Associations between pretreatment physical performance tests and treatment complications in patients with non-small cell lung cancer: A systematic review.

This systematic review evaluated which outcome variables and cut-off values of pretreatment exercise tests are associated with treatment complications in patients with stage I-III non-small cell lung cancer (NSCLC). PRISMA and Cochrane guidelines were followed. A total of 38 studies with adult patients undergoing treatment for stage I-III NSCLC who completed pretreatment exercise tests, and of whom treatment-related complications were recorded were included. A lower oxygen uptake at peak exercise amongst several other variables on the cardiopulmonary exercise test and a lower performance on field tests, such as the incremental shuttle walk test, stair-climb test, and 6-minute walk test, were associated with a higher risk for postoperative complications and/or postoperative mortality. Cut-off values were reported in a limited number of studies and were inconsistent. Due to the variety in outcomes, further research is needed to evaluate which outcomes and cut-off values of physical exercise tests are most clinically relevant.

Developing a parametric ear model for auricular reconstruction: a new step towards patient-specific implants.

INTRODUCTION: Ear reconstruction is a tedious and demanding surgical procedure and the implant framework used is essential for the esthetic result. The outcome of a reconstructed ear, however, is not necessarily limited to the implant shape but rather to the available options of transplantable tissue for coverage. Apart from the visual aesthetics, ear reconstruction subsequently also requires implant dimensions to be adapted to the surgical possibilities. In this article, we have brought different disciplines together to develop a customizable ear model for 3D printing of ear implants. MATERIAL AND METHODS: Computed tomography (CT) scans were made of 4 human cadaver ears before and after soft tissue dissection using a Discovery 750 High Definition Freedom Edition scanner (GE, Milwaukee, WI, USA) and subsequently converted into an STL data set using Mimics Software (Materialise, Leuven, Belgium). These scans were then used to develop a fully adjustable parametric model based on the essential ear anatomy using Rhinoceros and Grasshopper software. RESULTS: To determine the quality of the developed models, directed Hausdorff distance (DHD) was applied as the basis for measuring the similarity between the parametric model and the ear cartilage scanning data. Two methods were used. The mean directed Haussdorff distance (MDHD) was calculated based on the distribution of point sets showing an average similarity of 0.8 mm (±0.05 mm). The mean similarity coefficient (SC) of the model and scan surfaces was 94% with a 2-mm threshold. CONCLUSION: This study shows that a parametric standard model could be used as a feasible method to generate custom implants based on existing ear images.

Study of high-voltage breakdown and material consumption in spark-source mass spectrometry and their significance in analytical applications.

The breakdown voltage has been found to be dependent on the gap width between the electrodes and on the melting point of the sample elements in spark-source mass-spectrometry (SSMS). The number of discharges per pulse train and the time required to reach the first discharge depend only on the chosen breakdown voltage. The spark gap is proportional to the "radius" of the volume sampled (for a given element) and this radius is linearly related to the reciprocal of the melting point of the elements (23 different elements, metals or semiconductors), when fixed spark-parameters are used. The effect of electrode temperature on material consumption can be qualitatively explained by a fictive increase or decrease in melting point of the element. Knowledge of the relations between the different spark and instrumental parameters and the volume or weight of sample consumed can be applied to the study of the homogeneity of samples, to in-depth analysis by SSMS and to the analysis of microsamples.

Identification of cell surface dipeptidylpeptidase IV in human fibroblasts.

