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1,506 results on '"Heeren, Ron"'

1. Testing of rapid evaporative mass spectrometry for histological tissue classification and molecular diagnostics in a multi-site study

Author

Kaufmann, Martin, Vaysse, Pierre-Maxence, Savage, Adele, Kooreman, Loes F. S., Janssen, Natasja, Varma, Sonal, Ren, Kevin Yi Mi, Merchant, Shaila, Engel, Cecil Jay, Olde Damink, Steven W. M., Smidt, Marjolein L., Shousha, Sami, Chauhan, Hemali, Karali, Evdoxia, Kazanc, Emine, Poulogiannis, George, Fichtinger, Gabor, Tauber, Boglárka, Leff, Daniel R., Pringle, Steven D., Rudan, John F., Heeren, Ron M. A., Porta Siegel, Tiffany, Takáts, Zoltán, and Balog, Júlia

Published
2024
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2. A liver immune rheostat regulates CD8 T cell immunity in chronic HBV infection

Author

Bosch, Miriam, Kallin, Nina, Donakonda, Sainitin, Zhang, Jitao David, Wintersteller, Hannah, Hegenbarth, Silke, Heim, Kathrin, Ramirez, Carlos, Fürst, Anna, Lattouf, Elias Isaac, Feuerherd, Martin, Chattopadhyay, Sutirtha, Kumpesa, Nadine, Griesser, Vera, Hoflack, Jean-Christophe, Siebourg-Polster, Juliane, Mogler, Carolin, Swadling, Leo, Pallett, Laura J., Meiser, Philippa, Manske, Katrin, de Almeida, Gustavo P., Kosinska, Anna D., Sandu, Ioana, Schneider, Annika, Steinbacher, Vincent, Teng, Yan, Schnabel, Julia, Theis, Fabian, Gehring, Adam J., Boonstra, Andre, Janssen, Harry L. A., Vandenbosch, Michiel, Cuypers, Eva, Öllinger, Rupert, Engleitner, Thomas, Rad, Roland, Steiger, Katja, Oxenius, Annette, Lo, Wan-Lin, Klepsch, Victoria, Baier, Gottfried, Holzmann, Bernhard, Maini, Mala K., Heeren, Ron, Murray, Peter J., Thimme, Robert, Herrmann, Carl, Protzer, Ulrike, Böttcher, Jan P., Zehn, Dietmar, Wohlleber, Dirk, Lauer, Georg M., Hofmann, Maike, Luangsay, Souphalone, and Knolle, Percy A.

Published
2024
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19. Integrating multiplex immunofluorescent and mass spectrometry imaging to map myeloid heterogeneity in its metabolic and cellular context

Author

Goossens, Pieter, Lu, Chang, Cao, Jianhua, Gijbels, Marion J., Karel, Joël M.H., Wijnands, Erwin, Claes, Britt S.R., Fazzi, Gregorio E., Hendriks, Tim F.E., Wouters, Kristiaan, Smirnov, Evgueni, van Zandvoort, Marc J.M., Balluff, Benjamin, Cuypers, Eva, Donners, Marjo M.P.C., Heeren, Ron M.A., and Biessen, Erik A.L.

Published
2022
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21. Profiling and imaging of forensic evidence – A pan-European forensic round robin study part 1: Document forgery

Author

Fischer, Thomas, Marchetti-Deschmann, Martina, Cristina Assis, Ana, Levin Elad, Michal, Algarra, Manuel, Barac, Marko, Bogdanovic Radovic, Iva, Cicconi, Flavio, Claes, Britt, Frascione, Nunzianda, George, Sony, Guedes, Alexandra, Heaton, Cameron, Heeren, Ron, Lazic, Violeta, Luis Lerma, José, del Valle Martinez de Yuso Garcia, Maria, Nosko, Martin, O'Hara, John, Oshina, Ilze, Palucci, Antonio, Pawlaczyk, Aleksandra, Zelená Pospíšková, Kristýna, de Puit, Marcel, Radodic, Ksenija, Rēpele, Māra, Ristova, Mimoza, Saverio Romolo, Francesco, Šafařík, Ivo, Siketic, Zdravko, Spigulis, Janis, Iwona Szynkowska-Jozwik, Malgorzata, Tsiatsiuyeu, Andrei, Vella, Joanna, Dawson, Lorna, Rödiger, Stefan, and Francese, Simona

Published
2022
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23. Patient-responsive protein biomarkers for cartilage degeneration and repair identified in the infrapatellar fat pad.

