Interaction between Hydrophilic Ionic Liquid and Phospholipid/Cholesterol Mixed Film.

Surface pressure (π)-area (A) isotherms were studied to analyze the interactions between a hydrophilic ionic liquid (IL) (ethyl(2-hydroxyethyl)dimethylammonium methanesulfonate) and a pure dipalmitoylphosphatidylcholine (DPPC) film or a DPPC-cholesterol mixed film. When the hydrophilic IL was added to an underlayer solution, the isotherm shifted toward higher areas. Intriguingly, when the hydrophilic IL was added, the packing of the film materials became loose and the elastic modulus decreased, resulting in increased flexibility. This phenomenon was most evident under a cholesterol mole fraction of 0.2. This composition resembles that of cell membranes, which typically comprise phospholipids and cholesterol, suggesting that this hydrophilic IL may be able to interact significantly with biological membranes.

TBP-like protein (TLP) represses myogenesis via inhibition of the myogenin promoter.

TBP-like protein (TLP) is one of the metazoan-restricted transcription factors participating in development and differentiation, though the molecular mechanism by which TLP regulates these processes remains unclear. In this study, we investigated the relationship between TLP and myogenesis of mouse C2C12 myoblasts. We found that TLP gene expression decreases during myogenic differentiation. Overexpression and knockdown of TLP revealed that the levels of muscle-specific myosin heavy chain and the myogenic transcription factor myogenin are downregulated by TLP. TLP inhibits the progression of morphological change from myoblasts to myotubes, thereby suppressing myogenesis. We further show that TLP represses the promoter activity of myogenin. The proximal AT-rich sequence of the myogenin promoter is responsible for TLP-mediated transcriptional repression. The results of this study suggest that TLP inhibits myogenesis through downregulation of the myogenin gene.