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Phosphoproteomics for studying signaling pathways evoked by hormones of the renin-angiotensin system: A source of untapped potential.
Acta Physiol (Oxf)
February 2025
Department of Molecular Medicine, Cardiovascular and Renal Research Unit, University of Southern Denmark, Odense M, Denmark.
The Renin-Angiotensin System (RAS) is a complex neuroendocrine system consisting of a single precursor protein, angiotensinogen (AGT), which is processed into various peptide hormones, including the angiotensins [Ang I, Ang II, Ang III, Ang IV, Ang-(1-9), Ang-(1-7), Ang-(1-5), etc] and Alamandine-related peptides [Ang A, Alamandine, Ala-(1-5)], through intricate enzymatic pathways. Functionally, the RAS is divided into two axes with opposing effects: the classical axis, primarily consisting of Ang II acting through the AT receptor (ATR), and in contrast the protective axis, which includes the receptors Mas, ATR and MrgD and their respective ligands. A key area of RAS research is to gain a better understanding how signaling cascades elicited by these receptors lead to either "classical" or "protective" effects, as imbalances between the two axes can contribute to disease.
View Article and Find Full Text PDFOzNOxESI: A Novel Mass Spectrometry Ion Chemistry for Elucidating Lipid Double-Bond Regioisomerism in Complex Mixtures.
Anal Chem
January 2025
Center for Translational Biomedical Research, University of North Carolina at Greensboro, Kannapolis, North Carolina 28081, United States.
Double bond (C═C) position isomerism in unsaturated lipids can indicate abnormal lipid metabolism and pathological conditions. Novel chemical derivatization and mass spectrometry-based techniques are under continuing development to provide more accurate elucidation of lipid structure in finer structural detail. Here, we introduce a new ion chemistry for annotating lipid C═C positions, which is highly efficient for liquid chromatography-mass spectrometry-based lipidomics.
View Article and Find Full Text PDFMetabolomic characterisation of the glioblastoma invasive margin reveals a region-specific signature.
Heliyon
January 2025
Children's Brain Tumour Research Centre, School of Medicine, Biodiscovery Institute, University of Nottingham, UK.
Isocitrate dehydrogenase wild-type glioblastoma (GBM) is characterised by a heterogeneous genetic landscape resulting from dynamic competition between tumour subclones to survive selective pressures. Improvements in metabolite identification and metabolome coverage have led to increased interest in clinically relevant applications of metabolomics. Here, we use liquid chromatography-mass spectrometry and gene expression microarray to profile integrated intratumour metabolic heterogeneity, as a direct functional readout of adaptive responses of subclones to the tumour microenvironment.
View Article and Find Full Text PDFClinical Microbiome Analysis by Mass Spectrometry-Based Metaproteomics.
Annu Rev Anal Chem (Palo Alto Calif)
January 2025
2School of Pharmaceutical Sciences, Faculty of Medicine, University of Ottawa, Ottawa, Ontario, Canada; email:
Mass spectrometry-based proteomics and metaproteomics have long been used in the study of human microbiomes, with the potential of metaproteomics only recently being fully harnessed. This progress is due to the advancements of high-performance mass spectrometers, innovative proteomics strategies, and the development of dedicated bioinformatics tools. In this review, we critically examine the recent technological developments that enhance the application of metaproteomics in clinical microbiome analysis.
View Article and Find Full Text PDFNavigating the landscape of plant proteomics.
J Integr Plant Biol
January 2025
Institute of Advanced Biotechnology and School of Medicine, Southern University of Science and Technology, Shenzhen, 518055, China.
In plants, proteins are fundamental to virtually all biological processes, such as photosynthesis, signal transduction, metabolic regulation, and stress responses. Studying protein distribution, function, modifications, and interactions at the cellular and tissue levels is critical for unraveling the complexities of these biological pathways. Protein abundance and localization are highly dynamic and vary widely across the proteome, presenting a challenge for global protein quantification and analysis.
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