Author

Emanuel, Kaj S., Huang, Luojiao, Haartmans, Mirella J. J., Sanmartin Martinez, Javier, Zijta, Frank, Heeren, Ron M. A., Kerkhoffs, Gino M. M. J., Emans, Pieter J., and Cillero-Pastor, Berta

Abstract

Objectives: Cartilage defects (CDs) are regarded as early manifestation of osteoarthritis (OA). The infrapatellar fat pad (IPFP) is an important mediator in maintaining joint homeostasis, disease progression and tissue repair, with a crucial role of its secreted proteins. Here, we investigate the proteome of the IPFP in relation to clinical status and response to surgical treatment of CDs. Methods: In order to characterize the proteome of the IPFP, samples from a cohort of 53 patients who received surgical treatment for knee CDs were analyzed with label-free proteomics. Patients were divided based on validated outcome scores for pain and knee function, preoperatively and at 1-year postoperatively, and on MRI assessment of the defect severity, fibrosis and synovitis. Results: Specific proteins were differentially abundant in patients with MRI features and better clinical outcome after CD surgery, including a downregulation of cartilage intermediate layer protein 2 (CILP-2) and microsomal glutathione s-transferase 1 (MGST1), and an upregulation of aggrecan (ACAN), and proteoglycan 4 (PRG4). Pathways related to cell interaction, oxidation and matrix remodeling were altered. Conclusion: Proteins in the IPFP that have a function in extracellular matrix, inflammation and immunomodulation were identified as potentially relevant markers for cartilage repair monitoring. [ABSTRACT FROM AUTHOR]

Published
2024
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35. Biosynthesis and differential spatial distribution of the 3‐deoxyanthocyanidins apigenidin and luteolinidin at the interface of a plant‐cyanobacteria symbiosis exposed to cold.

Author

Güngör, Erbil, Bartels, Benjamin, Bolchi, Giorgio, Heeren, Ron M. A., Ellis, Shane R., and Schluepmann, Henriette

Subjects
PHOTOOXIDATIVE stress, ABSCISIC acid, SYMBIOSIS, ACCLIMATIZATION, EPITHELIAL cells
Abstract

Aquatic ferns of the genus Azolla (Azolla) form highly productive symbioses with filamentous cyanobacteria fixing N2 in their leaf cavities, Nostoc azollae. Stressed symbioses characteristically turn red due to 3‐deoxyanthocyanidin (DA) accumulation, rare in angiosperms and of unknown function. To understand DA accumulation upon cold acclimation and recovery, we integrated laser‐desorption‐ionization mass‐spectrometry‐imaging (LDI‐MSI), a new Azolla filiculoides genome‐assembly and annotation, and dual RNA‐sequencing into phenotypic analyses of the symbioses. Azolla sp. Anzali recovered even when cold‐induced DA‐accumulation was inhibited by abscisic acid. Cyanobacterial filaments generally disappeared upon cold acclimation and Nostoc azollae transcript profiles were unlike those of resting stages formed in cold‐resistant sporocarps, yet filaments re‐appeared in leaf cavities of newly formed green fronds upon cold‐recovery. The high transcript accumulation upon cold acclimation of AfDFR1 encoding a flavanone 4‐reductase active in vitro suggested that the enzyme of the first step in the DA‐pathway may regulate accumulation of DAs in different tissues. However, LDI‐MSI highlighted the necessity to describe metabolite accumulation beyond class assignments as individual DA and caffeoylquinic acid metabolites accumulated differentially. For example, luteolinidin accumulated in epithelial cells, including those lining the leaf cavity, supporting a role for the former in the symbiotic interaction during cold acclimation. Summary statement: During cold acclimation in Azolla symbioses, individual compounds from the same phenolic class accumulated in different host tissues: luteolinidin associated with biotic interactions at the symbiosis interface while apigenidin with photooxidative stress mitigation in the mesophyll. [ABSTRACT FROM AUTHOR]

