Polyphosphate Activates von Willebrand Factor Interaction with Glycoprotein Ib in the Absence of Factor VIII In Vitro
Polyphosphate (polyP), a phosphate polymer released by activated platelets, may modulate various stages of hemostasis by binding to blood proteins. In this context, we previously reported that polyP binds to the von Willebrand factor (VWF). One of the most significant functions of VWF is to bind to...
- Autores:
-
Montilla Rodríguez, Liliana Marcela
Atienza- Navarro, Isabel
García- Cozar, Francisco Jose
Castro, Carmen
Rodriguez- Martorell, Francisco Javier
Ruiz, Felix A
- Tipo de recurso:
- Article of investigation
- Fecha de publicación:
- 2022
- Institución:
- Universidad Cooperativa de Colombia
- Repositorio:
- Repositorio UCC
- Idioma:
- OAI Identifier:
- oai:repository.ucc.edu.co:20.500.12494/52561
- Palabra clave:
- Factor VIII
Hemophilia A
Polyphosphate
Von Willebrand disease
Von Willebrand factor
- Rights
- openAccess
- License
- Atribución
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| dc.title.none.fl_str_mv |
Polyphosphate Activates von Willebrand Factor Interaction with Glycoprotein Ib in the Absence of Factor VIII In Vitro |
| title |
Polyphosphate Activates von Willebrand Factor Interaction with Glycoprotein Ib in the Absence of Factor VIII In Vitro |
| spellingShingle |
Polyphosphate Activates von Willebrand Factor Interaction with Glycoprotein Ib in the Absence of Factor VIII In Vitro Factor VIII Hemophilia A Polyphosphate Von Willebrand disease Von Willebrand factor |
| title_short |
Polyphosphate Activates von Willebrand Factor Interaction with Glycoprotein Ib in the Absence of Factor VIII In Vitro |
| title_full |
Polyphosphate Activates von Willebrand Factor Interaction with Glycoprotein Ib in the Absence of Factor VIII In Vitro |
| title_fullStr |
Polyphosphate Activates von Willebrand Factor Interaction with Glycoprotein Ib in the Absence of Factor VIII In Vitro |
| title_full_unstemmed |
Polyphosphate Activates von Willebrand Factor Interaction with Glycoprotein Ib in the Absence of Factor VIII In Vitro |
| title_sort |
Polyphosphate Activates von Willebrand Factor Interaction with Glycoprotein Ib in the Absence of Factor VIII In Vitro |
| dc.creator.fl_str_mv |
Montilla Rodríguez, Liliana Marcela Atienza- Navarro, Isabel García- Cozar, Francisco Jose Castro, Carmen Rodriguez- Martorell, Francisco Javier Ruiz, Felix A |
| dc.contributor.author.none.fl_str_mv |
Montilla Rodríguez, Liliana Marcela Atienza- Navarro, Isabel García- Cozar, Francisco Jose Castro, Carmen Rodriguez- Martorell, Francisco Javier Ruiz, Felix A |
| dc.subject.none.fl_str_mv |
Factor VIII Hemophilia A Polyphosphate Von Willebrand disease Von Willebrand factor |
| topic |
Factor VIII Hemophilia A Polyphosphate Von Willebrand disease Von Willebrand factor |
| description |
