 1999-6314

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«
Vol. 23, Art. 23 (pp. 357-368)    |    2022       
»

Collagen and hemostasis
Philippova O.I., Kurnikova E.A.

North-Western State Medical University named after I.I. Mechnikov



Brief summary

Collagen is the most common protein of the extracellular matrix and the key structural component of the connective tissue, determining its mechanical strength and stretchability. Different types of collagen predominate in different tissues, and this in turn is determined by the role that collagen plays in a particular organ or tissue. Collagen types I, III, IV, V, VI, XV and XVIII have been found in the vascular wall. Due to their adhesive properties, collagens are also direct participants in hemostasis. They are one of the main activators of platelets in case of damage to the integrity of the vascular wall. These proteins support both platelet adhesion and full activation. The article considers mechanisms of interaction of collagen and hemostasis, the role of collagen in regulation of coagulation system.


Key words

collagen, platelets, Willebrand factor, collagen binding capacity of Willebrand factor, Willebrand disease.





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Reference list

1. Shoulders M.D., Raines R.T. et al. Collagen structure and stability. Annu Rev Biochem. 2009; 78:929-958. doi: 10.1146/annurev.biochem.77.032207.120833.


2. Shehonin B.V., Kondalenko V.F., Domogatskii S.P. i dr. Raspredelenie kollagena I, III, IV, V tipov v stenke arterii cheloveka. Kardiologiya. 1984; 24(4):95-99.


3. Howard P.S., Macarak E.J. Localization of collagen types in regional segments of the fetal bovine aorta. Lab Invest. 1989; 61: 548- 555.


4. Farndale R.W., Sixma J. J., Barnes M. J., De GrootP. G. The role of collagen in thrombosis and hemostasis. Journal of Thrombosis and Haemostasis. 2004; 2: 561-573.


5. Manon-Jensen T., Kjeld N. G., Karsdal M.A. Collagen-mediated hemostasis. Journal of Thrombosis and Haemostasis. 2016; 14: 438-448. doi: 10.1111/jth.13249.


6. Baum J., Brodsky B. Folding of peptide models of collagen and misfolding in disease. Current Opinion in Structural Biology.1999; 9: 122-128.


7. Brondijk T.H., Bihan D. Farndale R.W., Huizinga E.G. Implications for collagen I chain registry from the structure of the collagen von Willebrand factor A3 domain complex. ProcNatlAcadSci USA. 2012; 109(14): 5253-5258. doi: 10.1073/pnas.1112388109.


8. Lisman T., Raynal N., Groeneveld D. et al. A single high-affinity binding site for von Willebrand factor in collagen III, identified using synthetic triple-helical peptides. Blood. 2006; 108:3753-3756.


9. Knight C.G., Morton L.F., Peachey A.R.et al. The collagen-binding A-domains of integrinsalpha(1)beta(1) and alpha(2)beta(1) recognize the same specific amino acid sequence, GFOGER, in native (triple-helical) collagens. J Biol Chem. 2000; 275: 35 -40.


10. Heemskerk J.W., Kuijpers M.J. et al. Platelet collagen receptors and coagulation. A characteristic platelet response as possibl e target for antithrombotic treatment Trends Cardiovasc Med. 2005; 15(3):86-92. doi: 10.1016/j.tcm.2005.03.003.


11. Santoro S.A. Identification of a 160,000 dalton platelet membrane protein that mediates the initial divalent cation-dependent adhesion of platelets to collagen. Cell 1986; 46:913- 920.


12. Sugiyam, T., Okum, M., Ushikubi F. et al. A novel platelet aggregating factor found in a patient with defective collagen-induced platelet aggregation and autoimmune thrombocytopenia. Blood 1987; 69:1712- 1720.


13. Staatz W.D., Fok K.F, Zutter M.M et al. Identification of a tetrapeptide recognition sequence for the alpha2 beta1 integrin in collagen. J Biol Chem. Inc. 1991; 266(12):7363-7367.


14. Morton L.F., Peachey A.R., Knight C.G. et al. The Platelet Reactivity of Synthetic Peptides Based on the Collagen III Fragment alpha1(III)CB4. Evidence for an Integrin alpha2beta1 Recognition Site Involving Residues 522-528 of the alpha1(III) Collagen Chain. J Biol Chem. 1997; 272 (17): 11044-11048.


