A recent study found that an amino acid, whose function in the body was previously unknown, acts as a seizure inhibitor in mice. These findings could have an important impact on the development of anti-seizure therapies in epilepsy patients.

Amino acids are the building blocks of proteins in the body that are necessary for survival. There are 20 essential amino acids. Humans can produce 10 of these, but the other half must be supplied by food. Lack of these essential amino acids can cause the degradation of the body’s proteins.

The study shows that D-leucine, an amino acid found in many foods and some bacteria, interrupts prolonged seizures—a symptom of the condition status epilepticus. In fact, it was just as effective as diazepam, the preferred epilepsy drug used to treat patients in the midst of a seizure, without any of the sedative side effects from the drug. Researchers induced seizures in mice and compared the abilities of D-leucine and diazepam to terminate them. D-leucine halted the seizures about 15 minutes earlier than the drug. Mice treated with D-leucine also displayed an earlier return to normal behavior and did not experience the drowsiness and sedative effects that were seen in mice treated with diazepam.

 Molecular structure of the amino acid leucine

Image Source: Martin McCarthy

The researchers also discovered that D-leucine works differently from other seizure treatments. Experiments conducted to measure D-leucine’s interaction with nerve receptors associated with cell-to-cell signaling and seizures found that D-leucine does not interact with any of the signaling pathways that play a role in controlling seizure activity. This could be very beneficial to people with drug-resistant forms of epilepsy, or recalcitrant epilepsy—almost one-third of epilepsy patients. This new treatment approach could allow people with this form of the disorder to be able to control their seizures.

Feature Image Source: Epilepsy by The Clear Communication People

Karina Kak

Author Karina Kak

UCSD alumnus. LinkedIn

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