Published
2024
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36. Mass spectrometry imaging in plants, microbes, and food: a review.

Author

Vats, Mudita, Cillero-Pastor, Berta, Cuypers, Eva, and Heeren, Ron M. A.

Subjects
FARM management, FOOD supply, AGRICULTURE, MOLECULAR biology, FARM produce, MASS spectrometry
Abstract

Plant health, which affects the nutritional quality and safety of derivative food products, is influenced by symbiotic interactions with microorganisms. These interactions influence the local molecular profile at the tissue level. Therefore, studying the distribution of molecules within plants, microbes, and plant-based food is crucial to assess plant health, ensure the safety and quality of the agricultural products that become part of our food supply, and plan agricultural management practices. Within this framework, the molecular distribution within plant-based samples can be visualized with mass spectrometry imaging (MSI). This review describes key MSI methodologies, highlighting the role they play in unraveling the localization of metabolites, lipids, proteins, pigments, and elemental components across plants, microbes, and food products. Furthermore, investigations that involve multimodal molecular imaging approaches combining MSI with other imaging techniques are described. The advantages and limitations of the different MSI techniques that influence their applicability in diverse agro-food studies are described to enable informed choices for tailored analyses. For example, some MSI technologies involve meticulous sample preparation while others compromise spatial resolution to gain throughput. Key parameters such as sensitivity, ionization bias and fragmentation, reference database and compound class specificity are described and discussed in this review. With the ongoing refinements in instrumentation, data analysis, and integration of complementary techniques, MSI deepens our insight into the molecular biology of the agricultural ecosystem. This in turn empowers the quest for sustainable and productive agricultural practices. [ABSTRACT FROM AUTHOR]

Published
2024
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37. Combined matrix‐assisted laser desorption/ionisation‐mass spectrometry imaging with liquid chromatography‐tandem mass spectrometry for observing spatial distribution of lipids in whole Caenorhabditis elegans.

Author

Vandenbosch, Michiel, van Hove, Erika R. Amstalden, Mohren, Ronny, Vermeulen, Isabeau, Dijkman, Henry, Heeren, Ron M. A., Leonards, Pim E. G., and Hughes, Samantha

Subjects
CAENORHABDITIS elegans, IMMERSION in liquids, MASS spectrometry, NEMATODES, SPATIAL resolution, MATRIX-assisted laser desorption-ionization
Abstract

Rationale: Matrix‐assisted laser desorption/ionisation‐mass spectrometry imaging (MALDI‐MSI) is a powerful label‐free technique for biomolecule detection (e.g., lipids), within tissue sections across various biological species. However, despite its utility in many applications, the nematode Caenorhabditis elegans is not routinely used in combination with MALDI‐MSI. The lack of studies exploring spatial distribution of biomolecules in nematodes is likely due to challenges with sample preparation. Methods: This study developed a sample preparation method for whole intact nematodes, evaluated using cryosectioning of nematodes embedded in a 10% gelatine solution to obtain longitudinal cross sections. The slices were then subjected to MALDI‐MSI, using a RapifleX Tissuetyper in positive and negative polarities. Samples were also prepared for liquid chromatography‐tandem mass spectrometry (LC‐MS/MS) analysis using an Exploris 480 coupled to a HPLC Vanquish system to confirm the MALDI‐MSI results. Results: An optimised embedding method was developed for longitudinal cross‐sectioning of individual worms. To obtain longitudinal cross sections, nematodes were frozen at −80°C so that all worms were rod shaped. Then, the samples were defrosted and transferred to a 10% gelatine matrix in a cryomold; the worms aligned, and the whole cryomold submerged in liquid nitrogen. Using MALDI‐MSI, we were able to observe the distribution of lipids within C. elegans, with clear differences in their spatial distribution at a resolution of 5 μm. To confirm the lipids from MALDI‐MSI, age‐matched nematodes were subjected to LC‐MS/MS. Here, 520 lipids were identified using LC‐MS/MS, indicating overlap with MALDI‐MSI data. Conclusions: This optimised sample preparation technique enabled (un)targeted analysis of spatially distributed lipids within individual nematodes. The possibility to detect other biomolecules using this method thus laid the basis for prospective preclinical and toxicological studies on C. elegans. [ABSTRACT FROM AUTHOR]

