Journal articles: 'Ancrod'

1

Cole, C. Wm, and Ianis Bormanis. "ANCROD." Journal of Trauma: Injury, Infection, and Critical Care 35, no. 1 (July 1993): 175. http://dx.doi.org/10.1097/00005373-199307000-00095.

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2

Dempfle, Carl-Erik, Sotiria Argiriou, Klaus Kucher, H. Müller-Peltzer, Klaus Rübsamen, and Dieter L. Heene. "Analysis of fibrin formation and proteolysis during intravenous administration of ancrod." Blood 96, no. 8 (October 15, 2000): 2793–802. http://dx.doi.org/10.1182/blood.v96.8.2793.

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Abstract Ancrod is a purified fraction of venom from the Malayan pit viper, Calloselasma rhodostoma, currently under investigation for treatment of acute ischemic stroke. Treatment with ancrod leads to fibrinogen depletion. The present study investigated the mechanisms leading to the reduction of plasma fibrinogen concentration. Twelve healthy volunteers received an intravenous infusion of 0.17 U/kg body weight of ancrod for 6 hours. Blood samples were drawn and analyzed before and at various time points until 72 hours after start of infusion. Ancrod releases fibrinopeptide A from fibrinogen, leading to the formation of desAA-fibrin monomer. In addition, a considerable proportion of desA-profibrin is formed. Production of desA-profibrin is highest at low concentrations of ancrod, whereas desA-profibrin is rapidly converted to desAA-fibrin at higher concentrations of ancrod. Both desA-profibrin and desAA-fibrin monomers form fibrin complexes. A certain proportion of complexes carries exposed fibrin polymerization sites EA, indicating that the terminal component of the protofibril is a desAA-fibrin monomer unit. Soluble fibrin complexes potentiate tissue-type plasminogen activator-induced plasminogen activation. Significant amounts of plasmin are formed when soluble fibrin in plasma reaches a threshold concentration, leading to the proteolytic degradation of fibrinogen and fibrin. In the present setting, high concentrations of soluble fibrin are detected after 1 hour of ancrod infusion, whereas a rise in fibrinogen and fibrin degradation products, and plasmin-α2–plasmin inhibitor complex levels is first detected after 2 hours of ancrod infusion. Ancrod treatment also results in the appearance of cross-inked fibrin degradation productd-dimer in plasma.

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3

Dempfle, Carl-Erik, Sotiria Argiriou, Klaus Kucher, H. Müller-Peltzer, Klaus Rübsamen, and Dieter L. Heene. "Analysis of fibrin formation and proteolysis during intravenous administration of ancrod." Blood 96, no. 8 (October 15, 2000): 2793–802. http://dx.doi.org/10.1182/blood.v96.8.2793.h8002793_2793_2802.

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Ancrod is a purified fraction of venom from the Malayan pit viper, Calloselasma rhodostoma, currently under investigation for treatment of acute ischemic stroke. Treatment with ancrod leads to fibrinogen depletion. The present study investigated the mechanisms leading to the reduction of plasma fibrinogen concentration. Twelve healthy volunteers received an intravenous infusion of 0.17 U/kg body weight of ancrod for 6 hours. Blood samples were drawn and analyzed before and at various time points until 72 hours after start of infusion. Ancrod releases fibrinopeptide A from fibrinogen, leading to the formation of desAA-fibrin monomer. In addition, a considerable proportion of desA-profibrin is formed. Production of desA-profibrin is highest at low concentrations of ancrod, whereas desA-profibrin is rapidly converted to desAA-fibrin at higher concentrations of ancrod. Both desA-profibrin and desAA-fibrin monomers form fibrin complexes. A certain proportion of complexes carries exposed fibrin polymerization sites EA, indicating that the terminal component of the protofibril is a desAA-fibrin monomer unit. Soluble fibrin complexes potentiate tissue-type plasminogen activator-induced plasminogen activation. Significant amounts of plasmin are formed when soluble fibrin in plasma reaches a threshold concentration, leading to the proteolytic degradation of fibrinogen and fibrin. In the present setting, high concentrations of soluble fibrin are detected after 1 hour of ancrod infusion, whereas a rise in fibrinogen and fibrin degradation products, and plasmin-α2–plasmin inhibitor complex levels is first detected after 2 hours of ancrod infusion. Ancrod treatment also results in the appearance of cross-inked fibrin degradation productd-dimer in plasma.

