Study of the motion artefacts of skin-mounted inertial sensors under different attachment conditions

A common problem shared by accelerometers, inertial sensors and any motion measurement method based on skin-mounted sensors is the movement of the soft tissues covering the bones. The aim of this work is to propose a method for the validation of the attachment of skin-mounted sensors. A second-order (mass-spring-damper) model was proposed to characterize the behaviour of the soft tissue between the bone and the sensor. Three sets of experiments were performed. In the first one, different procedures to excite the system were evaluated to select an adequate excitation stimulus. In the second one, the selected stimulus was applied under varying attachment conditions while the third experiment was used to test the model. The heel drop was chosen as the excitation method because it showed lower variability and could discriminate between different attachment conditions. There was, in agreement with the model, a trend to increase the natural frequency of the system with decreasing accelerometer mass. An important result is the development of a standard procedure to test the bandwidth of skin-mounted inertial sensors, such as accelerometers mounted on the skin or markers heavier than a few grams.     

Roles of phosphoinositide-dependent kinase-1 in α1B-adrenoceptor phosphorylation and desensitization

The role of phosphoinositide-dependent protein kinase-1 (PDK-1) activity on α(1B)-adrenoceptor phosphorylation and function was explored using pharmacological inhibitors and expression of a dominant-negative mutant of this enzyme. Noradrenaline-, phorbol myristate acetate-, lysophosphatidic acid- and epidermal growth factor-mediated α(1B)-adrenoceptor phosphorylation were markedly reduced by the two inhibitors used: UCN-01 [(7-hydroxystaurosporine; (3R*,8S*, 9R*, 10R*,12R*)-2,3,9,10,11,12-hexahydro-3-hydroxy-9-methoxy-8-methyl-10-(methylamino)-8,12-epoxy-1H, 8H-2,7b,12a-triazadibenzo[a,g]-cyclonona[cde]triden-1-one)] and OSU-03012 [(2-amino-N-[4-[5-(2-phenanthrenyl)-3-trifluoromethyl)-1H-pyrazol-1-yl]phenyl]-acetamide)]. A similar effect was observed in cells expressing a PDK-1 dominant-negative mutant. Phosphorylated PDK-1 (S241) and protein kinase C α (T497) were associated with cell membranes in the basal state which increased in response to the hormonal stimuli mentioned previously. UCN-01 essentially abolished phospho-PDK-1 membrane-association and markedly attenuated that of protein kinase C α. Consistent with the findings, UCN-01 reduced lysophosphatidic acid- and epidermal growth factor-induced α(1B-)adrenoceptor desensitization. Our data suggest that PDK-1 plays a permissive role in α(1B)-adrenoceptor desensitization and phosphorylation and participates in the formation of signaling complexes, which delicately modulate receptor function and regulation.