Published
2024
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38. INSPIRE: A European training network to foster research and training in cardiovascular safety pharmacology

Author

Guns, Pieter-Jan D., Guth, Brian D., Braam, Stefan, Kosmidis, Georgios, Matsa, Elena, Delaunois, Annie, Gryshkova, Vitalina, Bernasconi, Sylvain, Knot, Harm J., Shemesh, Yair, Chen, Alon, Markert, Michael, Fernández, Miguel A., Lombardi, Damiano, Grandmont, Céline, Cillero-Pastor, Berta, Heeren, Ron M.A., Martinet, Wim, Woolard, Jeanette, Skinner, Matt, Segers, Vincent F.M., Franssen, Constantijn, Van Craenenbroeck, Emeline M., Volders, Paul G.A., Pauwelyn, Thomas, Braeken, Dries, Yanez, Paz, Correll, Krystle, Yang, Xi, Prior, Helen, Kismihók, Gábor, De Meyer, Guido R.Y., and Valentin, Jean-Pierre

Published
2020
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41. Inflammation‐associated intramyocellular lipid alterations in human pancreatic cancer cachexia

Author

Deng, Min, primary, Cao, Jianhua, additional, van der Kroft, Gregory, additional, van Dijk, David P.J., additional, Aberle, Merel R., additional, Grgic, Andrej, additional, Neumann, Ulf P., additional, Wiltberger, Georg, additional, Balluff, Benjamin, additional, Schaap, Frank G., additional, Heeren, Ron M.A., additional, Olde Damink, Steven W.M., additional, and Rensen, Sander S., additional

Published
2024
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42. Mass Spectrometry Reveals Molecular Effects of Citrulline Supplementation during Bone Fracture Healing in a Rat Model

Author

Nauta, Sylvia, primary, Greven, Johannes, additional, Hofman, Martijn, additional, Mohren, Ronny, additional, Meesters, Dennis M., additional, Möckel, Diana, additional, Lammers, Twan, additional, Hildebrand, Frank, additional, Siegel, Tiffany Porta, additional, Cuypers, Eva, additional, Heeren, Ron M.A., additional, and Poeze, Martijn, additional

Published
2024
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45. Auto-aggressive CXCR6+ CD8 T cells cause liver immune pathology in NASH

Author

Dudek, Michael, Pfister, Dominik, Donakonda, Sainitin, Filpe, Pamela, Schneider, Annika, Laschinger, Melanie, Hartmann, Daniel, Hüser, Norbert, Meiser, Philippa, Bayerl, Felix, Inverso, Donato, Wigger, Jennifer, Sebode, Marcial, Öllinger, Rupert, Rad, Roland, Hegenbarth, Silke, Anton, Martina, Guillot, Adrien, Bowman, Andrew, Heide, Danijela, Müller, Florian, Ramadori, Pierluigi, Leone, Valentina, Garcia-Caceres, Cristina, Gruber, Tim, Seifert, Gabriel, Kabat, Agnieszka M., Mallm, Jan-Philipp, Reider, Simon, Effenberger, Maria, Roth, Susanne, Billeter, Adrian T., Müller-Stich, Beat, Pearce, Edward J., Koch-Nolte, Friedrich, Käser, Rafael, Tilg, Herbert, Thimme, Robert, Boettler, Tobias, Tacke, Frank, Dufour, Jean-Francois, Haller, Dirk, Murray, Peter J., Heeren, Ron, Zehn, Dietmar, Böttcher, Jan P., Heikenwälder, Mathias, and Knolle, Percy A.