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4

Demers, C., JS Ginsberg, P. Brill-Edwards, A. Panju, TE Warkentin, DR Anderson, C. Turner, and JG Kelton. "Rapid anticoagulation using ancrod for heparin-induced thrombocytopenia [see comments]." Blood 78, no. 9 (November 1, 1991): 2194–97. http://dx.doi.org/10.1182/blood.v78.9.2194.2194.

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Abstract In order to determine the efficacy and safety of ancrod, a rapid acting defibrinogenating drug, for patients with heparin-induced thrombocytopenia, 11 consecutive patients who required anticoagulant therapy because of venous thromboembolism and who developed acute heparin-induced thrombocytopenia or had a history of heparin-induced thrombocytopenia were treated with ancrod. Heparin therapy was discontinued (in patients receiving heparin) and ancrod started at a dose of 1 to 2 U/kg every 24 hours with subsequent daily doses adjusted to maintain fibrinogen levels between 0.5 and 1.0 g/L. Ancrod was continued until warfarin had become effective. The platelet count increased to more than 150 x 10(9)/L within 2 to 10 days in all thrombocytopenic patients. Two patients with a history of heparin- induced thrombocytopenia maintained normal platelet counts while receiving ancrod. Two patients had recurrent venous thrombosis while receiving warfarin, 10 days after ancrod was discontinued: one of these patients had metastatic pancreatic carcinoma and developed phlegmasia cerulea dolens and the other patient developed a venographically proven extension of her deep venous thrombosis. One patient suffered a bleeding episode into the thigh with a 16-g/L decrease in her hemoglobin level while receiving ancrod therapy. No other side effects were noted. Our experience indicates that ancrod therapy is a reasonable approach for patients with heparin-induced thrombocytopenia who require anticoagulant therapy.

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5

Demers, C., JS Ginsberg, P. Brill-Edwards, A. Panju, TE Warkentin, DR Anderson, C. Turner, and JG Kelton. "Rapid anticoagulation using ancrod for heparin-induced thrombocytopenia [see comments]." Blood 78, no. 9 (November 1, 1991): 2194–97. http://dx.doi.org/10.1182/blood.v78.9.2194.bloodjournal7892194.

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In order to determine the efficacy and safety of ancrod, a rapid acting defibrinogenating drug, for patients with heparin-induced thrombocytopenia, 11 consecutive patients who required anticoagulant therapy because of venous thromboembolism and who developed acute heparin-induced thrombocytopenia or had a history of heparin-induced thrombocytopenia were treated with ancrod. Heparin therapy was discontinued (in patients receiving heparin) and ancrod started at a dose of 1 to 2 U/kg every 24 hours with subsequent daily doses adjusted to maintain fibrinogen levels between 0.5 and 1.0 g/L. Ancrod was continued until warfarin had become effective. The platelet count increased to more than 150 x 10(9)/L within 2 to 10 days in all thrombocytopenic patients. Two patients with a history of heparin- induced thrombocytopenia maintained normal platelet counts while receiving ancrod. Two patients had recurrent venous thrombosis while receiving warfarin, 10 days after ancrod was discontinued: one of these patients had metastatic pancreatic carcinoma and developed phlegmasia cerulea dolens and the other patient developed a venographically proven extension of her deep venous thrombosis. One patient suffered a bleeding episode into the thigh with a 16-g/L decrease in her hemoglobin level while receiving ancrod therapy. No other side effects were noted. Our experience indicates that ancrod therapy is a reasonable approach for patients with heparin-induced thrombocytopenia who require anticoagulant therapy.

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6

Wiles, P. G., S. R. Nelson, K. K. Hampton, B. Casali, M. Boothby, and C. R. M. Prentice. "Therapeutic defibrinogenation by ancrod." Blood Coagulation & Fibrinolysis 1, no. 5 (October 1990): 385–88. http://dx.doi.org/10.1097/00001721-199010000-00005.

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7

Liu, Shuo, Victor J. Marder, David E. Levy, Shur-Jen Wang, Fan Yang, Annlia Paganini-Hill, and Mark J. Fisher. "Ancrod and Fibrin Formation." Stroke 42, no. 11 (November 2011): 3277–80. http://dx.doi.org/10.1161/strokeaha.111.622753.

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8

Soutar, R. L., and J. S. Ginsberg. "Anticoagulant therapy with ancrod." Critical Reviews in Oncology/Hematology 15, no. 1 (August 1993): 23–33. http://dx.doi.org/10.1016/1040-8428(93)90018-y.

