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

Heavy membrane-associated caspase 3: identification, isolation, and characterization.

J F Krebs1, A Srinivasan, A M Wong

  • 1IDUN Pharmaceuticals, 11085 North Torrey Pines Road, Suite 300, La Jolla, California 92037, USA.

Biochemistry
|December 22, 2000
PubMed
Summary

A novel caspase-3 zymogen tightly bound to heavy membranes was identified. This membrane-bound procaspase can be activated by caspase-1, revealing distinct N-terminal processing compared to cytoplasmic forms.

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

Integrating multimodal prehabilitation into enhanced recovery after surgery programs (MPhERAS) for elderly patients: a systematic review and meta-analysis of randomized controlled trials and cohort studies.

Techniques in coloproctology·2025
Same author

<i>Meso</i>-Modified Porphyrinoids: Stimuli-Driven Conformational Plasticity, Modulation of π-Conjugation, and Bis-Rh(I) Complexation.

Inorganic chemistry·2025
Same author

Nonalternant Acenaphthylene-Fused Carbaporphyrins: Topological Modulation of π-Delocalization, (Anti)aromaticity, and B<sup>III</sup> Coordination.

Organic letters·2025
Same author

Siamese Twin Homocarbaporphyrin Dimer: Nonplanar Architecture, Localized Conjugation and Bis-B<sup>III</sup> Complex.

Chemistry, an Asian journal·2025
Same author

<i>E</i>-Stilbene-Imprinted Cyclic Diphyrin and Its B<sup>III</sup> Complex.

Organic letters·2025
Same author

Ectopic expression of the cation-chloride cotransporter KCC2 in blood exosomes as a biomarker for functional rehabilitation.

Frontiers in molecular neuroscience·2025

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Caspases are key proteases involved in apoptosis.
  • Caspase zymogens are typically found in the cytoplasm.
  • The localization and activation mechanisms of membrane-bound caspases are not fully understood.

Purpose of the Study:

  • To identify and characterize a novel caspase zymogen associated with heavy membranes.
  • To investigate the activation pathways and properties of this membrane-bound procaspase.
  • To compare the activated membrane-bound caspase-3 with its cytoplasmic counterpart.

Main Methods:

  • Isolation of heavy membrane preparations from 697 lymphoblastoid cells.
  • Activation of procaspase using caspase-1.
  • Purification of activated caspase-3 via affinity chromatography.

Related Experiment Videos

  • Characterization through amino acid sequencing and inhibitor specificity analysis.

    • Main Results:

    • A tightly bound caspase zymogen was found in heavy membrane preparations.
    • This procaspase could be activated by caspase-1 without detergents.
    • The purified enzyme was identified as caspase-3, enzymatically indistinguishable from cytoplasmic caspase-3.
    • Distinct N-terminal sequences were observed between membrane-bound (Lys14) and cytoplasmic (Ser10) caspase-3.

    Conclusions:

    • Heavy membranes harbor a distinct pool of caspase-3 zymogen.
    • Caspase-1 can activate membrane-bound procaspase-3.
    • Structural differences in N-terminal processing suggest unique regulatory mechanisms for membrane-associated caspase-3.