Kinect-Based Correction of Overexposure Artifacts in Knee Imaging with C-Arm CT Systems.

Objective. To demonstrate a novel approach of compensating overexposure artifacts in CT scans of the knees without attaching any supporting appliances to the patient. C-Arm CT systems offer the opportunity to perform weight-bearing knee scans on standing patients to diagnose diseases like osteoarthritis. However, one serious issue is overexposure of the detector in regions close to the patella, which can not be tackled with common techniques. Methods. A Kinect camera is used to algorithmically remove overexposure artifacts close to the knee surface. Overexposed near-surface knee regions are corrected by extrapolating the absorption values from more reliable projection data. To achieve this, we develop a cross-calibration procedure to transform surface points from the Kinect to CT voxel coordinates. Results. Artifacts at both knee phantoms are reduced significantly in the reconstructed data and a major part of the truncated regions is restored. Conclusion. The results emphasize the feasibility of the proposed approach. The accuracy of the cross-calibration procedure can be increased to further improve correction results. Significance. The correction method can be extended to a multi-Kinect setup for use in real-world scenarios. Using depth cameras does not require prior scans and offers the possibility of a temporally synchronized correction of overexposure artifacts. To achieve this, we develop a cross-calibration procedure to transform surface points from the Kinect to CT voxel coordinates.

A cell-permeable fusion protein based on Clostridium botulinum C2 toxin for delivery of p53 tumorsuppressor into cancer cells.

Genetically engineered bacterial protein toxins are attractive systems for delivery of exogenous proteins into the cytosol of mammalian cells. The binary C2 toxin from C. botulinum has emerged as powerful delivery vehicle, which rests on its binding/translocation component C2IIa and the genetically modified adaptor domain C2IN that act in concert to trigger cell uptake. The p53 tumor suppressor protein has a crucial function in suppressing carcinogenesis and is frequently inactivated by diverse mechanisms in human tumor cells. Therefore, we constructed a C2IN-p53 fusion protein, which is internalized into cancer cells by C2IIa. To this end, the C2IN-p53 fusion construct was overexpressed in E. coli with good solubility, purified by heparin affinity chromatography and protein identity was confirmed by immunoblotting. We demonstrated that the fusion protein is capable of binding to the p53 consensus-DNA with high affinity in a p53-specific manner in vitro. Next, the internalization of C2IN-p53 was monitored in HeLa cells by cell fractionation and immunoblot analysis, which revealed a C2IIa-mediated translocation of the fusion protein into the cytosol. The uptake was also shown in A549 and Saos-2 cells with similar efficiency. These findings were further corroborated by confocal immunofluorescence analyses of C2IN-p53/C2IIa-treated HeLa and A549 cells, displaying predominantly cytoplasmic localization of the fusion construct.