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Biochemical processing of E-cadherin under cellular stress
Steven H Keller1, Sanjay K Nigam
1Department of Medicine, University of California, San Diego, CA 92103-8382, USA. shkeller@ucsd.edu
Biochemical and Biophysical Research Communications
|July 16, 2003
Summary
Cellular stress from antimycin A and deoxyglucose activates caspase-mediated pathways, cleaving E-cadherin. This caspase activation leads to the dissolution of adherens junctions, crucial for epithelial integrity.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- E-cadherin is a key cell adhesion molecule in adherens junctions, vital for epithelial tissue integrity.
- Understanding E-cadherin processing under cellular stress is crucial for comprehending tissue homeostasis and disease.
Purpose of the Study:
- To characterize the proteolytic cleavage pathways of E-cadherin in Madin-Darby canine kidney (MDCK) cells under cellular stress.
- To investigate the role of caspases in E-cadherin cleavage during antimycin A and deoxyglucose treatment.
Main Methods:
- MDCK cells were treated with antimycin A and deoxyglucose to induce cellular stress.
- E-cadherin cleavage fragments were analyzed, and the effect of caspase inhibitors (DEVD-CHO) was assessed.
Main Results:
- Antimycin A and deoxyglucose treatment activated caspase-mediated pathways, leading to E-cadherin cleavage.
- E-cadherin was cleaved into two major fragments, consistent with caspase-3 activity.
- Caspase inhibition prevented E-cadherin cleavage and C-terminal fragment deposition.
Conclusions:
- Caspase activation initiates E-cadherin cleavage and adherens junction dissolution under cellular stress.
- This mechanism highlights the role of apoptosis pathways in regulating cell-cell adhesion during stress.