Related Experiment Video
Updated: May 20, 2026

Evaluation of Caspase Activation to Assess Innate Immune Cell Death
Published on: January 20, 2023
Important role of β1-integrin in fucoidan-induced apoptosis via caspase-8 activation
Yumi Yamasaki1, Masao Yamasaki, Hirofumi Tachibana
1Department of Bioscience and Biotechnology, Faculty of Agriculture, Kyushu University, Fukuoka, Japan. yamasakiy@cc.miyazaki-u.ac.jp
Abstract:
Fucoidan induces apoptosis by activating caspase-8 in human MCF-7 breast cancer cells, but the detailed mechanism for this is not understood. We demonstrate here that fucoidan interacted with the cell surface, and silencing the β1-integrin gene expression inhibited fucoidan-induced apoptosis accompanied by caspase-8 activation. Fucoidan induced formation of the β1-integrin-caspase-8 complex. These data indicate that β1-integrin is an important factor for the cell-surface binding of fucoidan and plays an important role in fucoidan-induced apoptosis. Fucoidan also induced recruitment of caspase-8 to the β1-integrin intracellular domain, cleaved it into the activated protein by direct combination with β1-integrin, and induced apoptosis via the caspase cascade in MCF-7 cells.
Insights
Fucoidan triggers breast cancer cell death by binding to β1-integrin, activating caspase-8. This interaction is crucial for fucoidan-induced apoptosis in MCF-7 cells.
Area of Science:
- * Molecular Biology
- * Cell Biology
- * Cancer Research
Background:
- * Fucoidan is known to induce apoptosis in human MCF-7 breast cancer cells via caspase-8 activation.
- * The precise mechanism underlying fucoidan's apoptotic effect, particularly its cell surface interactions, remains unclear.
Purpose of the Study:
- * To elucidate the mechanism of fucoidan-induced apoptosis in MCF-7 cells.
- * To investigate the role of β1-integrin in fucoidan's interaction with the cell surface and subsequent apoptosis induction.
Main Methods:
- * Investigated fucoidan's interaction with MCF-7 cell surface.
- * Utilized gene silencing of β1-integrin to assess its role in apoptosis.
- * Examined the formation of β1-integrin-caspase-8 complexes.
- * Analyzed caspase-8 recruitment and cleavage associated with β1-integrin.
Main Results:
- * Fucoidan binds to the cell surface, and β1-integrin is essential for this interaction.
- * Silencing β1-integrin inhibited fucoidan-induced apoptosis and caspase-8 activation.
- * Fucoidan promoted the formation of a β1-integrin-caspase-8 complex.
- * Caspase-8 was recruited to and cleaved at the intracellular domain of β1-integrin, leading to its activation.
Conclusions:
- * β1-integrin is a critical mediator for fucoidan cell-surface binding and subsequent apoptosis induction.
- * Fucoidan activates apoptosis through a pathway involving β1-integrin and caspase-8 in MCF-7 cells.
- * This study reveals a novel mechanism for fucoidan's anti-cancer effects in breast cancer cells.
Related Concept Videos
The Extrinsic Apoptotic Pathway
Intracellular Signaling Affects Focal Adhesions
Some...
Caspases
The Intrinsic Apoptotic Pathway
Phagocytosis of Apoptotic Cells
Normal cells contain receptors that prevent them from being recognized by phagocytes.
Apoptosis
