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

Caspase structure, proteolytic substrates, and function during apoptotic cell death.

D W Nicholson1

  • 1Merck Frosst Centre for Therapeutic Research, Merck Frosst Canada & Co., PO Box 1005, Pointe Claire-Dorval, Quebec, Canada, H9R 4P8. donald_nicholson@merck.com

Cell Death and Differentiation
|December 1, 1999
PubMed
Summary
This summary is machine-generated.

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

Guidelines for the use and interpretation of assays for monitoring cell death in higher eukaryotes.

Cell death and differentiation·2009
Same author

L-454,560, a potent and selective PDE4 inhibitor with in vivo efficacy in animal models of asthma and cognition.

Biochemical pharmacology·2007
Same author

Peripheral phosphodiesterase 4 inhibition produced by 4-[2-(3,4-Bis-difluoromethoxyphenyl)-2-[4-(1,1,1,3,3,3-hexafluoro-2-hydroxypropan-2-yl)-phenyl]-ethyl]-3-methylpyridine-1-oxide (L-826,141) prevents experimental autoimmune encephalomyelitis.

The Journal of pharmacology and experimental therapeutics·2006
Same author

Caspase-3 cleaved spectrin colocalizes with neurofilament-immunoreactive neurons in Alzheimer's disease.

Neuroscience·2006
Same author

Differential regulation of caspase-3 by pharmacological and developmental stimuli as demonstrated using humanised caspase-3 mice.

Apoptosis : an international journal on programmed cell death·2004
Same author

Effects of fimbria-fornix transection on calpain and choline acetyl transferase activities in the septohippocampal pathway.

Neuroscience·2004
Same journal

A planar dimer of bovine ATP synthase.

Cell death and differentiation·2026
Same journal

GCN5 and TADA2B constitutively regulate XRCC1 function during DNA repair to maintain cell survival.

Cell death and differentiation·2026
Same journal

MEGF8 controls osteogenic differentiation through post-transcriptional regulation of BMP-SMAD signaling in craniosynostosis.

Cell death and differentiation·2026
Same journal

Macrophage-secreted brain-derived neurotrophic factor promotes tumor growth in triple-negative breast cancer by inducing axonogenesis.

Cell death and differentiation·2026
Same journal

Species-specific regulation of necroptosis by STK38-dependent RIPK1 phosphorylation.

Cell death and differentiation·2026
Same journal

Ssu72 phosphatase orchestrates obesogenic adipogenesis and metabolic homeostasis during nutrient excess.

Cell death and differentiation·2026
See all related articles

Caspases, a family of cysteine proteases, are crucial for programmed cell death (apoptosis). They cleave specific cellular targets, driving the characteristic events of apoptosis and potentially worsening disease.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Caspases are a family of cysteine proteases.
  • They are essential enzymes in the process of apoptotic cell death.
  • Mammalian cells possess over a dozen distinct caspase family members.

Purpose of the Study:

  • To elucidate the role of caspases in apoptotic cell death.
  • To understand the substrate specificity and function of caspases.
  • To explore the contribution of caspases to disease pathogenesis.

Main Methods:

  • Analysis of caspase enzyme activity.
  • Identification of caspase substrates.
  • Investigation of caspase involvement in cellular and morphological changes during apoptosis.

Related Experiment Videos

Main Results:

  • Caspases cleave a discrete subset of cellular polypeptides.
  • This cleavage accounts for most cellular and morphological events in apoptosis.
  • Caspases can contribute to increased apoptosis propensity and disease exacerbation.

Conclusions:

  • Caspases are key executioners of apoptosis, orchestrating its cellular and morphological features.
  • Their specific substrate cleavage is central to the apoptotic process.
  • Dysregulation of caspases may contribute to the pathogenesis of various diseases.