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Related Concept Videos

Caspases01:24

Caspases

Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside cells.
The Extrinsic Apoptotic Pathway01:17

The Extrinsic Apoptotic Pathway

The extrinsic apoptotic pathway is initiated when extracellular death-inducing signals, such as specific cytokines, activate the death receptors expressed on the cell surface. The immune cells involved in this pathway are natural killer cells (NK cells) and cytotoxic T-lymphocytes. NK cells are critical in innate immune response, while cytotoxic T-lymphocytes are associated with adaptive immune response. These cells recognize specific receptors expressed on the altered cells and activate...
The Intrinsic Apoptotic Pathway01:31

The Intrinsic Apoptotic Pathway

Internal cellular stress, such as cellular injury or hypoxia, triggers intrinsic apoptosis. The B-cell lymphoma 2 (Bcl-2) family of proteins are the primary regulators of the intrinsic apoptotic pathway. For example, during DNA damage, checkpoint proteins, such as Ataxia Telangiectasia Mutated (ATM protein) and Checkpoints Factor-2 (Chk2) proteins, are activated. These proteins phosphorylate p53 which further activates pro-apoptotic proteins, such as Bax, Bak, PUMA, and Noxa, and inhibits...
Apoptosis01:30

Apoptosis

Apoptosis is a combination of two Greek words, 'apo' and 'ptosis,' meaning separation and falling off, respectively. Hippocrates used this word to describe gangrene, which was caused due to bandaging of fractured bones. Apoptosis was distinguished from necrosis in 1970 when John Kerr reported observations of morphological changes occurring during apoptosis. During one experiment, he observed that the disruption of blood supply to the liver tissue resulted in a size reduction of the tissue.
Autophagic Cell Death01:18

Autophagic Cell Death

Christian de Duve discovered “autophagy,” a process in which cellular components are engulfed by membrane-bound organelles called autophagosomes. The autophagosomes then fuse with lysosomes to digest the enclosed contents. Autophagy is generally activated in cells to prevent cell death. However, cell death is triggered when the damage is beyond repair.
Autophagy and Apoptosis
Autophagy can activate apoptosis. In normal conditions, the autophagy activating protein Beclin-1 and pro-apoptotic...

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In Vivo Biosensor Tracks Non-apoptotic Caspase Activity in Drosophila
13:21

In Vivo Biosensor Tracks Non-apoptotic Caspase Activity in Drosophila

Published on: November 27, 2016

Caspase-8: fly or die.

Steven M Frisch1

  • 1West Virginia University, Mary Babb Randolph Cancer Center, Morgantown, West Virginia, USA. sfrisch@hsc.wvu.edu

Cancer Research
|June 19, 2008
PubMed
Summary
This summary is machine-generated.

Procaspase-8 regulates cell adhesion and migration by interacting with Src kinase. This interaction prevents apoptosis, offering potential cancer therapy targets.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Cancer Research

Background:

  • Procaspase-8 plays a role in cell adhesion and motility.
  • Src phosphorylation influences procaspase-8's function.

Purpose of the Study:

  • To survey recent findings on procaspase-8's function in cell adhesion and motility.
  • To discuss the mechanism of Src phosphorylation in regulating procaspase-8.
  • To explore the implications for cancer prognosis and therapy.

Main Methods:

  • Literature review of recent studies on procaspase-8.
  • Analysis of molecular interactions involving procaspase-8, Src, p85alpha, Rac, and ERK.
  • Discussion of signaling pathways including PI3K and calpain activation.

Main Results:

  • Procaspase-8 acts as an adhesion/migration factor, while mature caspase-8 induces apoptosis.
  • Src phosphorylation prevents procaspase-8 conversion to mature caspase-8, thus controlling its function.
  • Procaspase-8 modulates Rac and ERK signaling and promotes calpain activation during migration.

Conclusions:

  • Src-mediated phosphorylation of procaspase-8 provides a switch between cell migration and apoptosis.
  • Understanding this mechanism may lead to novel cancer therapeutic strategies targeting cell adhesion and motility.