Publication de 6 numéros par an
ISSN Imprimer: 1045-4403
ISSN En ligne: 2162-6502
Indexed in
The Biology of Prothrombin
RÉSUMÉ
Prothrombin and thrombin are involved in diverse biological functions. The structure of prothrombin has been studied extensively and its cDNA has been cloned from several species. The tissue-specific expression of this protein has been studied, as well as the developmental expression pattern. The structure of the human gene coding for prothrombin has been determined, and gene regulation studies have been performed that indicate that HNF-1 might be responsible for the liver-specific expression of this protein. Other regulatory elements have been identified. In order to further study the biological properties of prothrombin, prothrombin-deficient mice have been generated using gene targeting technology. Prothrombin deficiency in mice results in partial embryonic lethality. The mice that survive to birth die from bleeding events. The embryonic lethality occurs between embryonic days 9.5 and 11.5 and appears to be due to the loss of integrity of the vasculature due to a failure in blood coagulation. These results indicate that prothrombin plays not only a key role in hemostasis but suggests that it may be important for mouse development.
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Lefkowitz J. B., Weller A., Nuss R., Santiago-Borrero P. J., Brown D. L., Ortiz I. R., A common mutation, Arg457Gln, links prothrombin deficiencies in the Puerto Rican population, Journal of Thrombosis and Haemostasis, 1, 11, 2003. Crossref
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Mar�n Yar� E., Chen Suzie, Involvement of metabotropic glutamate receptor�1, a G protein coupled receptor, in melanoma development, Journal of Molecular Medicine, 82, 11, 2004. Crossref
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Oh Jeong Hwan, Moon Hyo-Bang, Choe Eun Sang, Alterations in Differentially Expressed Genes in the Head of Oryzias latipes Following Benzo[a]pyrene Exposure, Bulletin of Environmental Contamination and Toxicology, 84, 6, 2010. Crossref
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Belogurov Alexey, Kozyr Arina, Ponomarenko Natalia, Gabibov Alexander, Catalytic antibodies: balancing between Dr. Jekyll and Mr. Hyde, BioEssays, 31, 11, 2009. Crossref
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Pagano Bruno, Martino Luigi, Randazzo Antonio, Giancola Concetta, Stability and Binding Properties of a Modified Thrombin Binding Aptamer, Biophysical Journal, 94, 2, 2008. Crossref
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Urra Félix A., Pulgar Rodrigo, Gutiérrez Ricardo, Hodar Christian, Cambiazo Verónica, Labra Antonieta, Identification and molecular characterization of five putative toxins from the venom gland of the snake Philodryas chamissonis (Serpentes: Dipsadidae), Toxicon, 108, 2015. Crossref
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Fiotti N., Di Chiara A., Altamura N., Miccio M., Fioretti P., Guarnieri G., Giansante C., Coagulation indicators in chronic stable effort angina and unstable angina: relationship with acute phase reactants and clinical outcome, Blood Coagulation & Fibrinolysis, 13, 3, 2002. Crossref
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Monteiro Robson Q, Campana Patricia T, Melo Paulo A, Bianconi M.Lucia, Suramin interaction with human α-thrombin: inhibitory effects and binding studies, The International Journal of Biochemistry & Cell Biology, 36, 10, 2004. Crossref
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Mariano-Oliveira Andréa, De Freitas Marta S., Monteiro Robson Q., Barja-Fidalgo Christina, Prothrombin fragments containing kringle domains induce migration and activation of human neutrophils, The International Journal of Biochemistry & Cell Biology, 40, 3, 2008. Crossref
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Sadana Ajit, Sadana Neeti, Binding and Dissociation of Biomarkers for Systemic Lupus Erythematosus, in Biomarkers and Biosensors, 2015. Crossref
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Car B. D., Eng V. M., Special Considerations in the Evaluation of the Hematology and Hemostasis of Mutant Mice, Veterinary Pathology, 38, 1, 2001. Crossref
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Zhu He, Hoppensteadt Debra, Iqbal Omer, Litinas Evangelos, Adiguzel Cafer, Fareed Jawed, Relative Purity of Different Bovine Thrombin Preparations, Clinical and Applied Thrombosis/Hemostasis, 15, 6, 2009. Crossref
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Festoff Barry W., Role of Proteinase-Activated Receptors in Brain Function, in Proteases In The Brain, 3, 2005. Crossref
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Sun William Y., Burkart Melissa C., Holahan Joseph R., Degen Sandra J. F., Prothrombin San Antonio: a single amino acid substitution at a Factor Xa activation site (Arg320 to His) results in dysprothrombinemia, Blood, 95, 2, 2000. Crossref
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Butenas Saulius, van’t Veer Cornelis, Mann Kenneth G., “Normal” Thrombin Generation, Blood, 94, 7, 1999. Crossref
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Thiagarajan Perumal, Dannenbring Robert, Matsuura Kinji, Tramontano Alfonso, Gololobov Gennady, Paul Sudhir, Monoclonal Antibody Light Chain with Prothrombinase Activity, Biochemistry, 39, 21, 2000. Crossref
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Le Anhquyen, Dasgupta Swapan, Planque Stephanie, Paul Sudhir, Thiagarajan Perumal, Lupus-Derived Antiprothrombin Autoantibodies from a V Gene Phage Display Library Are Specific for the Kringle 2 Domain of Prothrombin, Biochemistry, 43, 13, 2004. Crossref
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Abrams Simon T., Su Dunhao, Sahraoui Yasmina, Lin Ziqi, Cheng Zhenxing, Nesbitt Kate, Alhamdi Yasir, Harrasser Micaela, Du Min, Foley Jonathan H., Lillicrap David, Wang Guozheng, Toh Cheng-Hock, Assembly of alternative prothrombinase by extracellular histones initiates and disseminates intravascular coagulation, Blood, 137, 1, 2021. Crossref
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Tarumi Takashi, Kravtsov Dmitri V., Zhao Mingming, Williams Scott M., Gailani David, Cloning and Characterization of the Human Factor XI Gene Promoter, Journal of Biological Chemistry, 277, 21, 2002. Crossref
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Smirnov Ivan V., Belogurov Alexey A., Kozyr Arina V., Gabibov Alexander, Catalytic Antibodies, in Enzyme Catalysis in Organic Synthesis, 2012. Crossref
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Tellez Carmen, Bar-Eli Menashe, Role and regulation of the thrombin receptor (PAR-1) in human melanoma, Oncogene, 22, 20, 2003. Crossref
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Bukys Michael A., Blum Melissa A., Kim Paul Y., Brufatto Nicole, Nesheim Michael E., Kalafatis Michael, Incorporation of Factor Va into Prothrombinase Is Required for Coordinated Cleavage of Prothrombin by Factor Xa, Journal of Biological Chemistry, 280, 29, 2005. Crossref