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Adenofection: A Method for Studying the Role of Molecular Chaperones in Cellular Morphodynamics by Depletion-Rescue Experiments

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A Bioengineering Strategy to Control ADAM10 Activity in Living Cells.

Francesco Pastore¹, Martina Battistoni¹, Raimondo Sollazzo¹

¹Department of Neuroscience, Università Cattolica del Sacro Cuore, 00168 Rome, Italy.

International Journal of Molecular Sciences

|January 21, 2023

Summary

This summary is machine-generated.

Researchers developed a bioengineering strategy to control ADAM10 activity, crucial for Alzheimer's disease (AD) research. This method precisely regulates ADAM10 shedding, promoting non-amyloidogenic APP cleavage and increasing neuroprotective sAPPα production for potential AD gene therapy.

Keywords:

APP Alzheimer TEV cytosolic domain engineered protein prodomain

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Area of Science:

Biochemistry
Molecular Biology
Neuroscience

Background:

ADAM10 is a cell surface protease involved in physiological processes, with dysregulation linked to Alzheimer's disease (AD).
Mechanisms of ADAM10 activation and its role in protein ectodomain shedding are not fully understood.
Precise control over ADAM10 activity is needed to study its cleavage mechanisms and develop therapeutic applications.

Purpose of the Study:

To develop a bioengineering strategy for spatiotemporal control of ADAM10 activity.
To investigate the roles of prodomain and cytosolic tail cleavage in ADAM10 activation.
To assess the potential of this strategy for AD gene therapy by modulating APP processing.

Main Methods:

Engineered ADAM10 analogs with Tobacco Etch Virus protease (TEV) cleavage sites (TEVcs).
Utilized TEV protease to induce specific cleavage of the prodomain and cytosolic tail.
Generated ADAM10 with minimal constitutive activity, inducible by TEV or chemically activatable TEV.

Main Results:

TEV-mediated prodomain removal alone did not activate ADAM10.
Cleavage of the cytosolic domain significantly increased ADAM10 activity.
Engineered ADAM10 showed increased activity upon TEV induction or chemical activation.
The strategy promoted α-secretase activity, leading to non-amyloidogenic cleavage of APP and increased sAPPα production.

Conclusions:

A novel bioengineering approach allows for precise, spatiotemporal control of ADAM10 activity in living cells.
Cytosolic tail cleavage is a key regulatory step for ADAM10 proteolytic function.
This strategy offers a potential next-generation gene therapy for AD by enhancing neuroprotective pathways.