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868 results on '"Verbeek, Marcel M."'

2. Temporal Ordering of Biomarkers in Dutch-Type Hereditary Cerebral Amyloid Angiopathy

Author

Koemans, Emma A., Rasing, Ingeborg, Voigt, Sabine, van Harten, Thijs W., van der Zwet, Reinier G.J., Kaushik, Kanishk, Schipper, Manon R., van der Weerd, Nelleke, van Zwet, Erik W., van Etten, Ellis S., van Osch, Matthias J.P., Kuiperij, Bea, Verbeek, Marcel M., Terwindt, Gisela M., Greenberg, Steven M., van Walderveen, Marianne A.A., and Wermer, Marieke J.H.

Published
2024
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5. Correction: Serum and cerebrospinal fluid neurofilament light chain and glial fibrillary acid protein levels in early and advanced stages of cerebral amyloid angiopathy

Author

Rasing, Ingeborg, Voigt, Sabine, Koemans, Emma A., de Kort, Anna M., van Harten, Thijs W., van Etten, Ellis S., van Zwet, Erik W., Stoops, Erik, Francois, Cindy, Kuiperij, H. Bea, Klijn, Catharina J.M., Schreuder, Floris H.B.M., van der Weerd, Louise, van Osch, Matthias J.P., van Walderveen, Marianne A.A., Verbeek, Marcel M., Terwindt, Gisela M., and Wermer, Marieke J.H.

Published
2024
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9. Serum and cerebrospinal fluid neurofilament light chain and glial fibrillary acid protein levels in early and advanced stages of cerebral amyloid Angiopathy

Author

Rasing, Ingeborg, Voigt, Sabine, Koemans, Emma A., de Kort, Anna M., van Harten, Thijs W., van Etten, Ellis S., van Zwet, Erik W., Stoops, Erik, Francois, Cindy, Kuiperij, H. Bea, Klijn, Catharina J.M., Schreuder, Floris H.B.M., van der Weerd, Louise, van Osch, Matthias J.P., van Walderveen, Marianne A.A., Verbeek, Marcel M., Terwindt, Gisela M., and Wermer, Marieke J.H.

Published
2024
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10. Neuropsychiatric symptoms with focus on apathy and irritability in sporadic and hereditary cerebral amyloid angiopathy

Author

Kaushik, Kanishk, de Kort, Anna M., van Dort, Rosemarie, van der Zwet, Reinier G.J., Siegerink, Bob, Voigt, Sabine, van Zwet, Erik W., van der Plas, Maaike C., Koemans, Emma A., Rasing, Ingeborg, Kessels, Roy P.C., Middelkoop, Huub A.M., Schreuder, Floris H.B.M., Klijn, Catharina J.M., Verbeek, Marcel M., Terwindt, Gisela M., van Etten, Ellis S., and Wermer, Marieke J.H.

Published
2024
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14. Profiling amyloid‐β peptides as biomarkers for cerebral amyloid angiopathy.

Author

van den Berg, Emma, Kersten, Iris, Brinkmalm, Gunnar, Johansson, Kjell, de Kort, Anna M., Klijn, Catharina J. M., Schreuder, Floris H. B. M., Gobom, Johan, Stoops, Erik, Portelius, Erik, Gkanatsiou, Eleni, Zetterberg, Henrik, Blennow, Kaj, Kuiperij, H. Bea, and Verbeek, Marcel M.

Subjects
CEREBRAL amyloid angiopathy, LIQUID chromatography-mass spectrometry, PEPTIDES, ALZHEIMER'S disease, BIOMARKERS
Abstract

Brain amyloid‐β (Aβ) deposits are key pathological hallmarks of both cerebral amyloid angiopathy (CAA) and Alzheimer's disease (AD). Microvascular deposits in CAA mainly consist of the Aβ40 peptide, whereas Aβ42 is the predominant variant in parenchymal plaques in AD. The relevance in pathogenesis and diagnostic accuracy of various other Aβ isoforms in CAA remain understudied. We aimed to investigate the biomarker potential of various Aβ isoforms in cerebrospinal fluid (CSF) to differentiate CAA from AD pathology. We included 25 patients with probable CAA, 50 subjects with a CSF profile indicative of AD pathology (AD‐like), and 23 age‐ and sex‐matched controls. CSF levels of Aβ1‐34, Aβ1‐37, Aβ1‐38, Aβ1‐39, Aβ1‐40, and Aβ1‐42 were quantified by liquid chromatography mass spectrometry. Lower CSF levels of all six Aβ peptides were observed in CAA patients compared with controls (p = 0.0005–0.03). Except for Aβ1‐42 (p = 1.0), all peptides were decreased in CAA compared with AD‐like subjects (p = 0.007–0.03). Besides Aβ1‐42, none of the Aβ peptides were decreased in AD‐like subjects compared with controls. All Aβ peptides combined differentiated CAA from AD‐like subjects better (area under the curve [AUC] 0.84) than individual peptide levels (AUC 0.51–0.75). Without Aβ1‐42 in the model (since decreased Aβ1‐42 served as AD‐like selection criterion), the AUC was 0.78 for distinguishing CAA from AD‐like subjects. CAA patients and AD‐like subjects showed distinct disease‐specific CSF Aβ profiles. Peptides shorter than Aβ1‐42 were decreased in CAA patients, but not AD‐like subjects, which could suggest different pathological mechanisms between vascular and parenchymal Aβ accumulation. This study supports the potential use of this panel of CSF Aβ peptides to indicate presence of CAA pathology with high accuracy. [ABSTRACT FROM AUTHOR]

Published
2024
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15. Divergent Associations of Slow‐Wave Sleep versus Rapid Eye Movement Sleep with Plasma Amyloid‐Beta.

