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In the recent years, the number of Point-Of-Care-Tests (POCTs) available for clinical diagnostic has steadily increased. POCTs provide a near-patient testing with the potential to generate a result quickly so that appropriate treatment can be implemented, leading to improved clinical outcomes compared to traditional laboratory testing. Technological advances, such as miniaturization of sensors and improved instrumentation, have revolutionized POCTs, enabling the development of smaller and more accurate devices. In this context, it has also gained increasing importance the screening of various analytes simultaneously to increase specificity and improve the characterization of the disease. This study is aimed at developing and characterizing a photonic integrated circuit for multiple markers detection, which represents the functional core towards a full developed POCT device for clinical pathology applications. The photonic sensor, based on microring resonators (MRRs), is functionalized by immobilizing specific antibodies on a copolymer layer deposited on the MRR's surfaces. Surface chemical techniques were employed to analyse the surface chemical characteristics while fluorescence microscopy was involved to analyse the resulting bioreceptor surface density. The photonic sensor is characterized for the parallel detection of two biomarkers, the C-Reactive Protein (CRP) and the Creatine-Kinase-MB (CK-MB). The analyte-antibody binding curves were obtained both in buffer and in filtered un-diluted artificial saliva showing promising results both in terms of sensitivity, with limit of detection (LOD) of 103 pM for CRP and 140 pM for CK-MB, and in terms of specificity. These encouraging results let the assembly of a highly sensitive POC device for molecular diagnostics., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier B.V. All rights reserved.)

Background: Inferior vena cava (IVC) filters can present challenges to emergency physicians in the process of central venous catheter (CVC) placement., Case Report: A 68-year-old woman presented to the emergency department with severe shortness of breath and was intubated. A central line was placed after the intubation to facilitate peripheral access. A CVC guidewire unraveled during placement after getting caught on an IVC filter. WHY SHOULD AN EMERGENCY PHYSICIAN BE AWARE OF THIS?: Emergency physicians should be aware of the complications that IVC filters can cause in the placement of CVCs. Imaging and identification of IVC filters beforehand will allow for proper planning of how to manage the case in which a filter catches on the guidewire. Simple anecdotal techniques, such as advancing the guidewire and spinning the guidewire between the fingers, can facilitate the removal of the guide wire from the IVC filter., (Copyright © 2014 Elsevier Inc. All rights reserved.)

Advances in proteomic technology have enabled contaminant proteins to be identified from complex protein mixtures. The purity of two purified urinary gonadotrophin products, human menopausal gonadotrophin (u-HMG) and human FSH (u-hFSH), was compared with a preparation of recombinant human FSH (r-hFSH). After separation by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), western blot analysis showed that the recombinant preparation contained only FSH, whereas the urine-derived preparations exhibited several non-FSH or LH-related bands. These urinary components were further investigated by a proteomic approach using two-dimensional SDS-PAGE followed by mass spectrometric identification. The proteomic approach detected a total of 23 non-gonadotrophin-related proteins, at variable levels in different batches of the urine-derived preparations. Of these, 16 co-purified proteins have not been previously reported to be present in urine-derived gonadotrophins. These results indicate that the process used to purify urinary gonadotrophins may not remove all non-gonadotrophin proteins. By using a comprehensive proteomic approach, it has been shown that the recombinant FSH preparation has greater purity than either of the urine-derived preparations.

The revolutionary development of biotechnology-derived therapeutic proteins has provided the expected improvements in quality, purity and consistency, as demonstrated in recombinant human FSH (rhFSH). However, the development of urine-derived gonadotrophins has not always shown comparable improvements. More recently, highly purified urine-derived FSH (uFSH-HP) products have become widely available. The relative purity, level of urine-derived contaminants, and consistency of one such highly purified human uFSH (uhFSH) (urofollitropin) has been assessed and directly compared with rhFSH (follitropin alpha). It has been demonstrated that the highly purified urofollitropin contains variable levels of urine-derived contaminant proteins and demonstrates a variable level of FSH purity, FSH isoforms, and delivered dose. These variable factors may contribute to the control of ovarian stimulation. The relative purity, variable consistency and the presence of contaminants indicates that the urofollitropin is, at best, a partially purified uFSH that is not able to meet the quality attributes of follitropin alpha (rhFSH).