Ancrod
An enzyme fraction from the venom of the Malayan pit viper, Agkistrodon rhodostoma. It catalyzes the hydrolysis of a number of amino acid esters and a limited proteolysis of fibrinogen. It is used clinically to produce controlled defibrination in patients requiring anticoagulant therapy. EC 3.4.21.-.
Fibrin
Cellophane
A generic name for film produced from wood pulp by the viscose process. It is a thin, transparent sheeting of regenerated cellulose, moisture-proof and sometimes dyed, and used chiefly as food wrapping or as bags for dialysis. (Grant & Hackh's Chemical Dictionary, 5th ed & McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Fibrinogen
Plasma glycoprotein clotted by thrombin, composed of a dimer of three non-identical pairs of polypeptide chains (alpha, beta, gamma) held together by disulfide bonds. Fibrinogen clotting is a sol-gel change involving complex molecular arrangements: whereas fibrinogen is cleaved by thrombin to form polypeptides A and B, the proteolytic action of other enzymes yields different fibrinogen degradation products.
Development of an ischemic stroke survival score. (1/41)
BACKGROUND AND PURPOSE: There has been substantial interest in identifying predictors of survival for stroke patients. Current instruments used for measuring stroke severity are confined to either neurological, functional, or disability measures. The purpose of this study was to develop a stroke survival score that combines instruments from different domains to better predict long-term survival. METHODS: We took advantage of a particularly broad array of clinical and physiological variables collected during the Stroke Treatment with Ancrod Trial. Four hundred fifty-three patients completed a battery of instruments at day 7 after stroke and then were followed for 1 year. RESULTS: Of the 453 patients, 53% were male, 77% were aged 65 years or older, and 89% were white. One hundred nine patients (24%) died during the study period. Age was a highly significant predictor of mortality (P<0.001), but there were no statistically significant differences in 12-month survival with respect to sex, race, or educational level. The best model for predicting survival was the Ischemic Stroke Survival Score. This model included the Scandinavian Stroke Scale, Rapid Disability Rating Scale, age, and prior stroke. This model had substantially greater predictive power (R(2)=0.30, c statistic=0.86) than the Scandinavian Stroke Scale alone (R(2)=0.20, c statistic=0.78). CONCLUSIONS: This study demonstrates that combining day 7 poststroke information from multiple domains substantially improves the ability to predict 12-month survival of ischemic stroke patients compared with data from a single domain. The high mortality rate emphasizes the importance of preventive measures for a disease that has identifiable and modifiable risk factors. (+info)Analysis of fibrin formation and proteolysis during intravenous administration of ancrod. (2/41)
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 E(A), 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-alpha(2)-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 product D-dimer in plasma. (Blood. 2000;96:2793-2802) (+info)The effect of angrod on the delayed hypersensitivity response in rats. (3/41)
Delayed hypersensitivity was induced in rats by means of sheep erythrocytes and bovine serum albumin-lipid conjugate. Administration of heparin to rats sensitized to either antigen resulted in diminution of the delayed hypersensitivity reaction. Administration of ancrod, however, failed to inhibit the delayed cellular reaction to either antigen. Granuloma formation remained unaffected when rats were injected with either heparin or ancrod. The lack of ancrod effect, in contrast to heparin effect, on delayed hypersensitivity is discussed. (+info)A quantitative evaluation of anticoagulants in experimental nephrotoxic nephritis. (4/41)
The protective effects of anticoagulants in nephrotoxic nephritis in rabbits have been studied, using various doses of heparin and defibrination with ancrod. Massive doses of heparin (2000 units/kg/day) were required before significant reduction in glomerular fibrin deposition, extracepillary cell proliferation and urea retention occurred. Doses of 300 and 1000 units/kg/day were insufficient to modify fibrin deposition and cell proliferation. Defibrination with ancrod provided protection, judged by histological and functional criteria, comparable to 2000 units of heparin/kg/day; but fibrin could still be demonstrated in the glomeruli of animals treated with 2000 units of heparin/kg/day, contrasting with the virtual absence of fibrin in animals given ancrod. (+info)The effects of defibrination with ancrod in experimental allergic glomerular injury. (5/41)
