Various types of seaweed are potential functional foods as they contain multiple bioactive compounds. N-Methyltaurine (NMT) is a taurine derivative metabolite found in a type of red algae. The functional actions of NMT in mammalian animals have not been investigated, but the parent compound, taurine, possesses a variety of cellular actions. To explore the beneficial role of NMT in animals, the present study analyzed the effect of NMT against glucocorticoid-induced skeletal muscle atrophy. Glucocorticoids are one of the major causes of pathological muscle atrophy. Initially, we assessed the bioavailability of ingested NMT by determining its concentration in mouse blood. The bioavailability of orally administered NMT was found to be 96.1% that of intravenously administered NMT. Mice maintained on water containing 0.5% NMT for several days lead to the distribution of the taurine derivative to various tissues, including skeletal muscles. Like taurine, the delivery of NMT to skeletal muscles or myoblast cells is cytoprotective. The treatment with NMT prevents dexamethasone-induced atrophy of myotubes derived from C2C12 cells. Similarly, the addition of 0.5% NMT to drinking water attenuates dexamethasone-mediated reduction in muscle mass of the treated mice. The present study supports the hypothesis that orally administered NMT partially reverses skeletal muscle atrophy.

Taurine is a compatible osmolyte that infers stability to proteins. Recent studies have revealed that liquid-liquid phase separation (LLPS) of proteins underlie the formation of membraneless organelles in cells. In the present study, we evaluated the role of taurine on LLPS of hen egg lysozyme. We demonstrated that taurine decreases the turbidity of the polyethylene glycol-induced crowding solution of lysozyme. We also demonstrated that taurine attenuates LLPS-dependent cloudiness of lysozyme solution with 0.5 or 1M NaCl at a critical temperature. Moreover, we observed that taurine inhibits LLPS formation of a heteroprotein mix solution of lysozyme and ovalbumin. These data indicate that taurine can modulate the formation of LLPS of proteins..

Taurine is a compatible osmolyte that infers stability to proteins. Recent studies have revealed that liquid-liquid phase separation (LLPS) of proteins underlie the formation of membraneless organelles in cells. In the present study, we evaluated the role of taurine on LLPS of hen egg lysozyme. We demonstrated that taurine decreases the turbidity of the polyethylene glycol-induced crowding solution of lysozyme. We also demonstrated that taurine attenuates LLPS-dependent cloudiness of lysozyme solution with 0.5 or 1M NaCl at a critical temperature. Moreover, we observed that taurine inhibits LLPS formation of a heteroprotein mix solution of lysozyme and ovalbumin. These data indicate that taurine can modulate the formation of LLPS of proteins.