Polyphosphate (polyP), a phosphate polymer released by activated platelets, may modulate various stages of hemostasis by binding to blood proteins. In this context, we previously reported that polyP binds to the von Willebrand factor (VWF). One of the most significant functions of VWF is to bind to and protect the blood circulating Factor VIII (FVIII). Therefore, here, we study the role of polyP in the VWF-FVIII complex in vitro and suggest its biological significance. Surface plasmon resonance and electrophoretic mobility assays indicated that polyP binds dynamically to VWF only in the absence of FVIII. Using the VWF Ristocetin Cofactor assay, the most accepted method for studying VWF in platelet adhesion, we found that polyP activates this role of VWF only at low levels of FVIII, such as in plasmas with chemically depleted FVIII and plasmas from severe hemophilia A patients. Moreover, we demonstrated that FVIII competes with polyP in the activation of VWF. Finally, polyP also increases the binding of VWF to platelets in samples from patients with type 2 and type 3 von Willebrand disease. We propose that polyP may be used in designing new therapies to activate VWF when FVIII cannot be used. |
| publishDate |
2022 |
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2022-11 |
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2023-08-28T21:24:54Z |
| dc.date.available.none.fl_str_mv |
2023-08-28T21:24:54Z |
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Artículos Científicos |
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info:eu-repo/semantics/article |
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http://purl.org/redcol/resource_type/ART |
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2572-1100 |
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https://doi.org/10.3390/ijms232214118 https://hdl.handle.net/20.500.12494/52561 |
| dc.identifier.bibliographicCitation.none.fl_str_mv |
Montilla M, Atienza-Navarro I, García-Cozar FJ, Castro C, Rodríguez-Martorell FJ, Ruiz FA. Polyphosphate Activates von Willebrand Factor Interaction with Glycoprotein Ib in the Absence of Factor VIII In Vitro. Int J Mol Sci. 2022 Nov 15;23(22):14118. doi: 10.3390/ijms232214118. PMID: 36430595; PMCID: PMC9692336. |
| identifier_str_mv |
2572-1100 Montilla M, Atienza-Navarro I, García-Cozar FJ, Castro C, Rodríguez-Martorell FJ, Ruiz FA. Polyphosphate Activates von Willebrand Factor Interaction with Glycoprotein Ib in the Absence of Factor VIII In Vitro. Int J Mol Sci. 2022 Nov 15;23(22):14118. doi: 10.3390/ijms232214118. PMID: 36430595; PMCID: PMC9692336. |
| url |
https://doi.org/10.3390/ijms232214118 https://hdl.handle.net/20.500.12494/52561 |
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Int J Mol Sci |
| dc.relation.references.none.fl_str_mv |
Ruiz, F.A.; Lea, C.R.; Oldfield, E.; Docampo, R. Human Platelet Dense Granules Contain Polyphosphate and Are Similar to Acidocalcisomes of Bacteria and Unicellular Eukaryotes. J. Biol. Chem. 2004, 279, 44250–44257. Moreno-Sanchez, D.; Hernandez-Ruiz, L.; Ruiz, F.A.; Docampo, R. Polyphosphate Is a Novel Pro-inflammatory Regulator of Mast Cells and Is Located in Acidocalcisomes. J. Biol. Chem. 2012, 287, 28435–28444 Morrissey, J.H.; Smith, S.A. Polyphosphate as modulator of hemostasis, thrombosis, and inflammation. J. Thromb. Haemost. 2015, 13 (Suppl. 1), S92–S97. Smith, S.A.; Mutch, N.J.; Baskar, D.; Rohloff, P.; Docampo, R.; Morrissey, J.H. Polyphosphate modulates blood coagulation and fibrinolysis. Proc. Natl. Acad. Sci. USA 2006, 103, 903–908. Choi, S.H.; Smith, S.A.; Morrissey, J.H. Polyphosphate is a cofactor for the activation of factor XI by thrombin. Blood 2011, 118, 6963–6970. Choi, S.H.; Smith, S.A.; Morrissey, J.H. Polyphosphate accelerates factor V activation by factor XIa. Thromb. Haemost. 