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82. Thrombin generation and platelet activation related to subintimal percutaneous transluminal angioplasty.

Author

Jenssen, Erik Krag, Brosstad, Frank, Pedersen, Turid, Bjørnsen, Stine, Jørgensen, Jørgen J, and Sandbæk, Gunnar

Subjects
*BLOOD platelet activation, *THROMBIN, *TRANSLUMINAL angioplasty, *BLOOD coagulation, *FLOW cytometry, *FIBRINOGEN, *IMMUNOASSAY, *BLOOD testing
Abstract

Objective: The purpose of this study was to measure the in vivo platelet activation and thrombin generation in arterial blood after passing a subintimal conduit. Methods: Subintimal percutaneous transluminal angioplasty (SPTA) is a technique where a subintimal channel is created, allowing recanalization of long peripheral arterial occlusion. From 10 patients with intermittent claudication, undergoing successful SPTA for femoropopliteal occlusive disease, we collected antecubital venous blood samples immediately before treatment, preprocedural arterial blood samples taken at the entry level proximal to the vessel occlusion, and subsequently at the reentry level after successful recanalization. Venous follow-up blood samples were taken after 24 hours. Plasma concentrations of β-thromboglobulin (β-TG), RANTES, and Prothrombin fragment (F1 ++ 2), were determined by immunoassay. Fibrinogen binding to platelets, leukocyte-platelet adhesion, and P-selectin were determined by flow cytometry. Results: We found a statistically significant transluminal increase in the plasma concentrations of RANTES, β-TG and F1 ++ 2 ( p == 0.002, 0.001 and 0.001 respectively), which all normalized within 24 hours. Platelet-leukocyte aggregates significantly decreased after 24 hours compared with preprocedural and preentry levels (3.26% versus 5.26 %, p == 0.017). P-selectin expression on circulating platelets was statistically significantly increased in the blood sample taken at the re-entry level compared with the pre-procedural and pre-entry level ( p == 0.007). After 24 hours there was no statistically significant difference to pre-procedural levels. There was no significant change in platelet fibrinogen binding at any levels. Conclusion: When passing a subintimal conduit, in vivo sampled blood demonstrated an extremely rapid and substantial uniform platelet activation and thrombin generation. [ABSTRACT FROM AUTHOR]

Published
2012
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86. Tranexamic Acid Given into the Wound Reduces Postoperative Blood Loss by Half Orthopaedic Surgery.

Author

Krohn, Claus Danckert, Sørensen, Roger, Lange, Johan Emil, Riise, Rolf, Bjørnsen, Stine, and Brosstad, Frank

Subjects
ACIDS, BLOOD, WOUNDS & injuries, ORTHOPEDIC surgery, PLASMIN, DIMERS, FIBRINOLYSIS
Abstract

Objective: To evaluate the effect of locally applied tranexamic acid on postoperative blood loss and measures of fibrinolysis in drained blood. Design: Prospective study. Setting: University hospital, Norway. Patients: 30 patients operated on for low back pain by screw fixation of the lumbar spine, 16 of who were randomised to be given topical tranexamic acid. Main outcome measures: Postoperative blood loss after 18 hours. Concentrations of plasmin/α2-antiplasmin (PAP) and D-dimer in arterial and drained blood at the time of would closure and in drained blood after 1 hour. Results: In the tranexamic group median (interquartile) blood loss was reduced by half from 525 (325-750) ml to 252 (127-465) ml, p = 0.02. In drained blood after one hour the increase in the concentration of pap was 150 (109-170)% and D-dimer 150 (107-272)% in the tranexamic group compared with the control group where the increase in PAP was 320 (140-540)% and D-dimer 260 (161-670)%. Conclusion: Tranexamic acid applied in the wound inhibits blood loss by up to a half in major orthopaedic surgery probably because it prevents excessive fibrinolysis. [ABSTRACT FROM AUTHOR]

Published
2002

87. Fibrinolytic Activity and Postoperative Salvaged Untreated Blood for Autologous Transfusion in Major Orthopaedic Surgery.