Author

Rosenblum, Yevgenia, Pereira, Mariana, Stange, Oliver, Weber, Frederik D., Bovy, Leonore, Tzioridou, Sofia, Lancini, Elisa, Neville, David A., Klein, Nadja, de Wolff, Timo, Stritzke, Mandy, Kersten, Iris, Uhr, Manfred, Claassen, Jurgen A. H. R., Steiger, Axel, Verbeek, Marcel M., and Dresler, Martin

Subjects
RAPID eye movement sleep, SLOW wave sleep, SLEEP stages, SOMATOTROPIN, AMYLOID plaque
Abstract

Objective: Recent evidence shows that during slow‐wave sleep (SWS), the brain is cleared from potentially toxic metabolites, such as the amyloid‐beta protein. Poor sleep or elevated cortisol levels can worsen amyloid‐beta clearance, potentially leading to the formation of amyloid plaques, a neuropathological hallmark of Alzheimer disease. Here, we explored how nocturnal neural and endocrine activity affects amyloid‐beta fluctuations in the peripheral blood. Methods: We acquired simultaneous polysomnography and all‐night blood sampling in 60 healthy volunteers aged 20–68 years. Nocturnal plasma concentrations of amyloid‐beta‐40, amyloid‐beta‐42, cortisol, and growth hormone were assessed every 20 minutes. Amyloid‐beta fluctuations were modeled with sleep stages, (non)oscillatory power, and hormones as predictors while controlling for age and participant‐specific random effects. Results: Amyloid‐beta‐40 and amyloid‐beta‐42 levels correlated positively with growth hormone concentrations, SWS proportion, and slow‐wave (0.3–4Hz) oscillatory and high‐band (30–48Hz) nonoscillatory power, but negatively with cortisol concentrations and rapid eye movement sleep (REM) proportion measured 40–100 minutes previously (all t values > |3|, p values < 0.003). Older participants showed higher amyloid‐beta‐40 levels. Interpretation: Slow‐wave oscillations are associated with higher plasma amyloid‐beta levels, whereas REM sleep is related to decreased amyloid‐beta plasma levels, possibly representing changes in central amyloid‐beta production or clearance. Strong associations between cortisol, growth hormone, and amyloid‐beta presumably reflect the sleep‐regulating role of the corresponding releasing hormones. A positive association between age and amyloid‐beta‐40 may indicate that peripheral clearance becomes less efficient with age. ANN NEUROL 2024;96:46–60 [ABSTRACT FROM AUTHOR]

Published
2024
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17. Succinic semialdehyde dehydrogenase deficiency in mice and in humans: An untargeted metabolomics perspective.

Author

Peters, Tessa M. A., Engelke, Udo F. H., de Boer, Siebolt, Reintjes, Joris T. G., Roullet, Jean‐Baptiste, Broekman, Sanne, de Vrieze, Erik, van Wijk, Erwin, Wamelink, Mirjam M. C., Artuch, Rafael, Barić, Ivo, Merx, Jona, Boltje, Thomas J., Martens, Jonathan, Willemsen, Michèl A. A. P., Verbeek, Marcel M., Wevers, Ron A., Gibson, K. Michael, and Coene, Karlien L. M.

Abstract

Succinic semialdehyde dehydrogenase deficiency (SSADHD) is a rare neurometabolic disorder caused by disruption of the gamma‐aminobutyric acid (GABA) pathway. A more detailed understanding of its pathophysiology, beyond the accumulation of GABA and gamma‐hydroxybutyric acid (GHB), will increase our understanding of the disease and may support novel therapy development. To this end, we compared biochemical body fluid profiles from SSADHD patients with controls using next‐generation metabolic screening (NGMS). Targeted analysis of NGMS data from cerebrospinal fluid (CSF) showed a moderate increase of aspartic acid, glutaric acid, glycolic acid, 4‐guanidinobutanoic acid, and 2‐hydroxyglutaric acid, and prominent elevations of GHB and 4,5‐dihydroxyhexanoic acid (4,5‐DHHA) in SSADHD samples. Remarkably, the intensities of 4,5‐DHHA and GHB showed a significant positive correlation in control CSF, but not in patient CSF. In an established zebrafish epilepsy model, 4,5‐DHHA showed increased mobility that may reflect limited epileptogenesis. Using untargeted metabolomics, we identified 12 features in CSF with high biomarker potential. These had comparable increased fold changes as GHB and 4,5‐DHHA. For 10 of these features, a similar increase was found in plasma, urine and/or mouse brain tissue for SSADHD compared to controls. One of these was identified as the novel biomarker 4,5‐dihydroxyheptanoic acid. The intensities of selected features in plasma and urine of SSADHD patients positively correlated with the clinical severity score of epilepsy and psychiatric symptoms of those patients, and also showed a high mutual correlation. Our findings provide new insights into the (neuro)metabolic disturbances in SSADHD and give leads for further research concerning SSADHD pathophysiology. [ABSTRACT FROM AUTHOR]

