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snake venoms are notably abundant in metalloproteinases (proteins) (SVMPs), which are primarily responsible for inducing hemorrhage and disrupting the hemostatic process and tissue integrity in envenomed victims. In this study, barnettlysin-III (Bar-III), a hemorrhagic P-III SVMP, was purified from the venom of the Peruvian snake Bothrops barnetti. Bar-III has a molecular mass of approximately 50 kDa and is a glycosylation-dependent functional metalloproteinase. Some biochemical properties of Bar-III, including the full amino acid sequence deduced from its cDNA, are reported. Its enzymatic activity is increased by Ca2+ ions and inhibited by an excess of Zn2+. Synthetic metalloproteinase inhibitors and EDTA also inhibit its proteolytic action. Bar-III degrades several plasma and ECM proteins, including fibrin(ogen), fibronectin, laminin, and nidogen. Platelets play a key role in hemostasis and thrombosis and in other biological process, such as inflammation and immunity, and platelet activation is driven by the platelet signaling receptors, glycoprotein (GP)Ib-IX-V, which binds vWF, and GPVI, which binds collagen. Moreover, Bar-III inhibits vWF- and convulxin-induced platelet aggregation in human washed platelets by cleaving the recombinant A1 domain of vWF and GPVI into a soluble ectodomain fraction of ~55 kDa (sGPVI). Bar-III does not reduce the viability of cultured endothelial cells; however, it interferes with the adhesion of these cells to fibronectin, vitronectin, and RGD peptides, as well as their migration profile. Bar-III binds specifically to the surface of these cells, and part of this interaction involves \u03b15\u03b21 integrin receptors. These results contribute to a better comprehension of the pathophysiology of snakebite accidents\/incidents and could be used as a tool to explore novel and safer anti-venom therapeutics.<\/jats:p>","DOI":"10.3390\/toxins16110486","type":"journal-article","created":{"date-parts":[[2024,11,11]],"date-time":"2024-11-11T11:34:11Z","timestamp":1731324851000},"page":"486","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["A Novel P-III Metalloproteinase from Bothrops barnetti Venom Degrades Extracellular Matrix Proteins, Inhibits Platelet Aggregation, and Disrupts Endothelial Cell Adhesion via \u03b15\u03b21 Integrin Receptors to Arginine\u2013Glycine\u2013Aspartic Acid (RGD)-Containing Molecules"],"prefix":"10.3390","volume":"16","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8454-7454","authenticated-orcid":false,"given":"Pedro Henrique de Caires","family":"Schluga","sequence":"first","affiliation":[{"name":"Laborat\u00f3rio de Matriz Extracelular e Biotecnologia de Venenos, Universidade Federal do Paran\u00e1, UFPR, Curitiba 81531-980, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7141-7765","authenticated-orcid":false,"given":"Debora","family":"Larangote","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Toxinologia de Venenos Animais, Funda\u00e7\u00e3o Ezequiel Dias, FUNED, Belo Horizonte 30510-010, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ana Maria","family":"de Melo","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Matriz Extracelular e Biotecnologia de Venenos, Universidade Federal do Paran\u00e1, UFPR, Curitiba 81531-980, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Guilherme Kamienski","family":"Lobermayer","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Matriz Extracelular e Biotecnologia de Venenos, Universidade Federal do Paran\u00e1, UFPR, Curitiba 81531-980, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9385-6921","authenticated-orcid":false,"given":"Daniel","family":"Torrej\u00f3n","sequence":"additional","affiliation":[{"name":"Laboratorio de Biolog\u00eda Molecular, Facultad de Ciencias Biol\u00f3gicas, Universidad Nacional Mayor de San Marcos, Lima 15081, Peru"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2784-5658","authenticated-orcid":false,"given":"Luciana Souza","family":"de Oliveira","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Toxinologia de Venenos Animais, Funda\u00e7\u00e3o Ezequiel Dias, FUNED, Belo Horizonte 30510-010, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2631-4182","authenticated-orcid":false,"given":"Valeria