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9

Krishnamurti, C., C. Bolan, CA Colleton, TM Reilly, and BM Alving. "Role of plasminogen activator inhibitor-1 in promoting fibrin deposition in rabbits infused with ancrod or thrombin." Blood 82, no. 12 (December 15, 1993): 3631–36. http://dx.doi.org/10.1182/blood.v82.12.3631.3631.

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Abstract The role of defective fibrinolysis caused by elevated activity of plasminogen activator inhibitor-1 (PAI-1) in promoting fibrin deposition in vivo has not been well established. The present study compared the efficacy of thrombin or ancrod, a venom-derived enzyme that clots fibrinogen, to induce fibrin formation in rabbits with elevated PAI-1 levels. One set of male New Zealand rabbits received intravenous endotoxin to increase endogenous PAI-1 activity followed by a 1-hour infusion of ancrod or thrombin; another set of normal rabbits received intravenous human recombinant PAI-1 (rPAI-1) during an infusion of ancrod or thrombin. Thirty minutes after the end of the infusion, renal fibrin deposition was assessed by histopathology. Animals receiving endotoxin, rPAI-1, ancrod, or thrombin alone did not develop renal thrombi. All endotoxin-treated rabbits developed fibrin deposition when infused with ancrod (n = 4) or thrombin (n = 6). Fibrin deposition occurred in 7 of 7 rabbits receiving both rPAI-1 and ancrod and in only 1 of 6 receiving rPAI-1 and thrombin (P “ .01). In vitro, thrombin but not ancrod was inactivated by normal rabbit plasma and by purified antithrombin III or thrombomodulin. The data indicate that elevated levels of PAI-1 promote fibrin deposition in rabbits infused with ancrod but not with thrombin. In endotoxin-treated rabbits, fibrin deposition that occurs with thrombin infusion may be caused by decreased inhibition of procoagulant activity and not increased PAI-1 activity.

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10

Krishnamurti, C., C. Bolan, CA Colleton, TM Reilly, and BM Alving. "Role of plasminogen activator inhibitor-1 in promoting fibrin deposition in rabbits infused with ancrod or thrombin." Blood 82, no. 12 (December 15, 1993): 3631–36. http://dx.doi.org/10.1182/blood.v82.12.3631.bloodjournal82123631.

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The role of defective fibrinolysis caused by elevated activity of plasminogen activator inhibitor-1 (PAI-1) in promoting fibrin deposition in vivo has not been well established. The present study compared the efficacy of thrombin or ancrod, a venom-derived enzyme that clots fibrinogen, to induce fibrin formation in rabbits with elevated PAI-1 levels. One set of male New Zealand rabbits received intravenous endotoxin to increase endogenous PAI-1 activity followed by a 1-hour infusion of ancrod or thrombin; another set of normal rabbits received intravenous human recombinant PAI-1 (rPAI-1) during an infusion of ancrod or thrombin. Thirty minutes after the end of the infusion, renal fibrin deposition was assessed by histopathology. Animals receiving endotoxin, rPAI-1, ancrod, or thrombin alone did not develop renal thrombi. All endotoxin-treated rabbits developed fibrin deposition when infused with ancrod (n = 4) or thrombin (n = 6). Fibrin deposition occurred in 7 of 7 rabbits receiving both rPAI-1 and ancrod and in only 1 of 6 receiving rPAI-1 and thrombin (P “ .01). In vitro, thrombin but not ancrod was inactivated by normal rabbit plasma and by purified antithrombin III or thrombomodulin. The data indicate that elevated levels of PAI-1 promote fibrin deposition in rabbits infused with ancrod but not with thrombin. In endotoxin-treated rabbits, fibrin deposition that occurs with thrombin infusion may be caused by decreased inhibition of procoagulant activity and not increased PAI-1 activity.

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11

Levy, David E., Gregory J. del Zoppo, Bart M. Demaerschalk, Andrew M. Demchuk, Hans-Christoph Diener, George Howard, Markku Kaste, et al. "Ancrod in Acute Ischemic Stroke." Stroke 40, no. 12 (December 2009): 3796–803. http://dx.doi.org/10.1161/strokeaha.109.565119.

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12

O-Yurvati, Albert H., Glenn W. Laub, Theodore J. Southgate, and Lynn B. McGrath. "Heparinless cardiopulmonary bypass with ancrod." Annals of Thoracic Surgery 57, no. 6 (June 1994): 1656–58. http://dx.doi.org/10.1016/0003-4975(94)90148-1.

