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

Protein disulfide isomerase activity is released by activated platelets.

K Chen1, Y Lin, T C Detwiler

  • 1Department of Biochemistry, State University of New York Health Science Center, Brooklyn 11203.

Blood
|May 1, 1992
PubMed
Summary

Activated platelets release protein disulfide isomerase (PDI), an enzyme crucial for protein folding. This PDI facilitates disulfide bond formation and influences thrombospondin interactions, suggesting a role in platelet function.

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

A remarkable rate acceleration of the Baylis-Hillman reaction.

Chemical communications (Cambridge, England)·2002
Same author

[The thumb reconstruction by transferring the injured index finger with pedicles].

Zhongguo xiu fu chong jian wai ke za zhi = Zhongguo xiufu chongjian waike zazhi = Chinese journal of reparative and reconstructive surgery·2002
Same author

[A new practical route to stereospecific synthesis of (S)-(-)-ofloxacin].

Yao xue xue bao = Acta pharmaceutica Sinica·2002
Same author

Effects of image resolution on autoradiographic measurements of posterior cingulate activity in PDAPP mice: implications for functional brain imaging studies of transgenic mouse models of Alzheimer's Disease.

NeuroImage·2002
Same author

Heart rate dynamics in monoamine oxidase-A- and -B-deficient mice.

American journal of physiology. Heart and circulatory physiology·2002
Same author

[Clinical study on treatment of nasopharyngeal carcinoma by radio- and chemotherapy with supplementary moxibustion on Shenque point].

Zhongguo Zhong xi yi jie he za zhi Zhongguo Zhongxiyi jiehe zazhi = Chinese journal of integrated traditional and Western medicine·2002

Area of Science:

  • Biochemistry
  • Hematology
  • Molecular Biology

Background:

  • Platelets play a key role in hemostasis and thrombosis.
  • Previous studies suggested thiol-disulfide exchange in activated platelet supernatants.
  • The involvement of protein disulfide isomerase (PDI) was hypothesized.

Purpose of the Study:

  • To investigate the release and activity of protein disulfide isomerase (PDI) by activated platelets.
  • To characterize the nature of the detected PDI activity.
  • To explore the potential functions of released PDI in platelet biology.

Main Methods:

  • Platelet activation and collection of supernatant.
  • Assay of PDI activity using ribonuclease renaturation.
  • Inhibition studies with known PDI inhibitors.

Related Experiment Videos

  • Characterization of the PDI activity using dialysis and gel filtration chromatography.
  • Centrifugation to assess association with microvesicles.

    • Main Results:

    • Protein disulfide isomerase (PDI) activity was detected in the supernatant of activated platelets.
    • The activity catalyzed ribonuclease renaturation, indicating PDI function.
    • PDI activity was inhibited by specific peptides, which also affected thrombospondin-thrombin complex formation.
    • The activity was associated with a macromolecule larger than 50 kDa and not with microvesicles.

    Conclusions:

    • Activated platelets release functional protein disulfide isomerase (PDI).
    • The released PDI may play a role in regulating disulfide bond formation in the extracellular environment.
    • This finding opens new avenues for understanding platelet-mediated biological processes.