Gon\u00e7alves","family":"Alvarenga","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Toxinologia de Venenos Animais, Funda\u00e7\u00e3o Ezequiel Dias, FUNED, Belo Horizonte 30510-010, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4417-2026","authenticated-orcid":false,"given":"Dan Erick","family":"Vivas-Ruiz","sequence":"additional","affiliation":[{"name":"Laboratorio de Biolog\u00eda Molecular, Facultad de Ciencias Biol\u00f3gicas, Universidad Nacional Mayor de San Marcos, Lima 15081, Peru"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Silvio Sanches","family":"Veiga","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Matriz Extracelular e Biotecnologia de Venenos, Universidade Federal do Paran\u00e1, UFPR, Curitiba 81531-980, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eladio Flores","family":"Sanchez","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Toxinologia de Venenos Animais, Funda\u00e7\u00e3o Ezequiel Dias, FUNED, Belo Horizonte 30510-010, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luiza Helena","family":"Gremski","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Matriz Extracelular e Biotecnologia de Venenos, Universidade Federal do Paran\u00e1, UFPR, Curitiba 81531-980, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,11,9]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.jprot.2009.07.013","article-title":"Snake Venomics and Antivenomics of Bothrops Atrox Venoms from Colombia and the Amazon Regions of Brazil, Per\u00fa and Ecuador Suggest the Occurrence of Geographic Variation of Venom Phenotype by a Trend towards Paedomorphism","volume":"73","author":"Cid","year":"2009","journal-title":"J. Proteom."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/j.toxicon.2011.01.006","article-title":"Haemostatically Active Proteins in Snake Venoms","volume":"57","author":"Sajevic","year":"2011","journal-title":"Toxicon"},{"key":"ref_3","first-page":"42","article-title":"Snakebite Envenomation and Death in the Developing World","volume":"19","author":"Cruz","year":"2009","journal-title":"Ethn. Dis."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1080\/00222933808526872","article-title":"The Vertical Distribution of Some Reptiles and Amphibians in Southern Ecuador","volume":"2","author":"Parker","year":"1938","journal-title":"Ann. Mag. Nat. Hist."},{"key":"ref_5","unstructured":"Campbell, J.A., and Lamar, W.W. (2004). The Venomous Reptiles of the Western Hemisphere, Cornell University Press. [1st ed.]."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/j.toxicon.2016.09.010","article-title":"Neutralization of Toxicological Activities of Medically-Relevant Bothrops Snake Venoms and Relevant Toxins by Two Polyvalent Bothropic Antivenoms Produced in Peru and Brazil","volume":"122","author":"Gontijo","year":"2016","journal-title":"Toxicon"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/S0140-6736(09)61754-2","article-title":"Snake Bite","volume":"375","author":"Warrell","year":"2010","journal-title":"Lancet"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"2181","DOI":"10.1016\/j.jprot.2012.01.020","article-title":"Exploring the Proteomes of the Venoms of the Peruvian Pit Vipers Bothrops Atrox, B. Barnetti and B. Pictus","volume":"75","author":"Kohlhoff","year":"2012","journal-title":"J. Proteom."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1186\/1471-2164-11-605","article-title":"A Transcriptomic Analysis of Gene Expression in the Venom Gland of the Snake Bothrops Alternatus (Urutu)","volume":"11","author":"Cardoso","year":"2010","journal-title":"BMC Genom."