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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...

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Among all the organelles in an animal cell, only mitochondria have their own independent genomes. Animal mitochondrial DNA is a double-stranded, closed-circular molecule with around 20,000 base pairs. Mitochondrial DNA is unique in that one of its two strands, the heavy, or H, -strand is guanine rich, whereas the complementary strand is cytosine rich and called the light, or L, -strand. Compared to nuclear DNA, mitochondrial DNA has a very low percentage of non-coding regions and is marked by...

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The Equilibrium Binding Constant and Binding Strength

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Updated: Jan 25, 2026

Mitochondrial Ca2+ Retention Capacity Assay and Ca2+-triggered Mitochondrial Swelling Assay

Mitochondrial Ca2+ Retention Capacity Assay and Ca2+-triggered Mitochondrial Swelling Assay

Published on: May 1, 2018

Ceramides bind VDAC2 to trigger mitochondrial apoptosis.

Shashank Dadsena¹, Svenja Bockelmann¹, John G M Mina^2,3

¹Molecular Cell Biology Division, Department of Biology/Chemistry, University of Osnabrück, 49076, Osnabrück, Germany.

Nature Communications

|April 25, 2019

Summary

This summary is machine-generated.

This study identifies voltage-dependent anion channels (VDAC1 and VDAC2) as key mitochondrial proteins that bind ceramides. VDAC2 is crucial for ceramide-induced apoptosis, offering a molecular basis for cancer cell death.

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Saturated Fatty Acids Induce Ceramide-associated Macrophage Cell Death

Saturated Fatty Acids Induce Ceramide-associated Macrophage Cell Death

Published on: October 31, 2017

Area of Science:

Mitochondrial biology
Lipid signaling
Cancer cell death mechanisms

Background:

Ceramides are recognized as tumor suppressor lipids that induce apoptosis via mitochondria.
The precise molecular mechanisms by which ceramides trigger cell death remain largely undefined.

Purpose of the Study:

To elucidate the molecular targets of ceramides within mitochondria.
To understand the role of these targets in ceramide-mediated apoptosis and anti-neoplastic activity.

Main Methods:

Utilized a photoactivatable ceramide probe to identify binding proteins.
Employed coarse-grain molecular dynamics simulations to model ceramide-channel interactions.
Performed genetic manipulations (gene removal, residue substitution) in human colon cancer cells.

Main Results:

Identified Voltage-Dependent Anion Channels 1 and 2 (VDAC1 and VDAC2) as mitochondrial ceramide-binding proteins.
Discovered a specific ceramide binding site within VDACs involving a membrane-buried glutamate residue.
Demonstrated that loss of VDAC2, but not VDAC1, confers resistance to ceramide-induced apoptosis in cancer cells.

Conclusions:

VDAC2 acts as a direct effector in ceramide-mediated apoptosis.
Provides a molecular framework for ceramide's anti-neoplastic effects, highlighting VDAC2's critical role.
Uncovers a novel mechanism for regulating programmed cell death in cancer.