AI Article Synopsis
- Angiotensin-converting enzyme (ACE) plays a key role in regulating blood pressure and is found in high levels in the brain's striatal tissue, but its specific functions there are not well understood.
- * Researchers discovered that ACE breaks down the enkephalin peptide Met-enkephalin-Arg-Phe in the nucleus accumbens of mice, influencing opioid receptor activation and affecting glutamate release.
- * Inhibiting ACE did not provide a rewarding experience by itself, but it diminished addiction potential from fentanyl and improved social interaction, suggesting potential benefits for enhancing opioid signaling therapeutically while reducing addiction risks.
Article Abstract
Angiotensin-converting enzyme (ACE) regulates blood pressure by cleaving angiotensin I to produce angiotensin II. In the brain, ACE is especially abundant in striatal tissue, but the function of ACE in striatal circuits remains poorly understood. We found that ACE degrades an unconventional enkephalin heptapeptide, Met-enkephalin-Arg-Phe, in the nucleus accumbens of mice. ACE inhibition enhanced µ-opioid receptor activation by Met-enkephalin-Arg-Phe, causing a cell type-specific long-term depression of glutamate release onto medium spiny projection neurons expressing the Drd1 dopamine receptor. Systemic ACE inhibition was not intrinsically rewarding, but it led to a decrease in conditioned place preference caused by fentanyl administration and an enhancement of reciprocal social interaction. Our results raise the enticing prospect that central ACE inhibition can boost endogenous opioid signaling for clinical benefit while mitigating the risk of addiction.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9233526 | PMC |
| http://dx.doi.org/10.1126/science.abl5130 | DOI Listing |
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