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1007\/s00204-022-03420-0","article-title":"A Current Perspective on Snake Venom Composition and Constituent Protein Families","volume":"97","author":"Tasoulis","year":"2023","journal-title":"Arch. Toxicol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"8","DOI":"10.3390\/toxins8050155","article-title":"ADAM and ADAMTS Family Proteins and Snake Venom Metalloproteinases: A Structural Overview","volume":"8","author":"Takeda","year":"2016","journal-title":"Toxins"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1236","DOI":"10.1016\/j.toxicon.2010.03.011","article-title":"Snaclecs (Snake C-Type Lectins) That Inhibit or Activate Platelets by Binding to Receptors","volume":"56","author":"Clemetson","year":"2010","journal-title":"Toxicon"},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Po\u017eek, K., Leonardi, A., Punger\u010dar, J., Rao, W., Gao, Z., Liu, S., Laustsen, A.H., Bakija, A.T., Reber\u0161ek, K., and Podgornik, H. (2022). Genomic Confirmation of the P-IIIe Subclass of Snake Venom Metalloproteinases and Characterisation of Its First Member, a Disintegrin-like\/Cysteine-Rich Protein. Toxins, 14.","DOI":"10.3390\/toxins14040232"},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Oliveira, L.S., Estev\u00e3o-Costa, M.I., Alvarenga, V.G., Vivas-Ruiz, D.E., Yarleque, A., Lima, A.M., Cavaco, A., Eble, J.A., and Sanchez, E.F. (2019). Atroxlysin-III, A Metalloproteinase from the Venom of the Peruvian Pit Viper Snake Bothrops Atrox (Jerg\u00f3n) Induces Glycoprotein VI Shedding and Impairs Platelet Function. Molecules, 24.","DOI":"10.3390\/molecules24193489"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1016\/j.toxicon.2005.02.012","article-title":"Structural Considerations of the Snake Venom Metalloproteinases, Key Members of the M12 Reprolysin Family of Metalloproteinases","volume":"45","author":"Fox","year":"2005","journal-title":"Toxicon"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/S0014-5793(03)00799-3","article-title":"Identification of Sites in the Cysteine-Rich Domain of the Class P-III Snake Venom Metalloproteinases Responsible for Inhibition of Platelet Function","volume":"549","author":"Kamiguti","year":"2003","journal-title":"FEBS Lett."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1016\/j.biochi.2010.10.007","article-title":"Disintegrin-like\/Cysteine-Rich Domains of the Reprolysin HF3: Site-Directed Mutagenesis Reveals Essential Role of Specific Residues","volume":"93","author":"Menezes","year":"2011","journal-title":"Biochimie"},{"key":"ref_18","doi-asserted-by":"crossref","unstructured":"Baldo, C., Jamora, C., Yamanouye, N., Zorn, T.M., and Moura-da-Silva, A.M. (2010). Mechanisms of Vascular Damage by Hemorrhagic Snake Venom Metalloproteinases: Tissue Distribution and in Situ Hydrolysis. PLoS Negl. Trop. Dis., 4.","DOI":"10.1371\/journal.pntd.0000727"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1016\/j.abb.2006.09.018","article-title":"Novel Insights into Capillary Vessel Basement Membrane Damage by Snake Venom Hemorrhagic Metalloproteinases: A Biochemical and Immunohistochemical Study","volume":"455","author":"Escalante","year":"2006","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Herrera, C., Voisin, M.B., Escalante, T., Rucavado, A., Nourshargh, S., and Guti\u00e9rrez, J.M. (2016). Effects of PI and PIII Snake Venom Haemorrhagic Metalloproteinases on the Microvasculature: A Confocal Microscopy Study on the Mouse Cremaster Muscle. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0168643"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1042\/bj3200635","article-title":"Inhibition of Collagen-Induced Platelet Aggregation as the Result of Cleavage of A2\u03b21-Integrin by the Snake Venom Metalloproteinase Jararhagin","volume":"320","author":"Kamiguti","year":"1996","journal-title":"Biochem. J."},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Kini, R.M., and Koh, C.Y. (2016). Metalloproteases Affecting Blood Coagulation, Fibrinolysis and Platelet Aggregation from Snake Venoms: Definition and Nomenclature of Interaction Sites. Toxins, 8.","DOI":"10.3390\/toxins8100284"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"39746","DOI":"10.1074\/jbc.M604855200","article-title":"The Cysteine-Rich Domain of Snake Venom Metalloproteinases Is a Ligand for von Willebrand Factor A Domains: Role in Substrate Targeting","volume":"281","author":"Serrano","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"107097","DOI":"10.1016\/j.toxicon.2023.107097","article-title":"Rhomb-I, a P\u2013I Metalloproteinase from Lachesis Muta Rhombeata Venom Degrades Vessel Extra Cellular Matrix Components and Impairs Platelet Aggregation","volume":"228","author":"Oliveira","year":"2023","journal-title":"Toxicon"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1055\/s-0037-1615236","article-title":"Purification and Characterization of Kaouthiagin, a von Willebrand Factor-Binding and -Cleaving Metalloproteinase from Naja Kaouthia Cobra Venom","volume":"80","author":"Hamako","year":"1998","journal-title":"Thromb. Haemost."