Quantitative studies of the effects of defibrination (with ancrod) have been undertaken in two forms of allergic glomerular damage, nephrotoxic serum nephritis and acute serum sickness in rabbits. No differences in intrarenal fixation of nephrotoxic antibody, complement activation or host antibody response were detected between defibrinated and untreated rabbits with nephrotoxic serum nephritis. Defibrination prevented intraglomerular fibrin deposition in this disease; but some glomerular damage as shown by a rise in blood urea and endothelial proliferation still occurred in defibrinated animals. No differences in immune elimination of BSA, circulating immune complex formation or intrarenal localization of immune complexes were noted in defibrinated animals with acute serum sickness. No intraglomerular fibrin deposition was detected in treated or untreated animals in this disease model. It is concluded that the protective effects of ancrod are directly related to defibrination, and not to any other modification of allergic events. (+info)Fibrinogen depletion attenuates Staphyloccocus aureus infection by preventing density-dependent virulence gene up-regulation. (6/41)
Staphylococcus aureus undergoes a density-dependent conversion in phenotype from tissue-adhering to tissue-damaging and phagocyte-evading that is mediated in part by the quorum-sensing operon, agr, and its effector, RNAIII. Contributions of host factors to this mechanism for regulating virulence have not been studied. We hypothesized that fibrinogen, as a component of the inflammatory response, could create spatially constrained microenvironments around bacteria that increase density independently of bacterial numbers and thus potentiate quorum-sensing-dependent virulence gene expression. Here we show that transient fibrinogen depletion significantly reduces the bacterial burden and the consequential morbidity and mortality during experimental infection with wild-type S. aureus, but not with bacteria that lack expression of the quorum-sensing operon, agr. In addition, it inhibits in vivo activation of the promoter for the agr effector, RNAIII, and downstream targets of RNAIII, including alpha hemolysin and capsule production. Moreover, both in vitro and in vivo, the mechanism for promoting this phenotypic switch in virulence involves clumping of the bacteria, demonstrating that S. aureus responds to fibrinogen-mediated bacterial clumping by enhancing density-dependent virulence gene expression. These data demonstrate that down-modulation of specific inflammatory components of the host that augment bacterial quorum sensing can be a strategy for enhancing host defense against infection. (+info)Embolization itself stimulates thrombus propagation in pulmonary embolism. (7/41)
The role of active thrombosis in the pathophysiology of pulmonary embolism is unclear. We tested the hypothesis that venous thrombi significantly increase their thrombotic activity once they embolize into the high-flow circulation of the pulmonary arteries. Thrombotic activity was measured using an immunoassay that measures both fibrinopeptide B (FPB) as well as its most abundant metabolite des-arginine FPB. Thrombi were formed in the femoral veins of adult dogs. In one group, the thrombi were embolized without anticoagulation. In the second group, heparin (300 U/kg bolus, then 90 U x kg(-1) x h(-1) infusion) was administered before embolization to prevent subsequent thrombotic activity. Plasma FPB concentrations were significantly suppressed in the heparinized group relative to the nonheparinized group for 1 h postembolization (P = 0.038). We conclude that pulmonary embolization itself causes preexisting venous thrombi to greatly intensify their thrombotic activity and that embolization-associated thrombus propagation can be prevented by heparin. (+info)Soluble fibrin is the main mediator of Staphylococcus aureus adhesion to platelets. (8/41)
BACKGROUND: Infective endocarditis (IE) caused by Staphylococcus aureus is associated with significant morbidity and mortality rates. Platelets play a dual role as adhesive cells forming associates with bacteria as well as specialized inflammatory cells. The specific role of the various factors involved in bacteria-platelet association has not yet been fully elucidated. METHODS AND RESULTS: We observed a dramatic increase in the capability to bind S aureus when platelets were activated with thrombin (from 5% to 30%, P<0.001). To pinpoint platelet-binding sites involved in the interaction, platelets from knockout mice and from patients with selective inherited deficiency of membrane proteins or of granules were used. CD36, GPIIb/IIIa, and P-selectin were excluded as receptors for S aureus. Platelets from patients with alpha-delta-storage pool disease and Gray platelet syndrome indicate the requirement of alpha-granule contents. Platelet activation by ADP did not promote platelet-S aureus associate formation, although these platelets were covered with bound fibrinogen. Only small numbers of associates between fibrinogen-covered bacteria and ADP-activated platelets were observed. Formation of fibrin alone was also not sufficient to induce association. Only when fibrin formation and platelet activation occurred together were large numbers of associates formed (P<0.001). A potential receptor for fibrin on S aureus is clumping factor A. Addition of thrombospondin-1 to control platelets increased the number of associates (P=0.02). CONCLUSIONS: Soluble fibrin but not fibrinogen is the main mediator of platelet-S aureus association. In addition, platelet activation and the release of alpha-granule contents, particularly thrombospondin-1, is a requirement for platelet-S aureus association. (+info)Ancrod snake venom peptide
Double-blind, Randomized, Placebo-controlled Study on Efficacy, Safety and Tolerability of Ancrod in Patients With Sudden...
