Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Bothrops jararaca snake venom: effects on platelet aggregation.

R B Zingali1, C R Carlini, I M Francischetti

  • 1Department of Biochemistry-ICB, Universidade Federal do Rio de Janeiro, Ilha do Fundão, Brazil.

Thrombosis Research
|May 1, 1990
PubMed
Summary

Bothrops jararaca venom contains distinct proteins that cause blood clotting and platelet aggregation. Phospholipase A2 (PLA2) activity in the venom also inhibits platelet aggregation, suggesting a dual role for these proteins.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Jack bean (Canavalia ensiformis) urease induces eicosanoid-modulated hemocyte aggregation in the Chagas' disease vector Rhodnius prolixus.

Toxicon : official journal of the International Society on Toxinology·2014
Same author

The presence of concanavalin A and canatoxin in Canavalia ensiformis DC tissue culture.

Plant cell reports·2013
Same author

Canatoxin-, concanavalin A- and canavalin-cross-reactive materials during maturation of Canavalia brasiliensis (Mart.) seeds.

Planta·2013
Same author

A phospholipase A2 gene is linked to Jack bean urease toxicity in the Chagas' disease vector Rhodnius prolixus.

Biochimica et biophysica acta·2013
Same author

Proteome of Rhipicephalus sanguineus tick saliva induced by the secretagogues pilocarpine and dopamine.

Ticks and tick-borne diseases·2013
Same author

[Fruit flies (Diptera: Tephritidae) and their parasitoids (Hymenoptera: Braconidae) associated to host plants in the southern region of Bahia State].

Neotropical entomology·2011

Area of Science:

  • Biochemistry
  • Toxicology
  • Pharmacology

Background:

  • The venom of Bothrops jararaca exhibits complex biological activities, including procoagulant and platelet-aggregating effects.
  • Phospholipase A2 (PLA2) is a known enzyme class found in snake venoms with diverse enzymatic and biological functions.

Purpose of the Study:

  • To investigate and separate the distinct protein components responsible for the procoagulant, platelet aggregating, and PLA2 activities in Bothrops jararaca venom.
  • To characterize the nature of the platelet aggregating factors and the relationship between PLA2 activity and platelet aggregation inhibition.

Main Methods:

  • Chromatographic fractionation of Bothrops jararaca crude venom using Sephacryl S-200.
  • Biochemical assays to measure procoagulant, platelet aggregating, and phospholipase A2 activities.

Related Experiment Videos

  • Enzymatic inhibition studies using PMSF, p-bromophenacyl bromide, and 2-mercaptoethanol.

    • Main Results:

    • Separation of distinct protein components responsible for procoagulant, platelet aggregating, and PLA2 activities.
    • Identification of two components involved in platelet aggregation: a serine proteinase and a calcium/plasma-dependent factor.
    • Fractions with PLA2 activity inhibited collagen-induced platelet aggregation and accelerated ADP-induced aggregation reversal.
    • PLA2 activity and platelet aggregation inhibition were abolished by p-bromophenacyl bromide and 2-mercaptoethanol, suggesting a common molecular basis.

    Conclusions:

    • Bothrops jararaca venom contains multiple protein components with distinct biological activities.
    • The PLA2 activity and the inhibition of platelet aggregation in this venom may reside in the same protein molecule.
    • These findings contribute to understanding the complex mechanisms of snake venom toxicity and potential therapeutic applications.