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Related Concept Videos

Caspases01:24

Caspases

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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 Extrinsic Apoptotic Pathway01:17

The Extrinsic Apoptotic Pathway

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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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The Intrinsic Apoptotic Pathway01:31

The Intrinsic Apoptotic Pathway

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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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Apoptosis01:30

Apoptosis

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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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cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

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Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
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Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

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Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
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Related Experiment Video

Updated: Apr 28, 2026

Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches
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Caspase-2: the reinvented enzyme.

M Olsson1, J Forsberg1, B Zhivotovsky2

  • 1Division of Toxicology, Institute of Environmental Medicine, Karolinska Institutet, Stockholm, Sweden.

Oncogene
|June 3, 2014
PubMed
Summary

Caspase-2

Area of Science:

  • Molecular Biology
  • Oncology
  • Cellular Biology

Background:

  • Caspase-2 gene targeting in mouse models accelerates tumor formation, implicating it in tumor suppression.
  • This observed function raises questions about caspase-2's role, considering potential concurrent tumorigenic molecular perturbations.

Purpose of the Study:

  • To critically evaluate whether caspase-2 can be definitively classified as a tumor suppressor.
  • To explore the multifaceted roles of caspase-2 beyond its traditional association with apoptosis.

Main Methods:

  • Review of existing evidence on caspase-2 function in tumor formation and suppression.
  • Analysis of caspase-2's involvement in oxidative stress response, aging, and genome surveillance.
  • Examination of caspase-2's proposed role as a cell cycle checkpoint regulator.

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Related Experiment Videos

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Main Results:

  • Caspase-2's function extends beyond apoptosis, involving processes like oxidative stress response, aging, and genome surveillance.
  • The enzyme acts as a cell cycle checkpoint regulator through various mechanisms.
  • Evidence suggests caspase-2 is a versatile factor with complex roles in tumorigenesis.

Conclusions:

  • The traditional view of caspase-2 solely mediating apoptotic cell death is challenged.
  • Caspase-2's diverse functions indicate a complex interplay with cellular processes relevant to cancer.
  • Further research is needed to fully elucidate caspase-2's precise mechanisms and its net effect on tumor suppression.