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Caspases01:24

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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...
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The Intrinsic Apoptotic Pathway01:31

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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...
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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...
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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...
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Caspases and their substrates.

Olivier Julien1, James A Wells1

  • 1Department of Pharmaceutical Chemistry and Cellular &Molecular Pharmacology, University of California, San Francisco, CA, USA.

Cell Death and Differentiation
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PubMed
Summary
This summary is machine-generated.

Human caspases are key cysteine proteases in cell death and remodeling. Proteomics reveals diverse caspase substrates, highlighting challenges in understanding cleavage events

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Human caspases are cysteine proteases crucial for apoptosis and pyroptosis.
  • Emerging roles in cellular remodeling include stem cell fate, spermatogenesis, and erythroid differentiation.
  • Global proteomics enables large-scale identification of caspase substrates.

Purpose of the Study:

  • To survey progress in global caspase substrate identification using proteomics.
  • To explore new avenues for understanding caspase substrate cleavage logic in cell death and remodeling.
  • To highlight challenges in determining functional consequences of proteolytic events.

Main Methods:

  • Global proteomics to identify caspase substrates in live cells and extracts.
  • Analysis of substrate cleavage rates across different caspases.
  • Review of studies on specific caspase targets and their functional outcomes.

Main Results:

  • Caspase substrate targets vary widely, from dozens to hundreds per caspase.
  • Each caspase exhibits preferred substrate cohorts with significant cleavage rate variations.
  • Few single cleavage events trigger apoptosis (e.g., caspase-3/-7, BIMEL) or pyroptosis (gasdermin D); most function cooperatively.
  • Caspase roles in non-apoptotic processes remain less understood.

Conclusions:

  • Proteomics has significantly advanced caspase substrate identification.
  • Understanding the functional impact of specific caspase cleavage events is a major challenge.
  • Further research is needed to elucidate caspase biology in non-apoptotic cellular remodeling.