Author

Krohn, Claus Danckert, Reikerås, Olav, Bjornsen, Stine, and Brosstad, Frank

Subjects
FIBRINOLYSIS, AUTOTRANSFUSION of blood
Abstract

Objective: To evaluate the fibrinolytic activity in a closed surgical wound, in postoperatively drained blood, and during autologous transfusion. Design: Prospective study. Setting: National hospital, Norway. Patients: 9 patients operated on for thoracic scoliosis. Main outcome measure: Concentrations of plasmin/antiplasmin (PAP), α[sub 2]-antiplasmin, and D-dimers in drained, arterial, and mixed venous blood before, during, and after infusion of 10 ml/kg body weight of postoperatively drained, untreated blood. Results: In drained blood the concentration of α[sub 2]-antiplasmin was 31% of the preoperative arterial control value. Together with the increased concentrations of PAP to 18076 μg/L and D-dimers to 126 mg/L, this indicates extensive fibrinolytic activity in the closed wound. The postoperative autologous transfusion of drained, untreated blood increased the concentration of PAP from 507 to 2453 μg/L and of D-dimer from 0.7 mg/L to 15.3 mg/L in systemic blood. Conclusion: The systemic concentration of fibrin(ogen) degradation products, indicated by D-dimers, after recirculation of drained, untreated blood might impair coagulation. The extensive activation of plasmin might exhaust available α[sub 2]-antiplasmin in the wound and result in postoperative rebleeding. [ABSTRACT FROM AUTHOR]

Published
2001
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90. Common Structural Genes for Platelet and Plasma Fibrinogen

Author

Teige, Brita, Gogstad, Geir, Brosstad, Frank, and Olaisen, Bj⊘rnar

Abstract

Fibrinogen from plasma was compared with fibrinogen from platelets using two-dimensional electrophoresis. The source of platelet fibrinogen was isolated α-granules, thrombin- and collagen-released platelet material. The Bβ- and γ-chains from the different sources showed similar two-dimensional patterns, while γ'-chains were not observed in platelet fibrinogen preparations. Furthermore, the Aα-chain could hardly be identified in platelet preparations. When individual fibrinogen was studied in persons heterozygous for genetic Bβ- and γ-chain variants, the two-dimensional variant pattern could be demonstrated in plasma fibrinogen as well as in platelet fibrinogen. This observation strongly indicates that the structural genes for plasma and platelet fibrinogen Bβ- and γ-chains are identical.

Published
1985
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92. Fibrinogen-Binding Properties of the Human Platelet Glycoprotein IIb–IIIa Complex: A Study Using Crossed-Radioimmunoelectrophoresis

Author

Gogstad, Geir O., Brosstad, Frank, Krutnes, May-Britt, Hagen, Inger, and Solum, Nils Olav

Abstract

Fibrinogen-binding platelet proteins have been examined by crossed-immunoeloctrophoresis of solubilized, washed platelets followed by the incubation of the immunoplates with 125l-fibrinogen and exposure to x-ray films. Incubation with 0.1 mg/ml of 125l-fibrinogen revealed the binding of fibrinogen to the immunoprecipitates representing the glycoprotein IIb–IIIa complex, factor XIIIa chain, a granule membrane protein termed G4, fibrinogen, and albumin. Only the glycoprotein IIb–IIIa precipitate and the fibrinogen precipitate showed significant binding when the concentration of 125l-fibrinogen was lowered to 0.01 mg/ml. The binding to all the immunoprecipitates was completely abolished in the presence of a 20 fold excess of unlabeled fibrinogen, but not when unlabeled fibrinogen was replaced by the same amounts of bovine serum albumin or human hemoglobin. This indicates that the binding of fibrinogen is specific. Furthermore, 125l-fibronectin and 125l-thrombin did not bind to the glycoprotein IIb–IIIa precipitate. The binding of 125l-fibrinogen to the precipitates representing the glycoprotein IIb–IIIa complex, the factor XIIIa chain, and G4, but not to the albumin precipitate, was significantly lowered in the presence of EDTA. This effect of EDTA increased with increasing pH, with no binding at pH 8.7. Immunoprecipitates of dissociated glycoprotein lIb and IIIa did not bind 125l-fibrinogen. Binding of 125l-fibrinogen to the glycoprotein IIb–IIIa precipitate was dependent on the presence of either Ca2+or Mg2+, the binding to the factor XIIIa chain required Ca2+, and the binding to G4 required Mg2+. The results indicate that the glycoprotein IIb–IIIa complex, but not the separate glycoproteins IIb and IIIa, can act as Ca2+or Mg2+-dependent fibrinogen receptor, under proper physiologic conditions.

Published
1982
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