Publications by authors named "Anne-Sophie Svensson"
Article Synopsis
- Recent research on immunotherapy for Alzheimer's disease highlights the need to understand how different antibodies bind to amyloid-beta (Aβ), as this affects their effectiveness and potential side effects.
- Lecanemab, a specific IgG1 antibody, was studied using brain samples from Alzheimer's patients and non-demented controls to explore its interactions with various Aβ forms, revealing high levels of insoluble Aβ, especially Aβ42, in Alzheimer's subjects.
- Findings indicate that lecanemab binds primarily to soluble aggregated Aβ protofibrils rather than insoluble Aβ plaques, suggesting a targeted approach in treating Alzheimer's through the modulation of these specific proteins.
Article Synopsis
- Therapeutic antibodies targeting amyloid-beta (Aβ) have been developed to help slow Alzheimer's disease progression, but they can lead to side effects known as amyloid-related imaging abnormalities with edema (ARIA-E).
- This study examined how these antibodies bind to cerebral amyloid angiopathy (CAA) fibrils isolated from human brain tissue to see if there’s a link to the occurrence of ARIA-E in clinical trials.
- Results showed significant differences in binding behavior; some antibodies like solanezumab and crenezumab had minimal binding and no ARIA-E cases, while others like aducanumab and gantenerumab showed high binding and increased ARIA-E frequencies.
Article Synopsis
- Molecular biomarkers in blood, such as proteins, can indicate disease states and guide treatment, but their clinical reliability is often uncertain, particularly for Duchenne muscular dystrophy (DMD), which lacks effective monitoring tools.
- A new strategy was employed to confirm the reliability of biomarkers for DMD by analyzing serum samples from patients using two different detection methods: immuno-assays and Parallel Reaction Monitoring Mass Spectrometry (PRM-MS).
- Five out of ten previously identified biomarkers were validated, with carbonic anhydrase III and lactate dehydrogenase B showing strong correlations between methods and significantly elevated levels in DMD patients compared to healthy individuals.
Targeted proteomics is an attractive approach for the analysis of blood proteins. Here, we describe a novel analytical platform based on isotope-labeled recombinant protein standards stored in a chaotropic agent and subsequently dried down to allow storage at ambient temperature. This enables a straightforward protocol suitable for robotic workstations.
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- * Researchers analyzed over 100 SARS-CoV-2 protein representations and selected three key antigens from the spike glycoprotein and nucleocapsid protein for further testing on samples from COVID-19 patients and uninfected controls.
- * The final assay achieved impressive accuracy, with sensitivities ranging from 99.1% to 99.7% and specificities from 95.7% to 100%, especially when using two antigens together, demonstrating the assay's potential for reliable COVID-19 detection.
Antibody-drug conjugates (ADCs) have demonstrated great therapeutic potential due to their ability to target the delivery of potent cytotoxins. However, the heterogeneous nature of conventional drug conjugation strategies can affect the safety, efficacy, and stability of ADCs. Site-specific conjugations can resolve these issues, but often require genetic modification of Immunoglobulin G (IgG), which can impact yield or cost of production, or require undesirable chemical linkages.
View Article and Find Full Text PDFThe proteins secreted by human tissues and blood cells, the secretome, are important both for the basic understanding of human biology and for identification of potential targets for future diagnosis and therapy. Here, a high-throughput mammalian cell factory is presented that was established to create a resource of recombinant full-length proteins covering the majority of those annotated as 'secreted' in humans. The full-length DNA sequences of each of the predicted secreted proteins were generated by gene synthesis, the constructs were transfected into Chinese hamster ovary (CHO) cells and the recombinant proteins were produced, purified and analyzed.
View Article and Find Full Text PDFThe proteins secreted by human cells (collectively referred to as the secretome) are important not only for the basic understanding of human biology but also for the identification of potential targets for future diagnostics and therapies. Here, we present a comprehensive analysis of proteins predicted to be secreted in human cells, which provides information about their final localization in the human body, including the proteins actively secreted to peripheral blood. The analysis suggests that a large number of the proteins of the secretome are not secreted out of the cell, but instead are retained intracellularly, whereas another large group of proteins were identified that are predicted to be retained locally at the tissue of expression and not secreted into the blood.
View Article and Find Full Text PDFThe availability of proteomics resources hosting protein and peptide standards, as well as the data describing their analytical performances, will continue to enhance our current capabilities to develop targeted proteomics methods for quantitative biology. This study describes the analysis of a resource of 26,840 individually purified recombinant protein fragments corresponding to more than 16,000 human protein-coding genes. The resource was screened to identify proteotypic peptides suitable for targeted proteomics efforts, and we report LC-MS/MS assay coordinates for more than 25,000 proteotypic peptides, corresponding to more than 10,000 unique proteins.
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