2015, 113, 599–604. Mutch, N.J.; Myles, T.; Leung, L.L.K.; Morrissey, J.H. Polyphosphate binds with high affinity to exosite II of thrombin. J. Thromb. Haemost. 2010, 8, 548–555 Puy, C.; Tucker, E.I.; Ivanov, I.S.; Gailani, D.; Smith, S.A.; Morrissey, J.H.; Gruber, A.; McCarty, O.J.T. Platelet-Derived Short-Chain Polyphosphates Enhance the Inactivation of Tissue Factor Pathway Inhibitor by Activated Coagulation Factor XI. PLoS ONE 2016, 11, e0165172. Mutch, N.J.; Engel, R.; de Willige, S.U.; Philippou, H.; Ariëns, R.A.S. Polyphosphate modifies the fibrin network and down-regulates fibrinolysis by attenuating binding of tPA and plasminogen to fibrin. Blood 2010, 115, 3980–3988. Verhoef, J.J.F.; Barendrecht, A.D.; Nickel, K.F.; Dijkxhoorn, K.; Kenne, E.; Labberton, L.; Mccarty, O.J.T.; Schiffelers, R.; Heijnen, H.F.; Hendrickx, A.P.; et al. Polyphosphate nanoparticles on the platelet surface trigger contact system activation. Blood 2017, 129, 1707–1717. Wijeyewickrema, L.C.; Lameignere, E.; Hor, L.; Duncan, R.C.; Shiba, T.; Travers, R.J.; Kapopara, P.R.; Lei, V.; Smith, S.A.; Kim, H.; et al. Polyphosphate is a novel cofactor for regulation of complement by a serpin, C1 inhibitor. Blood 2016, 128, 1766–1776. Smith, S.A.; Morrissey, J.H. Polyphosphate enhances fibrin clot structure. Blood 2008, 112, 2810–2816 Montilla, M.; Hernández-Ruiz, L.; García-Cozar, F.J.; Alvarez-Laderas, I.; Rodríguez-Martorell, J.; Ruiz, F.A. Polyphosphate binds to human von Willebrand factor in vivo and modulates its interaction with glycoprotein Ib. J. Thromb. Haemost. 2012, 10, 2315–2323. Bryckaert, M.; Rosa, J.-P.; Denis, C.V.; Lenting, P.J. Of von Willebrand factor and platelets. Cell. Mol. Life Sci. 2014, 72, 307–326. Favaloro, E.J.; Pasalic, L.; Curnow, J. Laboratory tests used to help diagnose von Willebrand disease: An update. Pathology 2016, 48, 303–318. Skornova, I.; Simurda, T.; Stasko, J.; Zolkova, J.; Sokol, J.; Holly, P.; Dobrotova, M.; Plamenova, I.; Hudecek, J.; Brunclikova, M.; et al. Multimer Analysis of Von Willebrand Factor in Von Willebrand Disease with a Hydrasys Semi-Automatic Analyzer—Single-Center Experience. Diagnostics 2021, 11, 2153. Favaloro, E.J.; Oliver, S.; Mohammed, S.; Vong, R. Comparative assessment of von Willebrand factor multimers vs activity for von Willebrand disease using modern contemporary methodologies. Haemophilia 2020, 26, 503–512. Sadler, J.E. von Willebrand factor assembly and secretion. J. Thromb. Haemost. 2009, 7 (Suppl. 1), 24–27. Wagner, D.D. Cell Biology of von Willebrand Factor. Annu. Rev. Cell Biol. 1990, 6, 217–242. Federici, A.B. The factor VIII/von Willebrand factor complex: Basic and clinical issues. Haematologica 2003, 88, EREP02. Peake, I.; Goodeve, A. Type 1 von Willebrand disease. J. Thromb. Haemost. 2007, 5 (Suppl. 1), 7–11 Simurda, T.; Dobrotova, M.; Skornova, I.; Sokol, J.; Kubisz, P.; Stasko, J. Successful Use of a Highly Purified Plasma von Willebrand Factor Concentrate Containing Little FVIII for the Long-Term Prophylaxis of Severe (Type 3) von Willebrand’s Disease. Semin. Thromb. Hemost. 