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"13094","DOI":"10.1074\/jbc.272.20.13094","article-title":"Function of Disintegrin-like\/Cysteine-Rich Domains of Atrolysin A. Inhibition of Platelet Aggregation by Recombinant Protein and Peptide Antagonists","volume":"272","author":"Jia","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1006\/abbi.1996.9787","article-title":"Crovidisin, a Collagen-Binding Protein Isolated from Snake Venom of Crotalus Viridis, Prevents Platelet-Collagen Interaction","volume":"337","author":"Liu","year":"1997","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1006\/abbi.2000.2120","article-title":"The Disintegrin-like Domain of the Snake Venom Metalloprotease Alternagin Inhibits A2\u03b21 Integrin-Mediated Cell Adhesion","volume":"384","author":"Souza","year":"2000","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1065","DOI":"10.1016\/j.biochi.2005.06.002","article-title":"Primary Structure and Antiplatelet Mechanism of a Snake Venom Metalloproteinase, Acurhagin, from Agkistrodon Acutus Venom","volume":"87","author":"Wang","year":"2005","journal-title":"Biochimie"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1016\/j.bbrc.2003.08.049","article-title":"A Novel Disintegrin-like Domain of a High Molecular Weight Metalloprotease Inhibits Platelet Aggregation","volume":"309","author":"You","year":"2003","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1042\/bj3070411","article-title":"Molecular Cloning and Expression of Catrocollastatin, a Snake-Venom Protein from Crotalus Atrox (Western Diamondback Rattlesnake) Which Inhibits Platelet Adhesion to Collagen","volume":"307","author":"Zhou","year":"1995","journal-title":"Biochem. J."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1002\/rth2.12096","article-title":"Proteolytic Processing of Platelet Receptors","volume":"2","author":"Gardiner","year":"2018","journal-title":"Res. Pract. Thromb. Haemost."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1511","DOI":"10.1161\/ATVBAHA.107.141390","article-title":"Platelet Receptor Proteolysis: A Mechanism for Downregulating Platelet Reactivity","volume":"27","author":"Andrews","year":"2007","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/j.abb.2007.10.002","article-title":"Structural and Functional Characterization of a P-III Metalloproteinase, Leucurolysin-B, from Bothrops Leucurus Venom","volume":"468","author":"Sanchez","year":"2007","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"542","DOI":"10.1016\/j.bbagen.2015.12.021","article-title":"A Novel Fibrinolytic Metalloproteinase, Barnettlysin-I from Bothrops Barnetti (Barnett\u2019s Pitviper) Snake Venom with Anti-Platelet Properties","volume":"1860","author":"Sanchez","year":"2016","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1016\/j.toxicon.2008.08.021","article-title":"The Three-Dimensional Structure of Bothropasin, the Main Hemorrhagic Factor from Bothrops Jararaca Venom: Insights for a New Classification of Snake Venom Metalloprotease Subgroups","volume":"52","author":"Muniz","year":"2008","journal-title":"Toxicon"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"1363","DOI":"10.1161\/01.ATV.18.9.1363","article-title":"Fibronectin: Structure, Assembly, and Cardiovascular Implications","volume":"18","author":"Magnusson","year":"1998","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1016\/0014-5793(91)80810-P","article-title":"Plasmin Cleavage of Vitronectin Identification of the Site and Consequent Attenuation in Binding Plasminogen Activator Inhibitor-1","volume":"285","author":"Chain","year":"1991","journal-title":"FEBS Lett."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"3016","DOI":"10.1111\/j.1742-4658.2008.06466.x","article-title":"Insights into and Speculations about Snake Venom Metalloproteinase (SVMP) Synthesis, Folding and Disulfide Bond Formation and Their Contribution to Venom Complexity","volume":"275","author":"Fox","year":"2008","journal-title":"FEBS J."