DBU-intercalated γ-titanium phosphate as a latent thermal catalyst in the reaction of glycidyl phenyl ether (GPE) and hexahydro-4-methylphthalic anhydride (MHHPA).

The capabilities and performance of γ-titanium phosphate (γ-TiP) with 1,8-diazabicyclo[5.4.0]undec-7-ene (DBU) as a latent thermal catalyst were investigated by the copolymerization of glycidyl phenyl ether (GPE) and hexahydro-4-methylphthalic anhydride (MHHPA) at different temperatures for a period of one hour. Polymerization was not observed until the reactants were heated to 100 °C. Upon increasing the temperature to 120 °C, the conversion in the presence of γ-TiP·DBU as a catalyst showed 98% conversion in 1 h. The thermal stability of GPE and MHHPA reacted in the presence of γ-TiP·DBU at 40 °C for 144 h resulted in less than 7% conversion of GPE. The conversion of GPE did not show a significant increase at 40 °C.

Slit3 regulates cell motility through Rac/Cdc42 activation in lipopolysaccharide-stimulated macrophages.

Three slit genes, slit1 to slit3, have been cloned to date. Slit1 and slit2 act as chemorepellent factors for axon guidance. Slit3 is involved in the formation of the diaphragm and kidney during embryogenesis. However, its molecular function remains unclear. We found that slit3 expression was induced by lipopolysaccharide (LPS)-stimulation in macrophages and that it was localized in the mitochondria and along the plasma membrane. Silencing of slit3 expression by RNA interference reduced cell motility and Rac/Cdc42 activation. These results suggest that slit3 functions as an intracellular signaling molecule for cell motility as part of the LPS-induced signaling cascade.