2017, 43, 639–641. Zhou, Y.-F.; Eng, E.T.; Zhu, J.; Lu, C.; Walz, T.; Springer, T.A. Sequence and structure relationships within von Willebrand factor. Blood 2012, 120, 449–458. Fuller, J.R.; Knockenhauer, K.E.; Leksa, N.C.; Peters, R.T.; Batchelor, J.D. Molecular determinants of the factor VIII/von Willebrand factor complex revealed by BIVV001 cryo-electron microscopy. Blood 2021, 137, 2970–2980. Sehnal, D.; Bittrich, S.; Deshpande, M.; Svobodová, R.; Berka, K.; Bazgier, V.; Velankar, S.; Burley, S.K.; Koča, J.; Rose, A.S. Mol* Viewer: Modern web app for 3D visualization and analysis of large biomolecular structures. Nucleic Acids Res. 2021, 49, W431–W437. Smith, S.; Choi, S.H.; Davis-Harrison, R.; Huyck, J.; Boettcher, J.; Rienstra, C.M.; Morrissey, J. Polyphosphate exerts differential effects on blood clotting, depending on polymer size. Blood 2010, 116, 4353–4359. Pipe, S.W.; Montgomery, R.R.; Pratt, K.P.; Lenting, P.J.; Lillicrap, D. Life in the shadow of a dominant partner: The FVIII-VWF association and its clinical implications for hemophilia A. Blood 2016, 128, 2007–2016. Shi, Q.; Kuether, E.L.; Schroeder, J.A.; Perry, C.L.; Fahs, S.A.; Gill, J.C.; Montgomery, R.R. Factor VIII inhibitors: Von Willebrand factor makes a difference in vitro and in vivo. J. Thromb. Haemost. 2012, 10, 2328–2337. Iorio, A.; Halimeh, S.; Holzhauer, S.; Goldenberg, N.; Marchesini, E.; Marcucci, M.; Young, G.; Bidlingmaier, C.; Brandao, L.R.; Ettingshausen, C.E.; et al. Rate of inhibitor development in previously untreated hemophilia A patients treated with plasma-derived or recombinant factor VIII concentrates: A systematic review. J. Thromb. Haemost. 2010, 8, 1256–1265. Smith, S.A.; Morrissey, J.H. Polyphosphate as a general procoagulant agent. J. Thromb. Haemost. 2008, 6, 1750–1756. Weiss, H.J. Abnormalities of factor VIII and platelet aggregation—Use of ristocetin in diagnosing the von Willebrand syndrome. Blood 1975, 45, 403–412. Nakajima, Y.; Nogami, K.; Yada, K.; Kawamura, T.; Ogiwara, K.; Furukawa, S.; Shimonishi, N.; Takeyama, M.; Shima, M. Evaluation of clinical severity in patients with type 2N von Willebrand disease using microchip-based flow-chamber system. Int. J. Hematol. 2020, 111, 369–377. Hrdinova, J.; Fernández, D.I.; Ercig, B.; Tullemans, B.M.E.; Suylen, D.P.L.; Agten, S.M.; Jurk, K.; Hackeng, T.M.; Vanhoorelbeke, K.; Voorberg, J.; et al. Structure-Based Cyclic Glycoprotein Ibα-Derived Peptides Interfering with von Willebrand Factor-Binding, Affecting Platelet Aggregation under Shear. Int. J. Mol. Sci. 2022, 23, 2046. Okhota, S.; Melnikov, I.; Avtaeva, Y.; Kozlov, S.; Gabbasov, Z. Shear Stress-Induced Activation of von Willebrand Factor and Cardiovascular Pathology. Int. J. Mol. Sci. 2020, 21, 7804. Vollack-Hesse, N.; Oleshko, O.; Werwitzke, S.; Solecka-Witulska, B.; Kannicht, C.; Tiede, A. Recombinant VWF fragments improve bioavailability of subcutaneous factor VIII in hemophilia A mice. Blood 2021, 137, 1072–1081. Morfini, M.; Auerswald, G.; Kobelt, R.A.; Rivolta, G.F.; Rodríguez-Martorell, J.; Scaraggi, F.A.; Altisent, C.; Blatný, J.; Borel-Derlon, A.; Rossi, V. Prophylactic treatment of haemophilia patients with inhibitors: Clinical experience with recombinant factor VIIa in European Haemophilia Centres. Haemophilia 2007, 13, 502–507 Álvarez-Laderas, I.; Núñez, R.; Jiménez-Bárcenas, R.; Martorell, F.J.R.; Garcia-Lozano, J.R.; de Cos, C.; Garrido, R.P. The spectrum of mutations in Southern Spanish patients with von Willebrand disease. Haemophilia 2015, 21, e240–e242. Wurst, H.; Kornberg, A. A soluble exopolyphosphatase of Saccharomyces cerevisiae. Purification and characterization. J. Biol. Chem. 1994, 269, 10996–11001. [ Hernandez-Ruiz, L.; González-García, I.; Castro, C.; A Brieva, J.; A Ruiz, F. Inorganic polyphosphate and specific induction of apoptosis in human plasma cells. Haematologica 2006, 91, 1180–1186. Smith, S.A.; Morrissey, J.H. Sensitive fluorescence detection of polyphosphate in polyacrylamide gels using 4′,6-diamidino-2-phenylindol. Electrophoresis 2007, 28, 3461–3465. |
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Montilla Rodríguez, Liliana MarcelaAtienza- Navarro, IsabelGarcía- Cozar, Francisco JoseCastro, CarmenRodriguez- Martorell, Francisco JavierRuiz, Felix A23(22)2023-08-28T21:24:54Z2023-08-28T21:24:54Z2022-112572-1100https://doi.org/10.3390/ijms232214118https://hdl.handle.net/20.500.12494/52561Montilla M, Atienza-Navarro I, García-Cozar FJ, Castro C, Rodríguez-Martorell FJ, Ruiz FA. Polyphosphate Activates von Willebrand Factor Interaction with Glycoprotein Ib in the Absence of Factor VIII In Vitro. Int J Mol Sci. 2022 Nov 15;23(22):14118. doi: 10.3390/ijms232214118. PMID: 36430595; PMCID: PMC9692336.Polyphosphate (polyP), a phosphate polymer released by activated platelets, may modulate various stages of hemostasis by binding to blood proteins. In this context, we previously reported that polyP binds to the von Willebrand factor (VWF). One of the most significant functions of VWF is to bind to and protect the blood circulating Factor VIII (FVIII). Therefore, here, we study the role of polyP in the VWF-FVIII complex in vitro and suggest its biological significance. Surface plasmon resonance and electrophoretic mobility assays indicated that polyP binds dynamically to VWF only in the absence of FVIII. Using the VWF Ristocetin Cofactor assay, the most accepted method for studying VWF in platelet adhesion, we found that polyP activates this role of VWF only at low levels of FVIII, such as in plasmas with chemically depleted FVIII and plasmas from severe hemophilia A patients. Moreover, we demonstrated that FVIII competes with polyP in the activation of VWF. Finally, polyP also increases the binding of VWF to platelets in samples from patients with type 2 and type 3 von Willebrand disease. We propose that polyP may be used in designing new therapies to activate VWF when FVIII cannot be used.https://scienti.minciencias.gov.co/cvlac/visualizador/generarCurriculoCv.do?cod_rh=0001570468https://orcid.org/0000-0003-0917-4288https://scienti.minciencias.gov.co/gruplac/jsp/visualiza/visualizagr.jsp?nro=00000000009671felix.ruiz@uca.eshttps://scholar.google.com/citations?hl=es&user=68eHCisAAAAJ1-11Universidad Cooperativa de Colombia, Ciencias de la Salud, Medicina, VillavicencioMedicinaVillavicencioFactor VIIIHemophilia APolyphosphateVon Willebrand diseaseVon Willebrand