Dealing with the Effects of Sensor Displacement in Wearable Activity Recognition

Most wearable activity recognition systems assume a predefined sensor deployment that remains unchanged during runtime. However, this assumption does not reflect real-life conditions. During the normal use of such systems, users may place the sensors in a position different from the predefined sensor placement. Also, sensors may move from their original location to a different one, due to a loose attachment. Activity recognition systems trained on activity patterns characteristic of a given sensor deployment may likely fail due to sensor displacements. In this work, we innovatively explore the effects of sensor displacement induced by both the intentional misplacement of sensors and self-placement by the user. The effects of sensor displacement are analyzed for standard activity recognition techniques, as well as for an alternate robust sensor fusion method proposed in a previous work. While classical recognition models show little tolerance to sensor displacement, the proposed method is proven to have notable capabilities to assimilate the changes introduced in the sensor position due to self-placement and provides considerable improvements for large misplacements.

Expression and activity profiles of DPP IV/CD26 and NEP/CD10 glycoproteins in the human renal cancer are tumor-type dependent

Background: Cell-surface glycoproteins play critical roles in cell-to-cell recognition, signal transduction and regulation, thus being crucial in cell proliferation and cancer etiogenesis and development. DPP IV and NEP are ubiquitous glycopeptidases closely linked to tumor pathogenesis and development, and they are used as markers in some cancers. In the present study, the activity and protein and mRNA expression of these glycoproteins were analysed in a subset of clear-cell (CCRCC) and chromophobe (ChRCC) renal cell carcinomas, and in renal oncocytomas (RO). Methods: Peptidase activities were measured by conventional enzymatic assays with fluorogen-derived substrates. Gene expression was quantitatively determined by qRT-PCR and membrane-bound protein expression and distribution analysis was performed by specific immunostaining. Results: The activity of both glycoproteins was sharply decreased in the three histological types of renal tumors. Protein and mRNA expression was strongly downregulated in tumors from distal nephron (ChRCC and RO). Moreover, soluble DPP IV activity positively correlated with the aggressiveness of CCRCCs (higher activities in high grade tumors). Conclusions: These results support the pivotal role for DPP IV and NEP in the malignant transformation pathways and point to these peptidases as potential diagnostic markers.