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The Intrinsic Apoptotic Pathway

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...

Phagocytosis of Apoptotic Cells

Phagocytosis of Apoptotic Cells

Cells undergoing apoptosis form apoptotic bodies that must be removed immediately to prevent inflammation, autoimmune diseases, and necrosis. Phagocytosis is carried out by professional phagocytes such as macrophages or immature dendritic cells. Non-professional phagocytes such as epithelial cells and fibroblasts also take part in this process; however, they are not as effective as professional phagocytes.
Normal cells contain receptors that prevent them from being recognized by phagocytes.

The Extrinsic Apoptotic Pathway

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...

Protein-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

Apoptosis

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.

Caspases

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.

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Related Experiment Video

Updated: May 23, 2026

Detection and Isolation of Apoptotic Bodies to High Purity

Detection and Isolation of Apoptotic Bodies to High Purity

Published on: August 12, 2018

Interface of apoptotic protein complexes has distinct properties.

Pralay Mitra¹, Riddhiman Dhar, Debnath Pal

¹Supercomputer Education and Research Centre, Bangalore, India Bioinformatics Centre, Indian Institute of Science, Bangalore, India.

In Silico Biology

|March 21, 2012

Summary

This study reveals that apoptotic protein complexes have distinct interface properties, featuring more fragmented interfaces and unique secondary structural preferences compared to general protein complexes. Key residues like Arg, Met, and Asp play crucial roles in regulating apoptosis.

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Identification of Intracellular Signaling Events Induced in Viable Cells by Interaction with Neighboring Cells Undergoing Apoptotic Cell Death

Identification of Intracellular Signaling Events Induced in Viable Cells by Interaction with Neighboring Cells Undergoing Apoptotic Cell Death

Published on: December 27, 2016

Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Apoptosis, a programmed cell death, is vital for multicellular organism development and health.
Understanding the molecular mechanisms of apoptosis is crucial for disease research.

Purpose of the Study:

To investigate if interface properties of apoptotic protein complexes differ from general protein complexes.
To identify key residues and physico-chemical attributes involved in regulating apoptosis.

Main Methods:

Comparative analysis of interface properties (size, complementarity, hydrogen bonding, hydrophobicity) between apoptotic and general protein complexes.
Statistical analysis of amino acid frequencies at protein interfaces.

Main Results:

Apoptotic protein complexes exhibit similar overall interface properties but tend to have more fragmented interfaces and distinct secondary structural preferences.
Amino acids Arg, Met, and Asp were identified as important functional residues, with Met showing a unique role.

Conclusions:

Physico-chemical attributes at protein interfaces significantly influence apoptosis regulation.
Fragmented interfaces and specific amino acid compositions are characteristic of apoptotic protein complexes.