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

Endogenous ADP-ribosylation in human platelets.

L Molina y Vedia1, R D Nolan, E G Lapetina

  • 1Division of Cell Biology, Burroughs Wellcome Co., Research Triangle Park, NC 27709.

Biochemical and Biophysical Research Communications
|December 30, 1988
PubMed
Summary

Researchers investigated ADP-ribosyltransferase activity in platelets, identifying a 37 kDa protein ADP-ribosylation. This process, influenced by potassium phosphate and thiol reagents, offers a new method to study platelet signaling.

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

Interaction of the low-molecular-weight GTP-binding protein rap2 with the platelet cytoskeleton is mediated by direct binding to the actin filaments.

Journal of cellular biochemistry·1999
Same author

Resistance of Crohn's disease T cells to multiple apoptotic signals is associated with a Bcl-2/Bax mucosal imbalance.

Journal of immunology (Baltimore, Md. : 1950)·1999
Same author

Rap1B and Rap2B translocation to the cytoskeleton by von Willebrand factor involves FcgammaII receptor-mediated protein tyrosine phosphorylation.

The Journal of biological chemistry·1999
Same author

Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase.

The Journal of biological chemistry·1999
Same author

Phosphatidylinositol 3-kinase is a target for protein tyrosine nitration.

Biochemical and biophysical research communications·1998
Same author

Glutathione levels determine apoptosis in macrophages.

Biochemical and biophysical research communications·1998

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Hematology

Background:

  • ADP-ribosyltransferase (ADPRT) enzymes play crucial roles in cellular signaling pathways.
  • Platelets are key participants in hemostasis and thrombosis, with their signaling mechanisms being of significant interest.
  • Understanding endogenous protein modification in platelets, such as ADP-ribosylation, is essential for elucidating platelet function.

Purpose of the Study:

  • To characterize ADP-ribosyltransferase activity within human platelet cytosol.
  • To investigate ADP-ribosylation of specific proteins in electropermeabilized platelets.
  • To establish an experimental model for assessing the impact of agonists on platelet ADP-ribosylation.

Main Methods:

  • Assay of ADP-ribosyltransferase activity in platelet cytosol.

Related Experiment Videos

  • Incubation of electropermeabilized platelets with [alpha-32P]NAD to detect protein ADP-ribosylation.
  • Analysis of the effects of potassium phosphate, thiol reagents, cholera toxin, and nicotinamide on ADP-ribosylation.

    • Main Results:

    • Cytosolic ADP-ribosyltransferase activity was observed, leading to the ADP-ribosylation of a 37 kDa protein, which was enhanced by potassium phosphate.
    • ADP-ribosylation in electropermeabilized platelets modified the 37 kDa protein, other proteins, and albumin.
    • Thiol reagents partially inhibited ADP-ribosylation, an effect partly reversed by cholera toxin, while nicotinamide showed partial inhibition in electropermeabilized platelets.

    Conclusions:

    • A specific 37 kDa protein is a substrate for ADP-ribosylation in platelet cytosol.
    • The experimental system using electropermeabilized platelets allows for the study of endogenous protein ADP-ribosylation.
    • This model provides a foundation for investigating how cellular agonists modulate protein ADP-ribosylation in platelets.