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"10330","DOI":"10.1186\/1758-2946-3-S1-O22","article-title":"Backbone Flexibility Controls the Activity and Specificity of a Protein-Protein Interface\u2014Specificity in Snake Venom Metalloproteases (SVMPs)","volume":"3","author":"Wallnoefer","year":"2011","journal-title":"J. Cheminform."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"19274","DOI":"10.1073\/pnas.0909755106","article-title":"Crystal Structures of the Noncatalytic Domains of ADAMTS13 Reveal Multiple Discontinuous Exosites for von Willebrand Factor","volume":"106","author":"Akiyama","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"891","DOI":"10.1016\/j.jmb.2007.07.047","article-title":"Crystal Structures of Human ADAMTS-1 Reveal a Conserved Catalytic Domain and a Disintegrin-like Domain with a Fold Homologous to Cysteine-Rich Domains","volume":"373","author":"Gerhardt","year":"2007","journal-title":"J. Mol. Biol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"29077","DOI":"10.1074\/jbc.M109.014258","article-title":"Structural Characterization of the Ectodomain of a Disintegrin and Metalloproteinase-22 (ADAM22), a Neural Adhesion Receptor Instead of Metalloproteinase. Insights on Adam Function","volume":"284","author":"Liu","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1110\/ps.073287008","article-title":"Crystal Structures of the Two Major Aggrecan Degrading Enzymes, ADAMTS4 and ADAMTS5","volume":"17","author":"Mosyak","year":"2008","journal-title":"Protein Sci."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1016\/j.bbapap.2011.04.009","article-title":"Snake Venom Metalloproteinases: Structure, Function and Relevance to the Mammalian ADAM\/ADAMTS Family Proteins","volume":"1824","author":"Takeda","year":"2012","journal-title":"Biochim. Biophys. Acta Proteins Proteom."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1041","DOI":"10.1016\/j.toxicon.2005.02.026","article-title":"Platelets as Targets of Snake Venom Metalloproteinases","volume":"45","author":"Kamiguti","year":"2005","journal-title":"Toxicon"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"3611","DOI":"10.1111\/j.1742-4658.2007.05895.x","article-title":"Interaction of the Cysteine-Rich Domain of Snake Venom Metalloproteinases with the A1 Domain of von Willebrand Factor Promotes Site-Specific Proteolysis of von Willebrand Factor and Inhibition of von Willebrand Factor-Mediated Platelet Aggregation","volume":"274","author":"Serrano","year":"2007","journal-title":"FEBS J."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1055\/s-0037-1613061","article-title":"Purification and Characterization of a Novel Metalloproteinase, Acurhagin, from Agkistrodon Acutus Venom","volume":"87","author":"Wang","year":"2002","journal-title":"Thromb. Haemost."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"100052","DOI":"10.1016\/j.toxcx.2020.100052","article-title":"Snake Venom Metalloproteinases (SVMPs): A Structure-Function Update","volume":"7","author":"Olaoba","year":"2020","journal-title":"Toxicon X"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1372","DOI":"10.1172\/JCI114581","article-title":"Vitronectin Binds to Activated Human Platelets and Plays a Role in Platelet Aggregation","volume":"85","author":"Asch","year":"1990","journal-title":"J. Clin. Invest."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/S0021-9150(99)00241-5","article-title":"Platelets Induce Alterations of Chemotactic and Adhesive Properties of Endothelial Cells Mediated through an Interleukin-1-Dependent Mechanism. Implications for Atherogenesis","volume":"148","author":"Gawaz","year":"2000","journal-title":"Atherosclerosis"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1055\/s-0038-1648847","article-title":"Properties of Fibrinogen Cleaved by Jararhagin, a Metalloproteinase from the Venom of Bothrops Jararaca","volume":"72","author":"Kamiguti","year":"1994","journal-title":"Thromb. Haemost."