Published
2021
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47. Spatial Neurolipidomics at the Single Amyloid-β Plaque Level in Postmortem Human Alzheimer's Disease Brain

Author

Michno, Wojciech, Bowman, Andrew, Jha, Durga, Minta, Karolina, Ge, Junyue, Koutarapu, Srinivas, Zetterberg, Henrik, Blennow, Kaj, Lashley, Tammaryn, Heeren, Ron M. A., Hanrieder, Jorg, Michno, Wojciech, Bowman, Andrew, Jha, Durga, Minta, Karolina, Ge, Junyue, Koutarapu, Srinivas, Zetterberg, Henrik, Blennow, Kaj, Lashley, Tammaryn, Heeren, Ron M. A., and Hanrieder, Jorg

Abstract

Lipid dysregulations have been critically implicated in Alzheimer's disease (AD) pathology. Chemical analysis of amyloid-beta (A beta) plaque pathology in transgenic AD mouse models has demonstrated alterations in the microenvironment in the direct proximity of A beta plaque pathology. In mouse studies, differences in lipid patterns linked to structural polymorphism among A beta pathology, such as diffuse, immature, and mature fibrillary aggregates, have also been reported. To date, no comprehensive analysis of neuronal lipid microenvironment changes in human AD tissue has been performed. Here, for the first time, we leverage matrix-assisted laser desorption/ionization mass spectrometry imaging (MALDI-MSI) through a high-speed and spatial resolution commercial time-of-light instrument, as well as a high-mass-resolution in-house-developed orbitrap system to characterize the lipid microenvironment in postmortem human brain tissue from AD patients carrying Presenilin 1 mutations (PSEN1) that lead to familial forms of AD (fAD). Interrogation of the spatially resolved MSI data on a single A beta plaque allowed us to verify nearly 40 sphingolipid and phospholipid species from diverse subclasses being enriched and depleted, in relation to the A beta deposits. This included monosialo-gangliosides (GM), ceramide monohexosides (HexCer), ceramide-1-phosphates (CerP), ceramide phosphoethanolamine conjugates (PE-Cer), sulfatides (ST), as well as phosphatidylinositols (PI), phosphatidylethanolamines (PE), and phosphatidic acid (PA) species (including Lyso-forms). Indeed, many of the sphingolipid species overlap with the species previously seen in transgenic AD mouse models. Interestingly, in comparison to the animal studies, we observed an increased level of localization of PE and PI species containing arachidonic acid (AA). These findings are highly relevant, demonstrating for the first time A beta plaque pathology-related alteration in the lipid microenvironment in humans. They

Published
2024
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48. Spatial Metabolomics Identifies LPC(18:0) and LPA(18:1) in Advanced Atheroma With Translation to Plasma for Cardiovascular Risk Estimation

Author

Cao, Jianhua, Martin-Lorenzo, Marta, van Kuijk, Kim, Wieland, Elias, Gijbels, Marion J, Claes, Britt S R, Heredero, Angeles, Aldamiz-Echevarria, Gonzalo, Heeren, Ron M A, Goossens, Pieter, Sluimer, Judith, Balluff, Benjamin, Alvarez-Llamas, Gloria, Cao, Jianhua, Martin-Lorenzo, Marta, van Kuijk, Kim, Wieland, Elias, Gijbels, Marion J, Claes, Britt S R, Heredero, Angeles, Aldamiz-Echevarria, Gonzalo, Heeren, Ron M A, Goossens, Pieter, Sluimer, Judith, Balluff, Benjamin, and Alvarez-Llamas, Gloria