factorPolyphosphate Activates von Willebrand Factor Interaction with Glycoprotein Ib in the Absence of Factor VIII In VitroArtículos Científicoshttp://purl.org/coar/resource_type/c_2df8fbb1http://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articlehttp://purl.org/redcol/resource_type/ARTinfo:eu-repo/semantics/publishedVersionAtribucióninfo:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2Int J Mol SciRuiz, F.A.; Lea, C.R.; Oldfield, E.; Docampo, R. Human Platelet Dense Granules Contain Polyphosphate and Are Similar to Acidocalcisomes of Bacteria and Unicellular Eukaryotes. J. Biol. Chem. 2004, 279, 44250–44257.Moreno-Sanchez, D.; Hernandez-Ruiz, L.; Ruiz, F.A.; Docampo, R. Polyphosphate Is a Novel Pro-inflammatory Regulator of Mast Cells and Is Located in Acidocalcisomes. J. Biol. Chem. 2012, 287, 28435–28444Morrissey, J.H.; Smith, S.A. Polyphosphate as modulator of hemostasis, thrombosis, and inflammation. J. Thromb. Haemost. 2015, 13 (Suppl. 1), S92–S97.Smith, S.A.; Mutch, N.J.; Baskar, D.; Rohloff, P.; Docampo, R.; Morrissey, J.H. Polyphosphate modulates blood coagulation and fibrinolysis. Proc. Natl. Acad. Sci. USA 2006, 103, 903–908.Choi, S.H.; Smith, S.A.; Morrissey, J.H. Polyphosphate is a cofactor for the activation of factor XI by thrombin. Blood 2011, 118, 6963–6970.Choi, S.H.; Smith, S.A.; Morrissey, J.H. Polyphosphate accelerates factor V activation by factor XIa. Thromb. Haemost. 2015, 113, 599–604.Mutch, N.J.; Myles, T.; Leung, L.L.K.; Morrissey, J.H. Polyphosphate binds with high affinity to exosite II of thrombin. J. Thromb. Haemost. 2010, 8, 548–555Puy, C.; Tucker, E.I.; Ivanov, I.S.; Gailani, D.; Smith, S.A.; Morrissey, J.H.; Gruber, A.; McCarty, O.J.T. Platelet-Derived Short-Chain Polyphosphates Enhance the Inactivation of Tissue Factor Pathway Inhibitor by Activated Coagulation Factor XI. PLoS ONE 2016, 11, e0165172.Mutch, N.J.; Engel, R.; de Willige, S.U.; Philippou, H.; Ariëns, R.A.S. Polyphosphate modifies the fibrin network and down-regulates fibrinolysis by attenuating binding of tPA and plasminogen to fibrin. Blood 2010, 115, 3980–3988.Verhoef, J.J.F.; Barendrecht, A.D.; Nickel, K.F.; Dijkxhoorn, K.; Kenne, E.; Labberton, L.; Mccarty, O.J.T.; Schiffelers, R.; Heijnen, H.F.; Hendrickx, A.P.; et al. Polyphosphate nanoparticles on the platelet surface trigger contact system activation. Blood 2017, 129, 1707–1717.Wijeyewickrema, L.C.; Lameignere, E.; Hor, L.; Duncan, R.C.; Shiba, T.; Travers, R.J.; Kapopara, P.R.; Lei, V.; Smith, S.A.; Kim, H.; et al. Polyphosphate is a novel cofactor for regulation of complement by a serpin, C1 inhibitor. Blood 2016, 128, 1766–1776.Smith, S.A.; Morrissey, J.H. Polyphosphate enhances fibrin clot structure. Blood 2008, 112, 2810–2816Montilla, M.; Hernández-Ruiz, L.; García-Cozar, F.J.; Alvarez-Laderas, I.; Rodríguez-Martorell, J.; Ruiz, F.A. Polyphosphate binds to human von Willebrand factor in vivo and modulates its interaction with glycoprotein Ib. J. Thromb. Haemost. 2012, 10, 2315–2323.Bryckaert, M.; Rosa, J.