15. Knight C.G., Morton L.F., Onley D.J.et al. Collagen-platelet interaction: Gly-Pro-Hyp is uniquely specific for platelet GpVI and mediates platelet activation by collagen. Cardiovasc Res. 1999; 41: 450-457.


16. Khoshnoodi J., Pedchenko V., Hudson B.G. Mammalian collagen IV. Microsc Res Tech. 2008; 71: 357-370.


17. Rand J.H., Wu X.X., Potter B.J., Uson R.R., Gordon R.E. Co-localization of von Willebrand factor and type VI collagen in human vascular subendothelium. Am J Pathol. 1993; 142:843-850.


18. vanZanten G.H., Saelman E.U., Schut-Hese K.M. et al. Platelet adhesion to collagen type IV under flow conditions. Blood. 1996; 88: 3862-3871.


19. Wolberg A.S., Stafford D.W., Erie D.A. Human factor IX binds to specific sites on the collagenous domain of collagen IV. J Biol Chem. 1997; 272: 16717-16720.


20. Gui T., Lin H.F., Jin D.Y. et al. Circulating and binding characteristics of wild-type factor IX and certain Gla domain mutants in vivo. Blood.2002; 100(1):153-158. doi: 10.1182/blood.v100.1.153


21. von der Mark H, Aumailley M, Wick G, Fleischmajer R, Timpl R. Immunochemistry, genuine size and tissue localization of collagen VI. Eur J Biochem. 1984; 142: 493-502.


22. Mazzucato M., Spessotto P., Masotti A. et al. Identification of Domains Responsible for von Willebrand Factor Type VI Collagen Interaction Mediating Platelet Adhesion under High Flow The Journal of Biological Chemistry. 1999; 274(5): 3033-3041,doi: 10.1074/jbc.274.5.3033


23. Farndale R.W., Lisman T., Bihan D. et al. Cell-collagen interactions: the use of peptide Toolkits to investigate collagen-receptor interactions Biochem Soc Trans. 2008; 36(Pt 2):241-250. doi: 10.1042/BST0360241.


24. Farndale R.W. Collagen-induced platelet activation. Blood Cells, Molecules, and Diseases. 2006; 36:162-165.


25. Watson S.P., Herbert J.M.J., Pollitt A.Y. GPVI and CLEC-2 in hemostasis and vascular integrity. J Thromb. Haemost. 2010; 8: 1456-1467.


26. Sixma J.J., van Zanten G.H., Huizinga E.G. et al. Platelet adhesion to collagen: an update. Thromb Haemost. 1997; 78: 434-438.


27. Sadler J. E. Biochemistry and genetics of von Willebrand factor Annu Rev Biochem 1998; 67:395-424. doi: 10.1146/annurev.biochem.67.1.395.


28. Chernova E.V. Faktor Villebranda. Vestnik Severo-Zapadnogo gosydarstvennogo medicinskogo yniversiteta im. I.I. Mechnikova. - 2018. - T. 10. - 4. - C. 73-80. doi: 10.17816/mechnikov201810473-80


29. Pannekoek H., Voorberg J. Molecular cloning, expression and assembly of multimeric von Willebrand factor. Baillieres Clin Haematol. 1989; 2:879-96.


30. Flood V.H., Schlauderaff A.C., Haberichter S.L. et al. Crucial role for the VWF A1 domain in binding to type IV collagen. Blood. 2015; 125: 2297-2304.


31. Rand J.H., Patel N.D., Schwartz E.et al. 150-kD von Willebrand factor binding protein extracted from human vascular subendothelium is type VI collagen. J Clin Invest. 1991; 88:253-259.


32. Pareti FI, Niiya K, McPherson JM, Ruggeri ZM. Isolation and characterization of two domains of human von willebrand factor that interact with fibrillar collagen types I and III. J Biol Chem. 1987; 262:13835-13841.


33. Romijn RA, Westein E, Bouma B. et al. Mapping the collagen-binding site in the von Willebrand factor-A3 domain. J Biol Chem 2003; 278: 15035-15039.


34. Bonnefoy A. , Romijn R. A., Vandervoort P. A. H. et al. von Willebrand factor A1 domain can adequately substitute for A3 domain in recruitment of flowing platelets to collagen. J Thromb. Haemost. 2006, 4: 2151-2161.


35. Morales LD, Martin C, Cruz MA. The interaction of von Willebrand factor-A1 domain with collagen: mutation G1324S (type 2M von Willebrand disease) impairs the conformational change in A1 domain induced by collagen. J Thromb Haemost. 2006; 4: 417-425.


