In too deep: understanding, detecting and managing DVT
School of Nursing and Midwifery, University of Salford.British journal of nursing (Mark Allen Publishing) 09/2010; 19(16):1021-7. DOI: 10.12968/bjon.2010.19.16.78188
Venous thromboembolism (VTE), which includes deep vein thrombosis (DVT) and pulmonary embolism (PE), is a serious health and social care problem of the developed world, affecting 1 in 1000 adults every year, and with an annual financial overhead of approximately £640 million. The nature of DVT means that often the condition can go unrecognized until the thrombus becomes an embolus. The pathogenesis of DVT continues to be based on Virchow's triad, which attributes VTE to 'hypercoagulability', 'stasis' and 'intimal injury'. The diagnosis of DVT is often the result of a number of tests performed either sequentially or in combination before mechanical and/or chemical treatment is embarked on. Creating public awareness of DVT and PE is the best way to prevent this condition. Nurses are in an ideal position to discuss the importance of lifestyle changes and other related measures to prevent DVT.
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ABSTRACT: Thromboembolic disorders are the leading cause of human mortality. Therefore, development of effective anticoagulant therapy is critical. Factor XIIIA (FXIIIA) protein is a crucial factor in the blood coagulation cascade, and hence it is a vital target for evolution of new antithrombotic agents. Structure-function studies of clotting factor active sites, clot formation, and thrombus structure have gained prominence in the efforts to develop novel anticoagulants. Factor XIIIA was homology modelled with the human transglutaminase-2 crystal structure as a base template for BLAST analysis. Docking and comparative binding site analysis revealed active site residue conservation and inhibitor-protein interactions. Nineteen small molecules possessing suspected anticoagulant properties were successfully docked into the FXIIIA active site following the best CoMFA and CoMSIA prediction values. Dabigatran etexilate was anticipated to be the best FXIIIA inhibitor among the nineteen anticoagulants with the highest binding affinity for the FXIIIA protein and the highest FlexX dock score of -29.8 KJ/mol. Structural properties of FXIIIA inhibitors with increased antithrombotic activity were predicted by this docking study
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