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13

Cole, C. William, and Janis Bormanis. "Ancrod: A practical alternative to heparin." Journal of Vascular Surgery 8, no. 1 (July 1988): 59–63. http://dx.doi.org/10.1067/mva.1988.avs0080059.

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14

Cole, C. William, and Janis Bormanis. "Ancrod: A practical alternative to heparin." Journal of Vascular Surgery 8, no. 1 (July 1988): 59–63. http://dx.doi.org/10.1016/0741-5214(88)90245-5.

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15

Au, L. C., S. B. Lin, J. S. Chou, G. W. Teh, K. J. Chang, and C. M. Shih. "Molecular cloning and sequence analysis of the cDNA for ancrod, a thrombin-like enzyme from the venom of Calloselasma rhodostoma." Biochemical Journal 294, no. 2 (September 1, 1993): 387–90. http://dx.doi.org/10.1042/bj2940387.

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The 1.54 kb cDNA for ancrod, a thrombin-like enzyme, was cloned from a lambda ZAP cDNA library derived from the venom glands of Calloselasma (Agkistrodon) rhodostoma. The cDNA sequence reveals that ancrod is synthesized as a pre-zymogen of 258 amino acids, including a putative secretory peptide of 18 amino acids and a proposed zymogen peptide of 6 amino-acid residues. The amino-acid sequence of the predicted active form of the enzyme exhibits a high degree of sequence similarity to those of mammalian serine proteases (trypsin and pancreatic kallikrein) and other thrombin-like enzymes (batroxobin and flavoxobin). Key amino-acid residues (His43, Asp88, Ser182 and Asp176) that are thought to be involved in the substrate cleavage and in the substrate-binding reaction are conserved. Ancrod contains 13 cysteine residues. Based on alignment with the amino-acid sequences of trypsin and batroxobin, six disulphide bridges can be predicted to be present in the ancrod protein. The existence of a free cysteine, which changes the common sequence surrounding the Ser182 active site from Gly-Asp-Ser-Gly-Gly-Pro to Cys-Asp-Ser-Gly-Gly-Pro, is unusual for a serine protease.

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16

Levy, David E., James Trammel, and Warren W. Wasiewski. "Ancrod for Acute Ischemic Stroke: A New Dosing Regimen Derived from Analysis of Prior Ancrod Stroke Studies." Journal of Stroke and Cerebrovascular Diseases 18, no. 1 (January 2009): 23–27. http://dx.doi.org/10.1016/j.jstrokecerebrovasdis.2008.07.009.

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17

Krishnamurti, C., CF Barr, MA Hassett, GD Young, and BM Alving. "Plasminogen activator inhibitor: a regulator of ancrod-induced fibrin deposition in rabbits." Blood 69, no. 3 (March 1, 1987): 798–803. http://dx.doi.org/10.1182/blood.v69.3.798.798.

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Abstract Plasma levels of a fast-acting plasminogen activator inhibitor (PAI), which neutralizes both tissue plasminogen activator (t-PA) and urokinase, are markedly increased in endotoxin-treated rabbits. The ability of this inhibitor to prevent the fibrinolysis that occurs after a thrombogenic stimulus was investigated in a rabbit model. Normal and endotoxin-treated male New Zealand rabbits were infused with ancrod, an enzyme that causes noncrosslinked fibrin formation in vivo. Ancrod stimulated t-PA activity by 90% in normal rabbits and caused hypofibrinogenemia but did not increase PAI levels or induce fibrin deposition in target organs. Rabbits injected with endotoxin (10 micrograms/kg) showed an increase in PAI from less than 1 to 32 U/mL 4 hours later. When ancrod was infused at this time, 90% of the rabbits developed renal fibrin thrombi. Fibrin deposition was recorded in 40% of the rabbits that received a lower dose of endotoxin (1.0 microgram/kg) and had a PAI level of 14 U/ml at the time of ancrod infusion 4 hours later. Fibrin deposition did not occur in the endotoxin-treated rabbits that received normal saline. These data suggest that high levels of PAI inhibit fibrinolysis in vivo, thereby promoting fibrin clot deposition following a thrombogenic stimulus.

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18

Krishnamurti, C., CF Barr, MA Hassett, GD Young, and BM Alving. "Plasminogen activator inhibitor: a regulator of ancrod-induced fibrin deposition in rabbits." Blood 69, no. 3 (March 1, 1987): 798–803. http://dx.doi.org/10.1182/blood.v69.3.798.bloodjournal693798.