OBSERVATIONS ON EARLY DETECTION AND THERAPY OF THE DEFIBRINATION SYNDROME IN MENINGOCOCCEMIA,
Correction | Stroke
Venom of snake used in stroke treatment | Lewiston Sun Journal
ancrod - oi
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Recombinant Calloselasma rhodostoma Thrombin-like enzyme ancrod | Technique alternative | 01014479754 - thrombrin - a serine...
Order Recombinant Calloselasma rhodostoma Thrombin-like enzyme ancrod 01014479754 at Gentaur Calloselasma rhodostoma Thrombin- ... Our Calloselasma rhodostoma Thrombin-like enzyme ancrod is a recombinant CALRH protein expressed in Yeast with His-tag ... For long term storage, keep the Recombinant Calloselasma rhodostoma Thrombin-like enzyme ancrod frozen at -20 or -80 degrees ... The CALRH Calloselasma rhodostoma Thrombin-like enzyme ancrod is shipped on ice packs. ...
Fluoxetine (Oral Route) Before Using - 妙佑医疗国际
Although certain medicines should not be used together at all, in other cases two different medicines may be used together even if an interaction might occur. In these cases, your doctor may want to change the dose, or other precautions may be necessary. When you are taking this medicine, it is especially important that your healthcare professional know if you are taking any of the medicines listed below. The following interactions have been selected on the basis of their potential significance and are not necessarily all-inclusive.. Using this medicine with any of the following medicines is not recommended. Your doctor may decide not to treat you with this medication or change some of the other medicines you take.. ...
Microstructure and Mechanics of Collagen-Fibrin Matrices Polymerized Using Ancrod Snake Venom Enzyme | J. Biomech Eng. | ASME...
Intravenous Ancrod for Acute Ischaemic Stroke in the European Stroke Treatment With Ancrod Trial: A Randomised Controlled Trial ... Microstructure and Mechanics of Collagen-Fibrin Matrices Polymerized Using Ancrod Snake Venom Enzyme Shaneen L. Rowe, Shaneen L ... Role of Fibrinopeptide B Release: Comparison of Fibrins Produced by Thrombin and Ancrod ... "Microstructure and Mechanics of Collagen-Fibrin Matrices Polymerized Using Ancrod Snake Venom Enzyme." ASME. J Biomech Eng. ...
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3.4.21.74: venombin A - BRENDA Enzyme Database
DeCS
use ANCROD to search ARVIN 1975-77. History Note:. 78; was ARVIN see under ENDOPEPTIDASES 1975-77; ARVIN was see ANCROD 1978-95 ... Ancrod - Preferred Concept UI. M0001092. Scope note. An enzyme fraction from the venom of the Malayan pit viper, Agkistrodon ... Ancrod Entry term(s):. Agkistrodon Serine Proteinase. Agkistrodon rhodostoma Venom Protease. Arvin. Arvin IRC 50. Arvin IRC-50 ... 78; was ARVIN see under PEPTIDE PEPTIDOHYDROLASES 1975-77; ARVIN was see ANCROD 1978-95. ...
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Nicotine poisoning - Wikipedia
The LD50 of nicotine is 50 mg/kg for rats and 3 mg/kg for mice. 0.5-1.0 mg/kg can be a lethal dosage for adult humans, and 0.1 mg/kg for children.[19][20] However the widely used human LD50 estimate of 0.5-1.0 mg/kg was questioned in a 2013 review, in light of several documented cases of humans surviving much higher doses; the 2013 review suggests that the lower limit causing fatal outcomes is 500-1000 mg of ingested nicotine, corresponding to 6.5-13 mg/kg orally.[21] An accidental ingestion of only 6 mg may be lethal to children.[22] It is unlikely that a person would overdose on nicotine through smoking alone. The US Food and Drug Administration (FDA) stated in 2013: "There are no significant safety concerns associated with using more than one [over the counter] OTC [nicotine replacement therapy] NRT at the same time, or using an OTC NRT at the same time as another nicotine-containing product-including a cigarette."[23][24][25] Ingestion of nicotine pharmaceuticals, tobacco products, or ...
