Implementation of the scale factor balance on two pairs of quartz-flexure capacitive accelerometers by trimming bias voltage.

Gravity gradient measurement makes use of the difference between the outputs of pairs of linear accelerometers, which results in cancelling out the common mode accelerations caused by mounting platform and external environment. One of the key technologies is to match the acceleration-to-voltage or acceleration-to-current transfer functions of the pairs of the accelerometers to an extremely high degree of accuracy. The differential signals then make the gravity gradients observable. By using two pairs of the quartz-flexure accelerometers with a capacitive sensing and electrostatic closed-loop control, the electrostatic control bias voltages were trimming remotely and automatically in real time. Each pair of accelerometers was matched individually and then all four accelerometers were finally re-balanced. The experimental results show that the consistency of five digits is achieved at a noise level of ~5×10(-8) g/√Hz (1 g ≈ 9.8 m/s(2)) and the scale factors ranging from 0.25 to 0.32 V/mg. Further improvement to the achieved level of matching is limited by the intrinsic noise of the accelerometers used.

Protein kinase C-mediated tyrosine phosphorylation of paxillin and focal adhesion kinase requires cytoskeletal integrity and is uncoupled to mitogen-activated protein kinase activation in human hepatoma cells.

Treatment of cultured human hepatoma HepG2 cells with the protein kinase C (PKC) activator, 12-O-tetradecanoylphorbol-13-acetate (TPA), results in an increase in tyrosine phosphorylation of several proteins, including the focal adhesion kinase (FAK) and paxillin using anti-phosphotyrosine Western blotting and immunoprecipitation. However, when cells are in suspension or in the presence of cytochalasin D which disrupts the intracellular network of actin microfilaments, TPA loses its ability to stimulate tyrosine phosphorylation of FAK and paxillin but it still activates mitogen-activated protein kinase (MAPK) and induces PKC translocation from cytosol to the membrane in HepG2 cells. On the other hand, PD98059, a specific inhibitor of mitogen-activated protein kinase kinase, blocks TPA-induced MAPK activation but has no effect on TPA-induced tyrosine phosphorylation. Our findings suggest that TPA-induced tyrosine phosphorylation of FAK and paxillin in human hepatoma cells is PKC dependent and requires the integrity of the cell cytoskeleton but is uncoupled to the signal transduction pathway of PKC leading to the translocation of PKC and MAPK activation.