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Plasma levels of a fast-acting plasminogen activator inhibitor (PAI), which neutralizes both tissue plasminogen activator (t-PA) and urokinase, are markedly increased in endotoxin-treated rabbits. The ability of this inhibitor to prevent the fibrinolysis that occurs after a thrombogenic stimulus was investigated in a rabbit model. Normal and endotoxin-treated male New Zealand rabbits were infused with ancrod, an enzyme that causes noncrosslinked fibrin formation in vivo. Ancrod stimulated t-PA activity by 90% in normal rabbits and caused hypofibrinogenemia but did not increase PAI levels or induce fibrin deposition in target organs. Rabbits injected with endotoxin (10 micrograms/kg) showed an increase in PAI from less than 1 to 32 U/mL 4 hours later. When ancrod was infused at this time, 90% of the rabbits developed renal fibrin thrombi. Fibrin deposition was recorded in 40% of the rabbits that received a lower dose of endotoxin (1.0 microgram/kg) and had a PAI level of 14 U/ml at the time of ancrod infusion 4 hours later. Fibrin deposition did not occur in the endotoxin-treated rabbits that received normal saline. These data suggest that high levels of PAI inhibit fibrinolysis in vivo, thereby promoting fibrin clot deposition following a thrombogenic stimulus.

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19

O[apos ]Donnell, Thomas F., Julie A. Freischlag, Michael D. Colburn, and William J. Qui[ntilde]ones-Baldrich. "Heparin, urokinase, and ancrod alter neutrophil function." Journal of Vascular Surgery 16, no. 4 (October 1992): 0565–74. http://dx.doi.org/10.1067/mva.1992.39288.

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20

Orbach, Darren. "Outcomes of Ancrod in Acute Ischemic Stroke." JAMA 284, no. 15 (October 18, 2000): 1926. http://dx.doi.org/10.1001/jama.284.15.1921.

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21

DEMPFLE, CARL-ERIK, SOTIRIA ARGIRIOU, SONJA ALESCI, KLAUS KUCHER, H. MÜLLER-PELTZER, KLAUS RÜBSAMEN, and DIETER L. HEENE. "Fibrin Formation and Proteolysis during Ancrod Treatment." Annals of the New York Academy of Sciences 936, no. 1 (January 25, 2006): 210–14. http://dx.doi.org/10.1111/j.1749-6632.2001.tb03507.x.

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22

Freischlag, Julie A., Michael D. Colburn, William J. Quiñones-Baldrich, and Wesley S. Moore. "Heparin, urokinase, and ancrod alter neutrophil function." Journal of Vascular Surgery 16, no. 4 (October 1992): 565–74. http://dx.doi.org/10.1016/0741-5214(92)90164-4.

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23

G. Kelton, J. W. Smith, D. Moffatt,, J. "The interaction of ancrod with human platelets." Platelets 10, no. 1 (January 1999): 24–29. http://dx.doi.org/10.1080/09537109976310.

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24

Hennerici, Michael G., Richard Kay, Julien Bogousslavsky, Gian Luigi Lenzi, Marc Verstraete, and Jean Marc Orgogozo. "Intravenous ancrod for acute ischaemic stroke in the European Stroke Treatment with Ancrod Trial: a randomised controlled trial." Lancet 368, no. 9550 (November 2006): 1871–78. http://dx.doi.org/10.1016/s0140-6736(06)69776-6.

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25

PhD, Gregory P. Samsa, David B. Matchar MD, G. Rhys Williams ScD, and David E. Levy MD. "Cost-effectiveness of ancrod treatment of acute ischaemic stroke: results from the Stroke Treatment with Ancrod Trial (STAT)." Journal of Evaluation in Clinical Practice 8, no. 1 (February 2002): 61–70. http://dx.doi.org/10.1046/j.1365-2753.2002.00315.x.

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26

Smith, Reginald E., Gary E. Townsend, Brian R. Berry, and Tom Bowen. "Enoxaparin for Unstable Angina and Ancrod for Cardiac Surgery following Heparin Allergy." Annals of Pharmacotherapy 30, no. 5 (May 1996): 476–80. http://dx.doi.org/10.1177/106002809603000508.