An antigen with dipeptidylpeptidase IV activity was identified at the surface of normal human fibroblasts. Hydrophobic interaction electrophoresis in phenyl-Sepharose revealed that the enzyme contained a hydrophobic domain, while lactoperoxidase-catalysed iodination with 125I of living cells indicated that the protein was located at the cell surface. Crossed immunoelectrophoresis with specific antibodies of acid-extracted or papain-treated cells showed a shift of the dipeptidylpeptidase IV peak to a faster mobility. The molecular properties of the fibroblast enzyme were clearly different from those described for dipeptidylpeptidase IV from other tissues and species. Fibroblast dipeptidylpeptidase IV contained two different disulphide-linked subunits, of apparent Mr values 125000 and 135000 (denatured and reduced). In gel filtration, an Mr of about 400000 was observed for the unreduced molecule. The enzymic properties of fibroblast dipeptidylpeptidase IV were very similar to those of the well-characterized pig kidney enzyme. Activity towards glycyl-L-prolyl-beta-naphthylamide was inhibited 50% by 0.023 mM-di-isopropylphosphorofluoridate. L-Alanyl-L-alanyl-beta-naphthylamide was hydrolysed ten times more slowly than glycyl-L-prolyl-beta-naphthylamide.

A comparison between secondary-ion mass-spectrometry and spark-source mass-spectrometry for the quantitative analysis of steel wire.

A comparison has been made between the results of the matrix-ion species ratio (MISR) method for quantification of secondary-ion mass-spectrometry data and spark-source mass-spectrometry analysis using photoplate detection for analysis of the steel basis of AlZn coated wire products. For SIMS quantification a suitable set of sensitivity factors, corrected for the actual surface sampling condition, was used. The results of both methods compare well. The SIMS results were, for most elements, within 25% of the concentration determined by SSMS. This could indicate that reasonably accurate results can be obtained by using the matrix-ion species ratio method for SIMS.

Localization of a highly antigenic human fibroblast surface glycoprotein (FSG) on fibroblasts and on epithelia involved in secretion or resorption.

The cellular distribution of a highly antigenic fibroblast glycoprotein, identified previously as aminopeptidase M, was studied in vitro by immunofluorescence and immuno-electron microscopy. The antigen was found to be localized at the surface of live and fixed fibroblasts in suspension and in cell layer; clustering or patching on live cells could be observed. Immunofluorescence after permeabilization of the cells with acetone showed distribution of the antigen in cytoplasmic granules. The tissue distribution of this antigen was examined by immunofluorescence on frozen sections of various human organs. In addition to fibroblasts, renal tubules, liver, pancreas and gut were found to react selectively with the antibody preparation. Moreover, a specific localization of the reaction product was observed. In the kidney the epithelium and brush border of the proximal convoluted tubules were stained. In the liver, the bile canaliculi reacted; in the pancreas the acinar cells and in the gut the brush border of the mucosal cells of the villi and crypts were stained. The same cells did not stain with an antiserum prepared in a similar fashion against another fibroblast component, or with preimmune IgG. In most sections of the selectively stained tissues, a predominant localization at the apical pole of the cells was observed. The localization of the antigen in different tissues corresponds with the distribution of aminopeptidase M, thereby confirming its identity and the antigenic cross-reaction between the fibroblast and tissue enzyme.

Immunochemical characterization of a 150 000 dalton human fibroblast surface glycoprotein.

The characterization of a human fibroblast surface glycoprotein, visualized by crossed immunoelectrophoresis using rabbit antibodies against whole fibroblasts, is described. The antigen is synthesized by fibroblasts in culture and was localized both intracellularly and at the cell surface. It was highly antigenic and was detected only in human cells of mesenchymal origin. The glycoprotein occurred in two different forms with alpha 2 and beta electrophoretic mobility. The slow migrating amphiphilic beta form was localized at the cell surface and showed a single protein band with an apparent molecular weight of 150 000 in SDS-polyacrylamide gel electrophoresis. By external papain treatment of intact viable cells, a water-soluble molecule was released with a reduced molecular weight (140 000) and an increased electrophoretic mobility as compared to the native membrane component. This hydrophilic form was also present intracellularly in fibroblasts not treated with exogeneous proteases. The observation that the detergent-solubilized beta form was irreversibly converted to a more anodic form by incubation of whole cell extract at acidic pH, suggested that the intracellular protein represented a lysosomal degradation product of native internalized fibroblast surface glycoprotein.