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

Calcyclin and calvasculin exist in human platelets.

Y Tomida1, M Terasawa, R Kobayashi

  • 1Department of Pharmacology, Nagoya University School of Medicine, Japan.

Biochemical and Biophysical Research Communications
|December 30, 1992
PubMed
Summary

Researchers identified three calcium-binding proteins in human platelets using affinity chromatography. These proteins, related to calcyclin, calvasculin, and calmodulin, suggest novel roles in platelet calcium 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

Anti-immunoglobulin M activates nuclear calcium/calmodulin-dependent protein kinase II in human B lymphocytes.

The Journal of experimental medicine·1995
Same author

Elucidation of the protein kinase C-dependent apoptosis pathway in distinct subsets of T lymphocytes in MRL-lpr/lpr mice.

European journal of immunology·1995
Same author

Purification and characterization of a novel protein activator of Ca2+/calmodulin-dependent protein kinase I.

Biochemical and biophysical research communications·1995
Same author

Effect of KN-62, Ca2+/calmodulin-dependent protein kinase II inhibitor, on adriamycin resistance of human ovarian cancer cells.

Biochemical and biophysical research communications·1995
Same author

The regulatory region of calcium/calmodulin-dependent protein kinase I contains closely associated autoinhibitory and calmodulin-binding domains.

The Journal of biological chemistry·1995
Same author

Prophylaxis of genetically determined diabetes by diazoxide: a study in a rat model of naturally occurring obese diabetes.

The Journal of pharmacology and experimental therapeutics·1995

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Calcium ions (Ca2+) are crucial intracellular messengers involved in numerous cellular processes.
  • Platelets play a vital role in hemostasis and thrombosis, with calcium signaling being critical for their function.
  • Understanding Ca2+-binding proteins in platelets is essential for elucidating platelet activation and signaling pathways.

Purpose of the Study:

  • To identify and characterize calcium-dependent proteins present in human platelets.
  • To investigate the potential roles of these identified proteins in platelet intracellular functions.
  • To explore the involvement of these proteins in the Ca2+-signal transduction system within platelets.

Main Methods:

  • Ca2+-dependent affinity chromatography utilizing a synthetic compound (W-7)-coupled Sepharose column.

Related Experiment Videos

  • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) for estimating molecular masses.
  • Partial amino acid sequencing to determine protein structures and homology.
  • Main Results:

    • Three distinct Ca2+-binding proteins were successfully isolated from human platelets.
    • The molecular masses of these proteins were estimated to be 10 kDa, 10.5 kDa, and 17 kDa.
    • Partial amino acid sequencing indicated EF-hand structures and high homology to calcyclin, calvasculin, and calmodulin.

    Conclusions:

    • The identification of calcyclin and calvasculin homologs in platelets suggests functions beyond cell proliferation control.
    • These Ca2+-binding proteins likely play significant intracellular roles in platelet Ca2+-signal transduction.
    • Further research is warranted to fully elucidate the specific functions of these proteins in platelet biology.