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OBJECTIVE: To describe a patient who presented with heparin allergy and required alternate anticoagulation for unstable angina and coronary artery bypass surgery. To review therapeutic alternatives to porcine heparin for patients with hypersensitivity or intolerance to standard heparin anticoagulation. CASE SUMMARY: A 74-year-old man with a 15-year-old coronary artery bypass graft presented to the emergency room with unstable angina and was scheduled for urgent coronary artery revascularization. A bolus dose of porcine heparin was administered followed by a continuous infusion. Shortly afterward the patient developed a type I allergic reaction to the porcine heparin that was confirmed by rechallenge. Three alternatives to porcine heparin were tried, including bovine lung heparin, low-molecular-weight heparin (enoxaparin), and ancrod. The patient was found to be cross-sensitive to bovine lung heparin, but tolerated enoxaparin for unstable angina without cross-sensitivity. Anticoagulation for cardiopulmonary bypass was achieved with an infusion of ancrod that was later reversed with cryoprecipitate. The patient was discharged postoperatively on day 5 without the complication of excessive bleeding. DISCUSSION: Type I allergic reaction to unfractionated heparin is a rare occurrence and could be the result of a variety of factors. Possible causes for the reaction include a porcine protein, a preservative contained in the heparin solution, or a hapten formed between heparin and a plasma protein. We considered four alternatives to heparin anticoagulation: rush desensitization, bovine lung heparin, low-molecular-weight heparin, and ancrod. The patient was cross-sensitive to bovine lung heparin, but was able to tolerate low-molecular-weight heparin (enoxaparin). This was unexpected because enoxaparin is derived from unfractionated porcine heparin. Testing for cross-sensitivity had no value in this case, as two negative subcutaneous test doses were followed by dramatic reactions when the drugs were given intravenously. Although enoxaparin has been used for anticoagulation during bypass surgery, there is more experience with ancrod as an alternative to heparin. Repeat bypass surgery, which normally results in above-average blood loss, was successfully performed with a very low fibrinogen concentration (<0.15 g/L) during ancrod anticoagulation. CONCLUSIONS: We conclude that ancrod was a safe and effective alternative to heparin for coronary artery bypass surgery in this patient in whom a heparin product had caused a hypersensitivity reaction. We discovered on two occasions that a negative subcutaneous test dose for heparin allergy did not predict a severe type I allergic reaction when the heparin was later administered intravenously. Furthermore, we found that a low-molecular-weight heparin administered subcutaneously for a short period of time did not cause cross-sensitivity in a patient with a type I allergy to unfractionated heparin.

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27

Barbanti, Miriam, Fiorella Calanni, Egidio Marchi, Nicola Semeraro, and Mario Colucci. "Desmin 370, a Low Molecular Weight Dermatan Sulfate, Reduces the Weight of Preformed Thrombi in Rats Made Afibrinogenemic by Ancrod." Thrombosis and Haemostasis 73, no. 02 (1995): 287–90. http://dx.doi.org/10.1055/s-0038-1653766.

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SummaryDesmin 370 (D370), a low molecular weight dermatan sulfate, has been shown to induce a marked reduction of the weight of preformed venous thrombi in rats and rabbits by mechanisms that appeared largely independent of inhibition of thrombus accretion. In order to provide further support for such a mechanism, we exploited the defibrinating capacity of ancrod to obtain a thrombosis model characterized by the lack of thrombus growth and thus sensitive only to agents promoting thrombus lysis. Thrombus formation in anesthetized rats was induced by vena cava ligature. Injection of ancrod (5 U/kg) 5 h after induction of venous stasis caused a more than 95% reduction in plasma fibrinogen and prevented thrombus accretion as indicated by the lack of thrombus weight increase during the 3h experimental period (12.2 ° 0.6 vs 14.5 ° 1 as compared to 12.6 ° 0.6 vs 19.6 ° 0.8, p <0.01, in control rats) and by the almost complete (>90%) inhibition of125I- fibrin(ogen) binding to thrombi. Moreover, when ancrod was given 1 h before vena cava ligature, no thrombi were formed within 2 h whereas at the same time interval visible thrombi were present in all control rats. Administration of D370 (10 mg/kg) to thrombus bearing rats, 1 h after induction of afibrinogenemia, resulted in a significant reduction in thrombus weight (43% after 2h, p <0.01) which was only slightly lower than that recorded in normofibrinogenemic rats (54%). Enhancement of plasma fibrinolytic activity by ancrod had no influence on thrombus lysis and was not at all affected by administration of D370. These data provide additional and more direct evidence that D370 may promote thrombus lysis independently of inhibition of thrombus accretion.

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28

Atkinson, Richard P. "Ancrod in the Treatment of Acute Ischaemic Stroke." Drugs 54, Supplement 3 (1997): 100–108. http://dx.doi.org/10.2165/00003495-199700543-00014.

