Determination of the total surface area in carbonaceous adsorbents by the selective adsorption of caffeine from water

The selective adsorption of caffeine from aqueous solutions onto the surface of carbonaceous materials can be monitored calorimetrically. The study of carbon blacks and active carbons shows that the proportionality factor is hi = - 112 ± 15 mJ/m2. The method leads to the total surface area of carbonaceous materials with pores wider than 0.6 - 0.7 nm. It is also shown that the surface area derived from CO2 adsorption is in good agreement with the value of the micropore surface area

Rap1 Activation in Collagen Phagocytosis Is Dependent on Nonmuscle Myosin II-A

Rap1 enhances integrin-mediated adhesion but the link between Rap1 activation and integrin function in collagen phagocytosis is not defined. Mass spectrometry of Rap1 immunoprecipitates showed that the association of Rap1 with nonmuscle myosin heavy-chain II-A (NMHC II-A) was enhanced by cell attachment to collagen beads. Rap1 colocalized with NM II-A at collagen bead-binding sites. There was a transient increase in myosin light-chain phosphorylation after collagen-bead binding that was dependent on myosin light-chain kinase but not Rho kinase. Inhibition of myosin light-chain phosphorylation, but not myosin II-A motor activity inhibited collagen-bead binding and Rap activation. In vitro binding assays demonstrated binding of Rap1A to filamentous myosin rods, and in situ staining of permeabilized cells showed that NM II-A filaments colocalized with F-actin at collagen bead sites. Knockdown of NM II-A did not affect talin, actin, or β1-integrin targeting to collagen beads but targeting of Rap1 and vinculin to collagen was inhibited. Conversely, knockdown of Rap1 did not affect localization of NM II-A to beads. We conclude that MLC phosphorylation in response to initial collagen-bead binding promotes NM II-A filament assembly; binding of Rap1 to myosin filaments enables Rap1-dependent integrin activation and enhanced collagen phagocytosis

Involvement of the Cytoskeleton in Controlling Leading-Edge Function during Chemotaxis

Cells activate signaling pathways at the site closest to the chemoattractant source that lead to pseudopod formation and directional movement up the gradient. We demonstrate that cytoskeletal components required for cortical tension, including MyoII and IQGAP/cortexillins help regulate the level and timing of leading-edge pathways