Proteases hydrolyze peptide bonds, thereby controlling the function of proteins and peptides on the posttranslational level. In the cardiovascular system, proteases play pivotal roles in the regulation of blood pressure, coagulation and other essential physiological processes. Accordingly, proteases are prime targets for therapeutic interventions and diagnostics. Proteases are part of complex proteolytic networks comprised of enzymes, inhibitors, activators, substrates and cleavage products. Analyzing these networks on a system-wide level is essential to understanding cardiovascular function and how dysregulation can lead to pathological conditions. Mass spectrometry-based quantitative and dynamic proteomics approaches are leading the way to enhance our knowledge of proteolytic networks such as the renin-angiotensin-system. Here, we critically review proteomics tools utilized in protease biology and provide an overview on how these methods can be used to characterize and validate protease function.
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http://dx.doi.org/10.1161/CIRCGENETICS.110.957811 | DOI Listing |
Commun Biol
January 2025
Department of Cellular Architecture Studies, Division of Shionogi Global Infectious Diseases Division, Institute of Tropical Medicine (NEKKEN), Nagasaki University, Nagasaki, Japan.
The rapid intraerythrocytic replication of Plasmodium falciparum, a deadly species of malaria parasite, requires a quick but constant supply of phospholipids to support marked cell membrane expansion. In the malarial parasite, many enzymes functioning in phospholipid synthesis pathway have not been identified or characterized. Here, we identify P.
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January 2025
Bavarian Center for Biomolecular Mass Spectrometry (BayBioMS), TUM School of Life Sciences, Technical University of Munich, 85354 Freising, Germany. Electronic address:
Mass spectrometry-based proteomics has revolutionized bacterial identification and elucidated many molecular mechanisms underlying bacterial growth, community formation, and drug resistance. However, most research has been focused on a few model bacteria, overlooking bacterial diversity. In this study, we present the most extensive bacterial proteomic resource to date, covering 303 species, 119 genera, and five phyla with over 636,000 unique expressed proteins, confirming the existence of over 38,700 hypothetical proteins.
View Article and Find Full Text PDFFood Chem
January 2025
College of Food Science and Technology, Northwest University, Xi'an 710069, Shaanxi, China; Laboratory of Nutritional and Healthy Food-Individuation Manufacturing Engineering, Xi'an 710069, Shaanxi, China; Research Center of Food Safety Risk Assessment and Control, Xi'an 710069, Shaanxi, China. Electronic address:
Apple polyphenols (APP) can reduce obesity. However, the effects of APP on abdominal subcutaneous adipose tissue (aSAT) at metabolic level were unclear. In this study, 5-week APP intervenes were conducted on 10-week high-fat diet (HFD) feeding mice with doses of 200 and 500 mg/kg b.
View Article and Find Full Text PDFSci Adv
January 2025
Division of Molecular Medicine, Department of Medicine, University of Minnesota Medical School, Minneapolis, MN, USA.
Ketogenesis is a dynamic metabolic conduit supporting hepatic fat oxidation particularly when carbohydrates are in short supply. Ketone bodies may be recycled into anabolic substrates, but a physiological role for this process has not been identified. Here, we use mass spectrometry-based C-isotope tracing and shotgun lipidomics to establish a link between hepatic ketogenesis and lipid anabolism.
View Article and Find Full Text PDFElife
January 2025
Centre for Cellular Biology and Signalling, Zhejiang University-University of Edinburgh (ZJU-UoE) Institute, Haining, China.
Mitochondrial dysfunction is involved in numerous diseases and the aging process. The integrated stress response (ISR) serves as a critical adaptation mechanism to a variety of stresses, including those originating from mitochondria. By utilizing mass spectrometry-based cellular thermal shift assay (MS-CETSA), we uncovered that phosphatidylethanolamine-binding protein 1 (PEBP1), also known as Raf kinase inhibitory protein (RKIP), is thermally stabilized by stresses which induce mitochondrial ISR.
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