Tmem86b, an integral membrane protein of the YhhN family, functions as a lysoplasmalogenase. It catalyzes the hydrolytic cleavage of the vinyl-ether bond of lysoplasmalogen, yielding fatty aldehyde and glycerophospho-ethanolamine or glycerophospho-choline. This activity is crucial in the catabolism of plasmalogens, a distinct subclass of glycerophospholipids with unique structural features [1,2,4].

In mice, global and hepatocyte-specific knockout of Tmem86b (Tmem86b KO mice) using cre-loxP technology revealed its role in plasmalogen catabolism. Tmem86b KO mice showed significantly elevated levels of plasmalogens (alkenylphosphatidylethanolamine and alkenylphosphatidylcholine) and lysoplasmalogens in the plasma, liver, and natural killer cells. Hepatocyte-specific knockout mice also had increased plasmalogen levels in the plasma and liver. These results suggest that Tmem86b ablation leads to elevated plasmalogen levels in certain tissues and cells, enhancing our understanding of plasmalogen metabolism regulation [3].

In conclusion, Tmem86b plays a vital role in plasmalogen catabolism. The Tmem86b KO mouse models have provided valuable insights into the regulatory mechanisms of plasmalogen metabolism, highlighting the potential of targeting Tmem86b to therapeutically raise plasmalogen levels, which may be relevant for conditions associated with plasmalogen deficiencies [3].