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29

de Vries, H. R. "Intraveneus ancrod voor de behandeling van acute hersentrombose." Medisch Farmaceutische Mededelingen 45, no. 5 (May 2007): 130–31. http://dx.doi.org/10.1007/bf03058983.

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30

Cole, Edward H., Michael F. X. Glynn, Carl A. Laskin, Joan Sweet, Nancy Mason, and Gary A. Levy. "Ancrod improves survival in murine systemic lupus erythematosus." Kidney International 37, no. 1 (January 1990): 29–35. http://dx.doi.org/10.1038/ki.1990.4.

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31

Atkinson, Richard P. "Ancrod in the Treatment of Acute Ischemic Stroke." Cerebrovascular Diseases 8, Suppl. 1 (1998): 23–28. http://dx.doi.org/10.1159/000047500.

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32

Cole, C. Wm. "Controlling Acute Elevation of Plasma Fibrinogen with Ancrod." Cerebrovascular Diseases 8, Suppl. 1 (1998): 29–34. http://dx.doi.org/10.1159/000047501.

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33

Nuber, R. "Clinical Experience with Ancrod in Acute Ischaemic Stroke." Cerebrovascular Diseases 10, no. 4 (2000): 27–29. http://dx.doi.org/10.1159/000047590.

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34

Soutar, R. L., and J. S. Ginsberg. "Uses of heparin. Ancrod for heparin induced thrombocytopenia." BMJ 306, no. 6889 (May 22, 1993): 1410. http://dx.doi.org/10.1136/bmj.306.6889.1410-a.

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35

EHRLICH, H. PAUL, WENDY L. McGRANE, and JOSEPH B. M. RAJARATNAM. "Ancrod Prevents Vascular Occlusion in Thermally Injured Rats." Journal of Trauma: Injury, Infection, and Critical Care 27, no. 4 (April 1987): 420–24. http://dx.doi.org/10.1097/00005373-198704000-00014.

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36

Sherman, David G., Richard P. Atkinson, Thomas Chippendale, Kenneth A. Levin, Ken Ng, Nancy Futrell, Chung Y. Hsu, David E. Levy, and for the STAT Participants. "Intravenous Ancrod for Treatment of Acute Ischemic Stroke." JAMA 283, no. 18 (May 10, 2000): 2395. http://dx.doi.org/10.1001/jama.283.18.2395.

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37

Mayberg, Marc R. "Ancrod—Is Snake Venom an Antidote for Stroke?" JAMA 283, no. 18 (May 10, 2000): 2440. http://dx.doi.org/10.1001/jama.283.18.2440.

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38

Rübsamen, K., W. Hornberger, and M. Kirchengast. "Inhibition of Arterial Thrombus Formation in Two Canine Models: Comparison of Ancrod, a Fibrinogen-Depleting Agent, the Thrombin-Inhibitor r-Hirudin, and the Glycoprotein IIb/IIIa-Receptor Antagonist Ro 43-8857." Thrombosis and Haemostasis 74, no. 05 (1995): 1353–60. http://dx.doi.org/10.1055/s-0038-1649939.

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SummaryInhibition of arterial thrombus formation by ancrod, a fibrinogen depleting agent isolated from a snake venom, r-hirudin, an inhibitor of thrombin-mediated fibrinogen cleavage, or the glycoprotein (GP)IIb/IIIa-receptor antagonist Ro 43-8857 interfering with fibrinogen binding to platelets, was evaluated in two canine models. As a marker of platelet-dependent thrombus formation, cyclic blood flow reductions (CFR) were induced in the left coronary artery (LAD) of mongrel dogs by mechanical injury of the endothelium combined with critical stenosis. In the second model CFRs were induced by thrombolysis of a copper coil-induced thrombus in the carotid artery. Blood flow rate during the reocclusion phase was used as an additional parameter of efficacy.The frequency of CFRs used as indicator of platelet aggregation and adhesion was significantly diminished by all treatments in both the carotid artery- and the LAD-model. In the LAD-model, following ancrod treatment, CFRs were correlated with plasma fibrinogen concentrations. Carotid artery blood flow after reperfusion, used as indicator of occlusive thrombus formation, rapidly declined to zero in the control group but remained at a high level after treatment with ancrod or r-hirudin. Ro 43-8857 at the selected dose improved blood flow rate only to a minor degree but prolonged the bleeding time from a mean value of 87.2 ± 10.9 s (n = 24) to values >300 s in 50% of the animals.Our results indicate that CFRs as indicator of platelet aggregation and adhesion are inhibited by either treatments. Blood flow as indicator of occlusive thrombus formation, however, is effectively improved by ancrod and r-hirudin only. Inhibition of fibrinogen binding to platelet GPIIb/IIIa receptors alone was found to be a less potent antithrombotic principle in this model.