Abstract

BACKGROUND: The metabolic alterations occurring within the arterial architecture during atherosclerosis development remain poorly understood, let alone those particular to each arterial tunica. We aimed to identify, in a spatially resolved manner, the specific metabolic changes in plaque, media, adventitia, and cardiac tissue between control and atherosclerotic murine aortas. Second, we assessed their translatability to human tissue and plasma for cardiovascular risk estimation. METHODS: In this observational study, mass spectrometry (MS) imaging was applied to identify region-specific metabolic differences between atherosclerotic (n=11) and control (n=11) aortas from low-density lipoprotein receptor-deficient mice, via histology-guided virtual microdissection. Early and advanced plaques were compared within the same atherosclerotic animals. Progression metabolites were further analyzed by MS imaging in 9 human atherosclerotic carotids and by targeted MS in human plasma from subjects with elective coronary artery bypass grafting (cardiovascular risk group, n=27) and a control group (n=27). RESULTS: MS imaging identified 362 local metabolic alterations in atherosclerotic mice (log2 fold-change, =1.5; =0.05). The lipid composition of cardiac tissue is altered during atherosclerosis development and presents a generalized accumulation of glycerophospholipids, except for lysolipids. Lysolipids (among other glycerophospholipids) were found at elevated levels in all 3 arterial layers of atherosclerotic aortas. Lysophosphatidylcholine(18:0; =0.024) and lysophosphatidic acid(18:1; =0.025) were found to be significantly elevated in advanced plaques as compared with mouse-matched early plaques. Higher levels of both lipid species were also observed in fibrosis-rich areas of advanced- versus early-stage human samples. They were found to be significantly reduced in human plasma from subjects with elective coronary artery bypass graft ( <0.001 and =0.031, respectively), with l

Published
2024

49. Recent Technological Developments in MALDI-MSI Based Hair Analysis

Author

Flinders, Bryn, Bassindale, Tom, Heeren, Ron M. A., Masys, Anthony J., Series Editor, Bichler, Gisela, Advisory Editor, Bourlai, Thirimachos, Advisory Editor, Johnson, Chris, Advisory Editor, Karampelas, Panagiotis, Advisory Editor, Leuprecht, Christian, Advisory Editor, Morse, Edward C., Advisory Editor, Skillicorn, David, Advisory Editor, Yamagata, Yoshiki, Advisory Editor, and Francese, Simona, editor

Published
2019
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50. Top-Down Mass Spectrometry Imaging of Intact Proteins by LAESI FT-ICR MS

Author

Kiss, András, Smith, Donald F., Reschke, Brent R., Powell, Matthew J., and Heeren, Ron M. A.

Subjects
Physics - Biological Physics, Quantitative Biology - Quantitative Methods
Abstract

Laser Ablation Electrospray Ionization is a recent development in mass spectrometry imaging. It has been shown that lipids and small metabolites can be imaged in various samples such as plant material, tissue sections or bacterial colonies without anysample pre-treatment. Further, laser ablation electrospray ionization has been shown to produce multiply charged protein ions from liquids or solid surfaces. This presents a means to address one of the biggest challenges in mass spectrometry imaging; the identification of proteins directly from biological tissue surfaces. Such identification is hindered by the lack of multiply charged proteins in common MALDI ion sources and the difficulty of performing tandem MS on such large, singly charged ions. We present here top-down identification of intact proteins from tissue with a LAESI ion source combined with a hybrid ion-trap FT-ICR mass spectrometer. The performance of the system was first tested with a standard protein with ECD and IRMPD fragmentation to prove the viability of LAESI FT-ICR for top-down proteomics. Finally, the imaging of a tissue section was performed, where a number of intact proteins were measured and the hemoglobin {\alpha} chain was identified directly from tissue using collision-induced dissociation and infrared multiphoton dissociation fragmentation.

Published
2013

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