1,721,179 research outputs found
PICCI P, RUGGIERI P, FABBRI N, BIAGINI R, TELLA G, CASADEI R, FERRARO A, DE CRISTOFARO R
No full textL'embolizzazione arteriosa selettiva nel trattamento delle lesioni tumorali e pseudotumorali del rachide
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Molecular Modeling of Thrombin and its Natural Mutants: Implications in Biochemistry, Pathophysiology and Drug Design
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Effect of fibrinogen concentration and platelet count on the inhibition of platelet aggregation by glycoprotein IIb/IIIa inhibitors
No full textRe: Shapiro F, Zurakowski D, Sethna NF. Tranexamic acid diminishes intraoperative blood loss and transfusion in spinal fusion for Duchenne muscular dystrophy scoliosis.
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Evaluation of pathological fracture risk in the metastatic patient
No full textIn recent years attempts have been made to identify the clinical and radiographic parameters which would enable metastatic lesion involving the risk of fracture to be highlighted. A total of 258 cases of pathological fracture of the femur and humerus referred to the Tumour Centre of the Rizzoli Orthopedic Institute from 1950 to 1991 were examined in order to evaluate the efficacy of radiographic parameters which identify osteolysis with the risk of pathological fracture
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The Asp272-Glu282 Region of Platelet Glycoprotein Ib Interacts with the Heparin-binding Site of -Thrombin and Protects the Enzyme from the Heparin-catalyzed Inhibition by Antithrombin III
No full textPlatelet glycoprotein Ib (GpIb) mediates interaction with both von Willebrand factor and thrombin. Thrombin binds to GpIb via its heparin-binding site (HBS) (De Candia, E., De Cristofaro, R., De Marco, L., Mazzucato, M., Picozzi, M., and Landolfi, R. (1997) Thromb. Haemostasis 77, 735–740; De Cristofaro, R., De Candia, E., Croce, G., Morosetti, R., and Landolfi, R. (1998) Biochem. J. 332, 643–650). To identify the thrombin-binding domain on GpIbα, we examined the effect of GpIbα1–282, a GpIbα fragment released by the cobra venom mocarhagin on the heparin-catalyzed rate of thrombin inhibition by antithrombin III (AT). GpIbα1–282 inhibited the reaction in a dose-dependent and competitive fashion. In contrast, the GpIbα1–271 fragment, produced by exposing GpIbα1–282 to carboxypeptidase Y, had no effect on thrombin inhibition by the heparin-AT complex. Measurements of the apparent equilibrium constant of the GpIbα1–282 binding to thrombin as a function of different salts (NaCl and tetramethyl-ammonium chloride) concentration (0.1–0.2 M) indicated a large salt dependence (Γ± = −4.5), similar to that pertaining to the heparin binding to thrombin. The importance of thrombin HBS in its interaction with GpIbα was confirmed using DNA aptamers, which specifically bind to either HBS (HD22) or the fibrinogen recognition site of thrombin (HD1). HD22, but not HD1, inhibited thrombin binding to GpIbα1–282. Furthermore, the proteolytic derivative γT-thrombin, which lacks the fibrinogen recognition site, binds to GpIbα via its intact HBS in a reaction that is inhibited by HD22. Neither α- nor γT-thrombin bound to GpIbα1–271, suggesting that the Asp272–Glu282 region of GpIbα may act as a “heparin-like” ligand for the thrombin HBS, thereby inhibiting heparin binding to thrombin. It was also demonstrated that intact platelets may dose-dependently inhibit the heparin-catalyzed thrombin inhibition by AT at enzyme concentrations <5 nM. Altogether, these findings show that thrombin HBS binds to the region of GpIbα involving the Asp272–Glu282 segment, protecting the enzyme from the inactivation by the heparin-AT system
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