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Published on: August 6, 2020
Captopril modulates acetylcholinesterase in human keratinocytes
Adone Baroni1, Elisabetta Buommino, Eleonora Ruocco
1Department of Dermatology, Second University of Naples, Italy.
Captopril, an ACE-inhibitor, increases acetylcholinesterase in human keratinocytes, degrading acetylcholine and reducing its secretion. This suggests ACE-inhibitor-induced acantholysis may involve altered acetylcholine levels.
Area of Science:
- Dermatology
- Cell Biology
- Pharmacology
Background:
- Human keratinocytes produce non-neuronal acetylcholine, a signaling molecule regulating cellular functions.
- The keratinocyte acetylcholine axis involves synthesis and degradation enzymes and receptors.
- Acetylcholine regulates keratinocyte proliferation, adhesion, motility, and desmosomal contact.
Purpose of the Study:
- To investigate the effect of captopril, an angiotensin-converting enzyme (ACE)-inhibitor, on acetylcholinesterase (AChE) and acetylcholine secretion in human keratinocytes.
- To explore the potential link between ACE-inhibitors, acetylcholine levels, and acantholysis.
Main Methods:
- Analysis of acetylcholinesterase levels in HaCat and NHEK cells using RT-PCR and Western blotting.
- Evaluation of captopril's effect on acetylcholinesterase activity.
- Assessment of acetylcholine secretion in response to captopril treatment.
Main Results:
- Captopril significantly up-regulates acetylcholinesterase expression in human keratinocytes.
- Increased acetylcholinesterase leads to enhanced degradation of acetylcholine.
- Captopril treatment results in reduced acetylcholine secretion from keratinocytes.
Conclusions:
- ACE-inhibitors like captopril alter the keratinocyte acetylcholine axis by increasing AChE.
- The observed changes in acetylcholine degradation and secretion may contribute to acantholysis.
- Altered acetylcholine levels are a potential mechanism underlying ACE-inhibitor-induced skin conditions.
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