Textilinins from Pseudonaja textilis textilis. Characterization of two plasmin inhibitors that reduce bleeding in an animal model

@article{Masci2000TextilininsFP,
  title={Textilinins from Pseudonaja textilis textilis. Characterization of two plasmin inhibitors that reduce bleeding in an animal model},
  author={P. Masci and A. Whitaker and L. Sparrow and J. de Jersey and D. Winzor and D. Watters and M. Lavin and P. Gaffney},
  journal={Blood Coagulation and Fibrinolysis},
  year={2000},
  volume={11},
  pages={385-393}
}
The incidence of vein-graft occlusion associated with myocardial infarction and thrombosis following the use of the plasmin inhibitor, aprotinin, to reduce blood loss during vascular surgery has prompted the isolation of an alternative kinetically distinct inhibitor of plasmin from the venom ofPseudonaja textilis. This inhibitor has been called textilinin (Txln) and two distinct forms have been isolated from the Brown-snake venom (molecular weight, 6688 and 6692). A comparison of plasmin… Expand
Comparison of Textilinin-1 with Aprotinin as Serine Protease Inhibitors and as Antifibrinolytic Agents
TLDR
From data, textilinin-1 appears to be a more specific plasmin inhibitor than aprotinin but aProtinin inhibits clot lysis to a greater extent. Expand
Purification and characterization of tenerplasminin-1, a serine peptidase inhibitor with antiplasmin activity from the coral snake (Micrurus tener tener) venom.
TLDR
TP1 is the first serine protease plasmine-like inhibitor isolated from Mtt snake venom which has been characterized in relation to its mechanism of action, formation of a plasmin:TP1 complex and therapeutic potential as anti-fibrinolytic agent, a biological characteristic of great interest in the field of biomedical research. Expand
Crystal structure of textilinin‐1, a Kunitz‐type serine protease inhibitor from the venom of the Australian common brown snake (Pseudonaja textilis)
TLDR
The presence of the bulkier valine as the P1′ residue in textilinin‐1 appears to be a major contributor to reducing the binding affinity for plasmin as compared to aprotinin and could also account for an observed narrower binding specificity. Expand
Identification and characterisation of Kunitz-type plasma kallikrein inhibitors unique to Oxyuranus sp. snake venoms.
TLDR
TSPI was found to be a broad spectrum inhibitor with most potent inhibitory activity observed against plasma kallikrein that corresponded to a K(i) of 0.057 ± 0.019 nM. Expand
Crystallization and preliminary X-ray analysis of a Kunitz-type inhibitor, textilinin-1 from Pseudonaja textilis textilis.
TLDR
The crystallization of recombinant textilinin-1 as the free molecule and in complex with bovine trypsin (229 amino acids) is reported and it is expected that the overall fold of these molecules is similar but that they have contrasting surface features. Expand
A family of textilinin genes, two of which encode proteins with antihaemorrhagic properties
TLDR
These recombinant textilinins have potential as therapeutic agents for reducing blood loss in humans, obviating the need for reliance on aprotinin, a bovine product with possible risk of transmissible disease, and compromising the fibrinolytic system in a less irreversible manner. Expand
Functional characterization of a slow and tight-binding inhibitor of plasmin isolated from Russell's viper venom.
TLDR
The first in-depth functional characterization of a plasmin inhibitor from a viperid snake is presented, which makes it a potential candidate for the development of novel antifibrinolytic agents. Expand
Textilinin‐1, an alternative anti‐bleeding agent to aprotinin: Importance of plasmin inhibition in controlling blood loss
TLDR
Textilinin‐1, a serine protease inhibitor from Pseudonaja textilis venom with sequence relatedness to aProtinin, is a potent but reversible plasmin inhibitor and has a narrower range of protease inhibition compared to aprotinin. Expand
A novel Kunitz protein with proposed dual function from Eudiplozoon nipponicum (Monogenea) impairs haemostasis and action of complement in vitro.