},{"key":"ref_53","doi-asserted-by":"crossref","unstructured":"Herrera, C., Escalante, T., Voisin, M.B., Rucavado, A., Moraz\u00e1n, D., Mac\u00eado, J.K.A., Calvete, J.J., Sanz, L., Nourshargh, S., and Guti\u00e9rrez, J.M. (2015). Tissue Localization and Extracellular Matrix Degradation by PI, PII and PIII Snake Venom Metalloproteinases: Clues on the Mechanisms of Venom-Induced Hemorrhage. PLoS Negl. Trop. Dis., 9.","DOI":"10.1371\/journal.pntd.0003731"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"984","DOI":"10.1124\/mol.107.038018","article-title":"Antithrombotic Effect of a Protein-Type I Class Snake Venom Metalloproteinase, Kistomin, Is Mediated by Affecting Glycoprotein Ib-von Willebrand Factor Interaction","volume":"72","author":"Hsu","year":"2007","journal-title":"Mol. Pharmacol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1075","DOI":"10.1016\/j.toxicon.2005.02.023","article-title":"Structure and Function of Snake Venom Toxins Interacting with Human von Willebrand Factor","volume":"45","author":"Matsui","year":"2005","journal-title":"Toxicon"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.biochi.2021.01.016","article-title":"A Fibrinolytic Snake Venom Metalloproteinase, Mutalysin-II, with Antiplatelet Activity and Targeting Capability toward Glycoprotein GPIb\u03b1 and Glycoprotein GPVI","volume":"184","author":"Sanchez","year":"2021","journal-title":"Biochimie"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"3011","DOI":"10.1074\/jbc.M109714200","article-title":"The Platelet Receptor GPVI Mediates Both Adhesion and Signaling Responses to Collagen in a Receptor Density-Dependent Fashion","volume":"277","author":"Chen","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"2120","DOI":"10.1093\/emboj\/20.9.2120","article-title":"Glycoprotein VI but Not A2\u03b21 Integrin Is Essential for Platelet Interaction with Collagen","volume":"20","author":"Nieswandt","year":"2001","journal-title":"EMBO J."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"53955","DOI":"10.1074\/jbc.M410355200","article-title":"Vav1 and Vav3 Have Critical but Redundant Roles in Mediating Platelet Activation by Collagen","volume":"279","author":"Pearce","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1712","DOI":"10.1182\/blood.V69.6.1712.1712","article-title":"A Novel Platelet Aggregating Factor Found in a Patient with Defective Collagen-Induced Platelet Aggregation and Autoimmune Thrombocytopenia","volume":"69","author":"Sugiyama","year":"1987","journal-title":"Blood"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/j.biochi.2006.08.009","article-title":"Purification and Functional Characterization of AAV1, a Novel P-III Metalloproteinase, from Formosan Agkistrodon Acutus Venom","volume":"89","author":"Wang","year":"2007","journal-title":"Biochimie"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1097\/GIM.0b013e3182035931","article-title":"Von Willebrand Disease","volume":"13","author":"James","year":"2011","journal-title":"Genet. Med."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/S0950-3536(96)80060-6","article-title":"Molecular Basis of von Willebrand Disease","volume":"9","author":"Mazurier","year":"1996","journal-title":"Bailli\u00e8res Clin. Haematol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1176","DOI":"10.1126\/science.107355","article-title":"Structures of Glycoprotein Ib\u03b1 and Its Complex with von Willebrand Factor A1 Domain","volume":"297","author":"Huizinga","year":"2002","journal-title":"Science"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"997","DOI":"10.1016\/j.toxicon.2005.02.029","article-title":"Hemorrhage Induced by Snake Venom Metalloproteinases: Biochemical and Biophysical Mechanisms Involved in Microvessel Damage","volume":"45","author":"Rucavado","year":"2005","journal-title":"Toxicon"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1689","DOI":"10.1016\/0041-0101(94)90330-1","article-title":"Effect of Various Viperidae and Crotalidae Snake Venoms on Endothelial Cells In Vitro","volume":"32","author":"Borkow","year":"1994","journal-title":"Toxicon"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"844","DOI":"10.1016\/j.toxicon.2006.02.006","article-title":"The Effect of Brown Spider Venom on Endothelial Cell Morphology and Adhesive Structures","volume":"47","author":"Paludo","year":"2006","journal-title":"Toxicon"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"107210","DOI":"10.1016\/j.toxicon.2023.107210","article-title":"Cobra Venom P-III Class Metalloproteinase Atrase A Induces Inflammatory Response and Cell Apoptosis in Endothelial Cells via Its Metalloproteinase