What can cause a decrease in pseudocholinesterase activity when used in anesthesia?

Pseudocholinesterase is an enzyme that plays a critical role in the breakdown of certain anesthetic agents, especially succinylcholine and other neuromuscular blocking drugs. When considering factors that can decrease pseudocholinesterase activity, echothiophate stands out as a key agent.

Echothiophate is an irreversible inhibitor of acetylcholinesterase and pseudocholinesterase. It works by binding to these enzymes and preventing them from functioning properly. This inhibition leads to a decrease in the activity of pseudocholinesterase, which directly impacts the metabolism of succinylcholine, potentially prolonging its neuromuscular blocking effects. This characteristic makes echothiophate particularly relevant in this context, as anesthesiologists must be aware of its effects on enzyme activity when planning anesthesia care.

In contrast, other agents listed, such as propofol, thiopental, and lidocaine, do not have a significant impact on pseudocholinesterase activity in clinically relevant ways. Propofol is a common anesthetic that does not affect pseudocholinesterase levels. Thiopental is a barbiturate used for induction of anesthesia but does not inhibit pseudocholinesterase