TLDR
It is suggested that the secretory Kunitz protein of E. nipponicum has a dual function, which impairs both haemostasis and complement activation in vitro, and thus might facilitate digestion of a host's blood and protect a parasite's gastrodermis from damage by the complement. Expand
Discreplasminin, a plasmin inhibitor isolated from Tityus discrepans scorpion venom
TLDR
Results suggest that discreplasminin presents an anti-fibrinolytic mechanism similar to aprotinin, which could partially explain the generalized fibrin deposition which was found previously in rams. Expand
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References

SHOWING 1-10 OF 51 REFERENCES
Fibrinolysis as a feature of disseminated intravascular coagulation (DIC) after Pseudonaja textilis textilis envenomation.
TLDR
Blood was obtained from four patients envenomated by the Australian common brown snake and the data suggest that the prothrombin activator of this venom causes the generation of thrombin which subsequently converts fibrinogen tofibrin and stimulates partial crosslinking of both alpha and gamma-chains. Expand
A novel serine protease inhibitor from the Australian brown snake, Pseudonaja textilis textilis: Inhibition kinetics
TLDR
Results demonstrate that the small protein protease inhibitor from the Australian brown snake does not act via the standard slow, tight-binding mechanism common to other small protein serine protease inhibitors. Expand
Aprotinin in perspective.
  • S. Westaby
  • Medicine
  • The Annals of thoracic surgery
  • 1993
TLDR
The fact that the hemostatic process is affected from the very beginning of cardiopulmonary bypass is substantiated by the fact that low-dose aprotinin therapy leads to the same preservative effect on Gp Ib receptors and blood loss as continuous high-dose infusion throughout the whole surgical procedure. Expand
The serine antiprotease aprotinin (Trasylol): a novel approach to reducing postoperative bleeding.
  • D. Royston
  • Medicine
  • Blood coagulation & fibrinolysis : an international journal in haemostasis and thrombosis
  • 1990
TLDR
The profound effect of aprotinin, given in a novel dosage to reverse the postoperative haemostatic defect suggests that this drug may abolish the need for blood transfusions in most patients after major surgery. Expand
Isolation and physiological characterization of taicatoxin, a complex toxin with specific effects on calcium channels.
TLDR
The resulting complex contains only alpha-neurotoxin and protease inhibitor and is still capable of blocking calcium channels, although with less potency than the native oligomeric form. Expand
Serine Proteinase Inhibitors from Vipera ammodytes Venom
TLDR
Three protein inhibitors of serine proteinases were isolated from the crude venom of the long-nosed viper Vipera ammodytes ammODYtes by ion-exchange and gel chromatography and belong to the Kunitzpancreatic trysin inhibitor family of inhibitors. Expand
Purification and characterization of a chymotrypsin Kunitz inhibitor type of polypeptide fro the venom of cobra (Naja naja naja)
TLDR
A chymotrypsin Kunitz inhibitor type of polypeptide has been isolated from the venom of Naja naja nja by reverse phase HPLC and cation exchange FPLC, showing the specificity of the inhibitor. Expand
Purification, characterization and substrate specificity of a basic proteinase in the venom of Habu (Trimeresurus flavoriridis)
TLDR
From the disappearance of intermediate peptides and the peptides accumulated, the order and the intensity of cleavage of these positions were determined, and the substrate specificity was compared with those hitherto described for hemorrhagic and nonhemorrhagic venom proteinases. Expand
A structural aspect of human fibrinogen suggested by its plasmin degradation
TLDR
The subunit molecular weights of human fibrinogen and various fragments released during its hydrolysis with plasmin are described and the location of the subunits of the anticoagulant core fragment, D, in native fibr inogen is suggested. Expand
Distribution of proteinase inhibitors in snake venoms.
TLDR
Toxic polypeptides such as α-bungarotoxin, cytotoxin I and II ( Naja naja venom) and cardiotoxin ( Nja naja atra venom) did not show any inhibitory action on typical mammalian proteinases including trypsin, α-chymotryps in, plasmin and kallikrein. Expand
...
1
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3
4
5
...