Domain","volume":"232","author":"Wei","year":"2023","journal-title":"Toxicon"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1007\/s10495-005-2945-1","article-title":"Jararhagin, a Snake Venom Metalloproteinase, Induces a Specialized Form of Apoptosis (Anoikis) Selective to Endothelial Cells","volume":"10","author":"Tanjoni","year":"2005","journal-title":"Apoptosis"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"3339","DOI":"10.1046\/j.1432-1327.2001.02246.x","article-title":"Purification, CDNA Cloning and Characterization of the Vascular Apoptosis-Inducing Protein, HV1, from Trimeresurus Flavoviridis","volume":"268","author":"Masuda","year":"2001","journal-title":"Eur. J. Biochem."},{"key":"ref_71","doi-asserted-by":"crossref","unstructured":"Oyama, E., and Takahashi, H. (2017). Structures and Functions of Snake Venom Metalloproteinases (SVMP) from Protobothrops Venom Collected in Japan. Molecules, 22.","DOI":"10.3390\/molecules22081305"},{"key":"ref_72","doi-asserted-by":"crossref","unstructured":"Guti\u00e9rrez, J.M., Escalante, T., Rucavado, A., Herrera, C., and Fox, J.W. (2016). A Comprehensive View of the Structural and Functional Alterations of Extracellular Matrix by Snake Venom Metalloproteinases (SVMPs): Novel Perspectives on the Pathophysiology of Envenoming. Toxins, 8.","DOI":"10.3390\/toxins8100304"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/j.semcdb.2008.07.009","article-title":"Three-Dimensional Domain Architecture of the ADAM Family Proteinases","volume":"20","author":"Takeda","year":"2009","journal-title":"Semin. Cell Dev. Biol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"2388","DOI":"10.1038\/sj.emboj.7601131","article-title":"Crystal Structures of VAP1 Reveal ADAMs\u2019 MDC Domain Architecture and Its Unique C-Shaped Scaffold","volume":"25","author":"Takeda","year":"2006","journal-title":"EMBO J."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.1016\/j.toxicon.2009.12.010","article-title":"Different Regions of the Class P-III Snake Venom Metalloproteinase Jararhagin Are Involved in Binding to A2\u03b21 Integrin and Collagen","volume":"55","author":"Tanjoni","year":"2010","journal-title":"Toxicon"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1186\/s40409-018-0150-2","article-title":"Alternagin-C Binding to A2\u03b21 Integrin Controls Matrix Metalloprotease-9 and Matrix Metalloprotease-2 in Breast Tumor Cells and Endothelial Cells","volume":"24","author":"Micocci","year":"2018","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.1016\/S0021-9258(18)54042-4","article-title":"Design of Potent and Specific Integrin Antagonists: Peptide Antagonists with High Specificity for Glycoprotein IIb-IIIa","volume":"268","author":"Scarborough","year":"1993","journal-title":"J. Biol. Chem."},{"key":"ref_78","doi-asserted-by":"crossref","unstructured":"Ruggeri, Z.M., and Jackson, S.P. (2013). Platelet Thrombus Formation in Flowing Blood. Platelets, Elsevier Inc.. [3rd ed.].","DOI":"10.1016\/B978-0-12-387837-3.00020-1"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.ceb.2016.03.014","article-title":"Collaboration of Fibronectin Matrix with Other Extracellular Signals in Morphogenesis and Differentiation","volume":"42","author":"Vega","year":"2016","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_80","doi-asserted-by":"crossref","unstructured":"Maria, A.A., da Silva, L.G.L., Correia, C.C., and Ruiz, G.R.G. (2014). Antiproliferative Effect of the Jararhagin Toxin on B16F10 Murine Melanoma. BMC Complement. Altern. Med., 14.","DOI":"10.1186\/1472-6882-14-446"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1242\/jcs.000232","article-title":"Integrin A9\u03b21 Is a Receptor for Nerve Growth Factor and Other Neurotrophins","volume":"121","author":"Staniszewska","year":"2008","journal-title":"J. Cell Sci."