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39

&NA;. "Ancrod ready for phase III trials after few adjustments." Reactions Weekly &NA;, no. 1222 (October 2008): 4. http://dx.doi.org/10.2165/00128415-200812220-00008.

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40

Gusberg, Richard Jefferson, C. William Cole, Janis William Bormanis, Gregory K. Luna, George K. Hajjar, Graeme G. Barber, and Kenneth A. Harris. "Ancrod versus heparin for anticoagulation during vascular surgical procedures." Journal of Vascular Surgery 17, no. 2 (February 1993): 288–93. http://dx.doi.org/10.1067/mva.1993.42069.

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41

Jahnke, Heidi. "Experimental Ancrod (Arvin) for Acute Ischemic Stroke: Nursing Implications." Journal of Neuroscience Nursing 23, no. 6 (December 1991): 386–89. http://dx.doi.org/10.1097/01376517-199112000-00008.

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42

Moore, G. K., and C. W. Cummings. "The Effect of Ancrod on Perfusion of Myocutaneous Flaps." Archives of Otolaryngology - Head and Neck Surgery 114, no. 10 (October 1, 1988): 1175–77. http://dx.doi.org/10.1001/archotol.1988.01860220109034.

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43

Cole, C. William, Janis Bormanis, Gregory K. Luna, George Hajjar, Graeme G. Barber, Kenneth A. Harris, and William F. Brien. "Ancrod versus heparin for anticoagulation during vascular surgical procedures." Journal of Vascular Surgery 17, no. 2 (February 1993): 288–93. http://dx.doi.org/10.1016/0741-5214(93)90414-h.

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44

Cercek, B., A. S. Lew, H. Hod, J. Yano, B. Lewis, K. N. N. Reddy, and W. Ganz. "Ancrod enhances the thrombolytic effect of streptokinase and urokinase." Thrombosis Research 47, no. 4 (August 1987): 417–26. http://dx.doi.org/10.1016/0049-3848(87)90457-9.

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Pollak, Victor E., Pia Glas-Greenwalt, Charles P. Olinger, Nand K. Wadhwa, and Steven A. Myre. "Ancrod Causes Rapid Thrombolysis in Patients with Acute Stroke." American Journal of the Medical Sciences 299, no. 5 (May 1990): 319–25. http://dx.doi.org/10.1097/00000441-199005000-00006.

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46

Benavente, Oscar, and David G. Sherman. "Therapeutic Potential of Ancrod in the Management of Cerebrovascular Disorders." CNS Drugs 9, no. 5 (1998): 341–46. http://dx.doi.org/10.2165/00023210-199809050-00001.

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Olinger, Charles P., Thomas G. Brott, William G. Barsan, Jerris R. Hedges, Pia Glas-Greenwalt, Victor E. Pollak, Judith Spilker, and Robert Eberle. "Use of ancrod in acute or progressing ischemic cerebral infarction." Annals of Emergency Medicine 17, no. 11 (November 1988): 1208–9. http://dx.doi.org/10.1016/s0196-0644(88)80071-4.

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Dempfle, C. E., S. Argirion, A. Keller, K. R??bsamen, K. Kucher, H. M??ller-Peltzer, and D. L. Heene. "91. Impact of ancrod treatment on measurement of plasma fibrinogen." Blood Coagulation & Fibrinolysis 9, no. 7 (October 1998): 713. http://dx.doi.org/10.1097/00001721-199810000-00111.

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Chowdhury, Sanghamitra M., and Jeffrey A. Hubbell. "Adhesion Prevention with Ancrod Released via a Tissue-Adherent Hydrogel." Journal of Surgical Research 61, no. 1 (February 1996): 58–64. http://dx.doi.org/10.1006/jsre.1996.0081.

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50

Yu, Xueling, Zhaofa Li, Xiaobing Xia, Hongqing Fang, Changlin Zhou, and Huipeng Chen. "Expression and purification of ancrod, an anticoagulant drug, in Pichia pastoris." Protein Expression and Purification 55, no. 2 (October 2007): 257–61. http://dx.doi.org/10.1016/j.pep.2007.07.002.

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Journal articles on the topic 'Ancrod'

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