-P.; Denis, C.V.; Lenting, P.J. Of von Willebrand factor and platelets. Cell. Mol. Life Sci. 2014, 72, 307–326.Favaloro, E.J.; Pasalic, L.; Curnow, J. Laboratory tests used to help diagnose von Willebrand disease: An update. Pathology 2016, 48, 303–318.Skornova, I.; Simurda, T.; Stasko, J.; Zolkova, J.; Sokol, J.; Holly, P.; Dobrotova, M.; Plamenova, I.; Hudecek, J.; Brunclikova, M.; et al. Multimer Analysis of Von Willebrand Factor in Von Willebrand Disease with a Hydrasys Semi-Automatic Analyzer—Single-Center Experience. Diagnostics 2021, 11, 2153.Favaloro, E.J.; Oliver, S.; Mohammed, S.; Vong, R. Comparative assessment of von Willebrand factor multimers vs activity for von Willebrand disease using modern contemporary methodologies. Haemophilia 2020, 26, 503–512.Sadler, J.E. von Willebrand factor assembly and secretion. J. Thromb. Haemost. 2009, 7 (Suppl. 1), 24–27.Wagner, D.D. Cell Biology of von Willebrand Factor. Annu. Rev. Cell Biol. 1990, 6, 217–242.Federici, A.B. The factor VIII/von Willebrand factor complex: Basic and clinical issues. Haematologica 2003, 88, EREP02.Peake, I.; Goodeve, A. Type 1 von Willebrand disease. J. Thromb. Haemost. 2007, 5 (Suppl. 1), 7–11Simurda, T.; Dobrotova, M.; Skornova, I.; Sokol, J.; Kubisz, P.; Stasko, J. Successful Use of a Highly Purified Plasma von Willebrand Factor Concentrate Containing Little FVIII for the Long-Term Prophylaxis of Severe (Type 3) von Willebrand’s Disease. Semin. Thromb. Hemost. 2017, 43, 639–641.Zhou, Y.-F.; Eng, E.T.; Zhu, J.; Lu, C.; Walz, T.; Springer, T.A. Sequence and structure relationships within von Willebrand factor. Blood 2012, 120, 449–458.Fuller, J.R.; Knockenhauer, K.E.; Leksa, N.C.; Peters, R.T.; Batchelor, J.D. Molecular determinants of the factor VIII/von Willebrand factor complex revealed by BIVV001 cryo-electron microscopy. Blood 2021, 137, 2970–2980.Sehnal, D.; Bittrich, S.; Deshpande, M.; Svobodová, R.; Berka, K.; Bazgier, V.; Velankar, S.; Burley, S.K.; Koča, J.; Rose, A.S. Mol* Viewer: Modern web app for 3D visualization and analysis of large biomolecular structures. Nucleic Acids Res. 2021, 49, W431–W437.Smith, S.; Choi, S.H.; Davis-Harrison, R.; Huyck, J.; Boettcher, J.; Rienstra, C.M.; Morrissey, J. Polyphosphate exerts differential effects on blood clotting, depending on polymer size. Blood 2010, 116, 4353–4359.Pipe, S.W.; Montgomery, R.R.; Pratt, K.P.; Lenting, P.J.; Lillicrap, D. Life in the shadow of a dominant partner: The FVIII-VWF association and its clinical implications for hemophilia A. Blood 2016, 128, 2007–2016.Shi, Q.; Kuether, E.L.; Schroeder, J.A.; Perry, C.L.; Fahs, S.A.; Gill, J.C.; Montgomery, R.R. Factor VIII inhibitors: Von Willebrand factor makes a difference in vitro and in vivo. J. Thromb. Haemost. 2012, 10, 2328–2337.Iorio, A.; Halimeh, S.; Holzhauer, S.; Goldenberg, N.; Marchesini, E.; Marcucci, M.; Young, G.; Bidlingmaier, C.; Brandao, L.R.; Ettingshausen, C.E.; et al. 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Electrophoresis 2007, 28, 3461–3465.PublicationLICENSElicense.txtlicense.txttext/plain; charset=utf-84334https://repository.ucc.edu.co/bitstreams/6dddb7de-1312-47c5-9443-ec0a7b63960d/download3bce4f7ab09dfc588f126e1e36e98a45MD5120.500.12494/52561oai:repository.ucc.edu.co:20.500.12494/525612024-08-20 16:23:56.605metadata.onlyhttps://repository.ucc.edu.coRepositorio Institucional Universidad Cooperativa de 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