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1016\/j.toxicon.2006.12.013","article-title":"Inhibition of Melanoma Cell Motility by the Snake Venom Disintegrin Eristostatin","volume":"49","author":"Tian","year":"2007","journal-title":"Toxicon"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1016\/j.toxicon.2014.11.228","article-title":"Inhibition of Pancreatic Tumoral Cells by Snake Venom Disintegrins","volume":"93","author":"Lucena","year":"2015","journal-title":"Toxicon"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1016\/j.toxicon.2011.02.020","article-title":"Development of a Chimeric Recombinant Disintegrin as a Cost-Effective Anti-Cancer Agent with Promising Translational Potential","volume":"59","author":"Minea","year":"2012","journal-title":"Toxicon"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1023\/A:1006457903545","article-title":"Contortrostatin, a Dimeric Disintegrin from Agkistrodon Contortrix Contortrix, Inhibits Breast Cancer Progression","volume":"61","author":"Zhou","year":"2000","journal-title":"Breast Cancer Res. Treat."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"2851","DOI":"10.2174\/138161207782023720","article-title":"Pharmacological Impact of Snake Venom Compounds","volume":"13","author":"Marcinkiewicz","year":"2007","journal-title":"Curr. Pharm. Des."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"1476","DOI":"10.1016\/j.biochi.2013.03.015","article-title":"Coagulant Thrombin-like Enzyme (Barnettobin) from Bothrops Barnetti Venom: Molecular Sequence Analysis of Its CDNA and Biochemical Properties","volume":"95","author":"Sandoval","year":"2013","journal-title":"Biochimie"},{"key":"ref_89","doi-asserted-by":"crossref","unstructured":"Torrej\u00f3n, D., C\u00e1rdenas, J., Ju\u00e1rez, D., Espinoza, J., Prole\u00f3n, A., Agurto-Arteaga, A., Lazo, F., Legu\u00eda, M., Urra, F.A., and S\u00e1nchez, E.F. (2023). Comparison of Four Methods of RNA Extraction and CDNA Synthesis from The Venom of Peruvian Snakes of the Genus Bothrops of Clinical Importance. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms241311161"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1093\/nar\/gku316","article-title":"Deciphering Key Features in Protein Structures with the New ENDscript Server","volume":"42","author":"Robert","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"D384","DOI":"10.1093\/nar\/gkac1096","article-title":"The Conserved Domain Database in 2023","volume":"51","author":"Wang","year":"2023","journal-title":"Nucleic Acids Res."},{"key":"ref_92","unstructured":"(2022, May 05). ProtParam\u2014Expasy. Available online: https:\/\/web.expasy.org\/protparam\/."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1038\/s41592-022-01488-1","article-title":"ColabFold: Making Protein Folding Accessible to All","volume":"19","author":"Mirdita","year":"2022","journal-title":"Nat. Methods"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"1121","DOI":"10.3181\/0703-MR-72","article-title":"Structure and Function of Basement Membranes","volume":"232","author":"LeBleu","year":"2007","journal-title":"Exp. Biol. Med."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"1609","DOI":"10.1016\/j.dib.2016.04.054","article-title":"Data for a Direct Fibrinolytic Metalloproteinase, Barnettlysin-I from Bothrops Barnetti (Barnett\u2019s Pitviper) Snake Venom with Anti-Thrombotic Effect","volume":"7","author":"Sanchez","year":"2016","journal-title":"Data Br."},{"key":"ref_96","unstructured":"Harlow, E., and Lane, D. (1988). Antibodies: A Laboratory Manual, Cold Spring Harbor Laboratory Press."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"1612","DOI":"10.1073\/pnas.73.5.1612","article-title":"Hormone and Neurotransmitter Receptors in an Established Vascular Endothelial Cell Line","volume":"73","author":"Buonassisi","year":"1976","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1038\/nprot.2007.30","article-title":"In Vitro Scratch Assay: A Convenient and Inexpensive Method for Analysis of Cell Migration in Vitro","volume":"2","author":"Liang","year":"2007","journal-title":"Nat. Protoc."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1038\/nmeth.2089","article-title":"NIH Image to ImageJ: 25 Years of Image Analysis","volume":"9","author":"Schneider","year":"2012","journal-title":"Nat. Methods"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1038\/bjc.1989.347","article-title":"Antimetastatic Effects of Synthetic Polypeptides Containing Repeated Structures of the Cell Adhesive Arg-Gly-Asp (RGD) and Tyr-Ile-Gly-Ser-Arg (YIGSR) Sequences","volume":"60","author":"Saiki","year":"1989","journal-title":"Br. J. 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