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Activation of apoptosis and its inhibition
1Department of Immunology and Rheumatology, Merck Research Laboratories, Rahway, New Jersey 07065, USA. douglas_miller@merck.com
Abstract:
The induction of apoptosis, or controlled cell death, by various stimuli has been shown to activate a cascade of endoproteases, called caspases, that cleave numerous cellular proteins necessary for cellular homeostasis. This review discusses this family of proteases together with a variety of mammalian and viral regulatory proteins that act to control this activation.
Insights
Apoptosis, or programmed cell death, triggers caspases, which are proteases that break down cellular proteins. This review covers caspases and their regulators in mammals and viruses.
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Biology
Background:
- Apoptosis is a crucial biological process involving controlled cell death.
- Various stimuli can initiate apoptosis, leading to cellular dismantling.
- This process involves a complex cascade of molecular events.
Purpose of the Study:
- To review the family of proteases known as caspases.
- To discuss the regulatory proteins that control caspase activation.
- To provide an overview of mammalian and viral caspase regulators.
Main Methods:
- Literature review of scientific publications on apoptosis and caspases.
- Analysis of the roles of caspases in cellular protein cleavage.
- Examination of regulatory mechanisms involving mammalian and viral proteins.
Main Results:
- Caspases are key endoproteases activated during apoptosis.
- These proteases cleave essential cellular proteins, disrupting homeostasis.
- A variety of regulatory proteins, both endogenous and viral, modulate caspase activity.
Conclusions:
- Caspase activation is central to the execution of apoptosis.
- Understanding caspase regulation is vital for comprehending cell death pathways.
- Regulatory proteins play critical roles in fine-tuning apoptosis by controlling caspases.