Warfarin
In the early 1920s, there was an outbreak of a previously unrecognized cattle disease in the northern United States and Canada. Cattle were haemorrhaging after minor procedures and on some occasions, spontaneously.[82] For example, 21 out of 22 cows died after dehorning and 12 out of 25 bulls died after castration. All of these animals had bled to death.[83]. In 1921, Frank Schofield, a Canadian veterinary pathologist, determined that the cattle were ingesting moldy silage made from sweet clover, and that this was functioning as a potent anticoagulant.[82] Only spoiled hay made from sweet clover (grown in northern states of the USA and in Canada since the turn of the century) produced the disease.[84] Schofield separated good clover stalks and damaged clover stalks from the same hay mow, and fed each to a different rabbit. The rabbit that had ingested the good stalks remained well, but the rabbit that had ingested the damaged stalks died from a haemorrhagic illness. A duplicate experiment with a ...
EC 3.4.21.74
1. Nolan, C., Hall, L.S. and Barlow, G.H. Ancrod, the coagulating enzyme from Malayan pit viper (Agkistrodon rhodostoma) venom ... Species variants of the enzyme include ancrod from Agkistrodon rhodostoma (Malayan pit viper) (formerly EC 3.4.21.28) [1], ... ancrod; (see also Comments). Comments: A somewhat thrombin-like enzyme from venoms of snakes of the viper/rattlesnake group. ...
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Plasma fibrinogen levels were reduced significantly by ancrod (baseline: 325.2 mg/dL, day 2: 107.2 mg/dL). Ancrod was tolerated ... 22 ancrod, 9 placebo). A significant improvement of hearing loss was registered in both groups (ancrod: - 14.3 dB ± 20.4 dB, - ... CONCLUSION: Ancrod reduced fibrinogen levels that support its mechanism of action. The safety profile can be rated positively. ... The aim was to determine the efficacy and safety of drug-induced defibrinogenation by ancrod for SSHL. METHODS: Double-blind, ...
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The N-terminal EGF domain has been shown to at least in part be responsible for binding tissue factor.[6] Wilkinson et al. conclude that residues 88 to 109 of the second EGF domain mediate binding to platelets and assembly of the factor X activating complex.[7] The structures of all four domains have been solved. A structure of the two EGF domains and the trypsin-like domain was determined for the pig protein.[8] The structure of the Gla domain, which is responsible for Ca(II)-dependent phospholipid binding, was also determined by NMR.[9] Several structures of super active mutants have been solved,[10] which reveal the nature of factor IX activation by other proteins in the clotting cascade. ...
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Enzyme4
- The CALRH Calloselasma rhodostoma Thrombin-like enzyme ancrod is shipped on ice packs. (thrombrin.com)
- For long term storage, keep the Recombinant Calloselasma rhodostoma Thrombin-like enzyme ancrod frozen at -20 or -80 degrees Celsius. (thrombrin.com)
- In order to vary the matrix microstructure, fibrin polymerization in mixed constructs was initiated using either the blood-derived enzyme thrombin or the snake venom-derived enzyme ancrod, each at low and high concentrations. (asme.org)
- 1. Nolan, C., Hall, L.S. and Barlow, G.H. Ancrod, the coagulating enzyme from Malayan pit viper ( Agkistrodon rhodostoma ) venom. (qmul.ac.uk)
Viprinex2
- Ancrod (Viprinex) is a coagulant substance prepared from the venom of the Malayan pit viper ( Calloselasma rhodostoma ). (reptilesmagazine.com)
- Scientists have developed an investigational agent, called ancrod (Viprinex), derived from the venom of the Malayan pit viper that offers the potential to extend the window of treatment opportunity. (20m.com)
Patients2
- Patients received an infusion of ancrod or placebo (day 1) followed by subcutaneous administrations (day 2, 4, 6). (bvsalud.org)
- RESULTS: The study was terminated early due to slow recruiting (31 enrolled patients: 22 ancrod, 9 placebo). (bvsalud.org)
Fibrinogen2
- The effect of fibrinogen was studied by using blood of varying natural fibrinogen concentration, defibrinogenated blood (by pre-treatment with Ancrod) and blodd whose fibrinogen concentration had been increased by the addition of purified autolgous canine fibrinogen. (bl.uk)
- Depletion of fibrinogen by ancrod treatment resulted in equalization in the quantity of fibrosis and collagen deposition in the lungs of knockout and wild-type mice. (cloudlegalproject.org)
Subsequently1
- Subsequently, a protein called Ancrod was shown to prevent blood clots to form. (smartox-biotech.com)
Results2
- Results of 500 Subjects Beginning Treatment Within 6 Hours of Stroke Onset in the Ancrod Stroke Program. (medscape.com)
- Whereas the first two types of treatment often give unsatisfactory results, a new rheological therapy using Ancrod seems to be successful. (cdc.gov)