36. Siedlecki C.A., Lestini B.J., Kottke-Marchant K.K. et al. Shear-dependent changes in the three-dimensional structure of human von Willebrand factor. Blood 1996; 88: 2939-2950.


37. Du X. Signaling and regulation of the platelet glycoprotein Ib-IX-V complex. Curr Opin Hematol. 2007;14:262-269.


38. Li Z, Delaney M. K., O?Brien K. A., Du X. Signaling during platelet adhesion and activation Arterioscler Thromb Vasc Biol. 2010; 30(12): 2341-2349. doi:10.1161/ATVBAHA. 110.207522.


39. Hynes, R.O. Integrins: bidirectional, allosteric signaling machines. Cell. 2002.110(6): 673-687.


40. Savage B, Almus-Jacobs F., Ruggeri Z.M. Specific synergy of multiple substrate-receptor interactions in platelet thrombus formation under flow. Cell. 1998; 94:657-666.


41. Poole, A., Gibbins, J. M., Turner, M. et al. The Fc receptor gamma-chain and the tyrosine kinase Syk are essential for activation of mouse platelets by collagen. EMBO J., 1997; 16, 2333- 2341.


42. Andrews R.K., Gardiner E.E., Shen Y., Berndt M.C. Platelet interactions in thrombosis. IUBMB Life. 2004;56(1):13-8.doi: 10.1080/15216540310001649831


43. Zhu J., Cole F., Woo-Rasberry V. et al. Type I and type III collagen-platelet interaction: inhibition by type specific receptor peptides. Thromb Res.2007; 119(1):111-119. doi: 10.1016/j.thromres.2005.11.012.


44. Monnet E., Depraetere H., Legrand C. et al. A monoclonal antibody to platelet type III collagen-binding protein (TIIICBP) binds to blood and vascular cells, and inhibits platelet vessel-wall interactions. J Thromb. Haemost. 2001; 86(2):694-701.


45. MauriceP., Legrand C., Fauvel-Lafeve F. Platelet adhesion and signaling induced by the octapeptide primary binding sequence (KOGEOGPK) from type III collagen The FASEB Journal ? Research Communication.2004; 18: 1339-1347.


46. Bendetowicz A.V., Wise R.J., Gilbertvon G.E. Willebrand factor (vWf) is a multimeric adhesive glycoprotein that serves as a carrier for factor VIII in plasma J Biol Chem. 1999; 274 (18): 12300-12307. doi: 10.1074/jbc.274.18.12300.


47. Byers P.H., Murray M.L. Ehlers-Danlos syndrome: a showcase of conditions that lead to understanding matrix biology. Matrix Biol. 2014; 33: 10-15.


48. Onel D., Ulutin S.B., Ulutin O.N. Platelet defect in a case of Ehlers-Danlos syndrome Acta Haematol. 1973; 50(4):238-244. doi: 10.1159/000208355.


49. Borza D.B., Neilson E.G., Hudson B.G. Pathogenesis of Goodpasture syndrome: a molecular perspective. Semin. Nephrol 2003; 23: 522-531.


50. deVries L.S., Koopman C., Groenendaal F.et al. COL4A1 mutation in two preterm siblings with antenatal onset of parenchymal hemorrhage. Ann Neurol. 2009; 65: 12 -18.


51. Koloskov A.V. Bolezn Villebranda. Jyrnal naychnih statei Zdorove i obrazovanie v XXI veke. - 2017. - T. 19. - 11. - S. 43-48.


52. Ribba A.S., Loisel I., Lavergne J.M.et al. Ser968Thr mutation within the A3 domain of von Willebrand factor (VWF) in two related patients leads to a defective binding of VWF to collagen J Thromb. Haemost. 2001; 86:848-854.


53. Riddell A.F., Gomez K., Millar C.M.et al. Characterization of W1745C and S1783A: 2 novel mutations causing defective collagen binding in the A3 domain of von Willebrand factor. Blood. 2009; 114:3489-3496.


54. Flood V.H., Lederman C.A., Wren J.S., et al. Absent collagen binding in a VWF A3 domain mutant: utility of the VWF:CB in diagnosis of VWD. J Thromb. Haemost. 2010; 8:1431-1433.


55. Larsen D.M., Haberichter S.L., Gill J.C. et al. Variability in platelet- and collagen-binding defects in type 2M von Willebrand disease. Haemophilia. 2013; 19:590-594.





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