Published
2024
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22. MFG-E8 (LACTADHERIN): a novel marker associated with cerebral amyloid angiopathy

Author

Marazuela, Paula, Solé, Montse, Bonaterra-Pastra, Anna, Pizarro, Jesús, Camacho, Jessica, Martínez-Sáez, Elena, Kuiperij, H. Bea, Verbeek, Marcel M., de Kort, Anna M., Schreuder, Floris H. B. M., Klijn, Catharina J. M., Castillo-Ribelles, Laura, Pancorbo, Olalla, Rodríguez-Luna, David, Pujadas, Francesc, Delgado, Pilar, and Hernández-Guillamon, Mar

Published
2021
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27. Longitudinal cerebrospinal fluid biomarker trajectories along the Alzheimer's disease continuum in the BIOMARKAPD study

Author

Lleó, Alberto, Alcolea, Daniel, Martínez-Lage, Pablo, Scheltens, Philip, Parnetti, Lucilla, Poirier, Judes, Simonsen, Anja H., Verbeek, Marcel M., Rosa-Neto, Pedro, Slot, Rosalinde E.R., Tainta, Mikel, Izaguirre, Andrea, Reijs, Babette L.R., Farotti, Lucia, Tsolaki, Magda, Vandenbergue, Rik, Freund-Levi, Yvonne, Verhey, Frans R.J., Clarimón, Jordi, Fortea, Juan, Frolich, Lutz, Santana, Isabel, Molinuevo, José Luis, Lehmann, Sylvain, Visser, Pieter J., Teunissen, Charlotte E., Zetterberg, Henrik, and Blennow, Kaj

Published
2019
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28. Autoimmune Encephalitis Resembling Dementia Syndromes

Author

Bastiaansen, Anna E.M., van Steenhoven, Robin W., de Bruijn, Marienke A.A.M., Crijnen, Yvette S., van Sonderen, Agnes, van Coevorden-Hameete, Marleen H., Nühn, Marieke M., Verbeek, Marcel M., Schreurs, Marco W.J., Sillevis Smitt, Peter A.E., de Vries, Juna M., Jan de Jong, Frank, and Titulaer, Maarten J.

Published
2021
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30. Prevalence of the apolipoprotein E ε4 allele in amyloid β positive subjects across the spectrum of Alzheimer's disease

Author

Mattsson, Niklas, Groot, Colin, Jansen, Willemijn J., Landau, Susan M., Villemagne, Victor L., Engelborghs, Sebastiaan, Mintun, Mark M., Lleo, Alberto, Molinuevo, José Luis, Jagust, William J., Frisoni, Giovanni B., Ivanoiu, Adrian, Chételat, Gaël, Resende de Oliveira, Catarina, Rodrigue, Karen M., Kornhuber, Johannes, Wallin, Anders, Klimkowicz-Mrowiec, Aleksandra, Kandimalla, Ramesh, Popp, Julius, Aalten, Pauline P., Aarsland, Dag, Alcolea, Daniel, Almdahl, Ina S., Baldeiras, Inês, van Buchem, Mark A., Cavedo, Enrica, Chen, Kewei, Cohen, Ann D., Förster, Stefan, Fortea, Juan, Frederiksen, Kristian S., Freund-Levi, Yvonne, Gill, Kiran Dip, Gkatzima, Olymbia, Grimmer, Timo, Hampel, Harald, Herukka, Sanna-Kaisa, Johannsen, Peter, van Laere, Koen, de Leon, Mony J., Maier, Wolfgang, Marcusson, Jan, Meulenbroek, Olga, Møllergård, Hanne M., Morris, John C., Mroczko, Barbara, Nordlund, Arto, Prabhakar, Sudesh, Peters, Oliver, Rami, Lorena, Rodríguez-Rodríguez, Eloy, Roe, Catherine M., Rüther, Eckart, Santana, Isabel, Schröder, Johannes, Seo, Sang W., Soininen, Hilkka, Spiru, Luiza, Stomrud, Erik, Struyfs, Hanne, Teunissen, Charlotte E., Verhey, Frans R.J., Vos, Stephanie J.B., van Waalwijk van Doorn, Linda J.C., Waldemar, Gunhild, Wallin, Åsa K., Wiltfang, Jens, Vandenberghe, Rik, Brooks, David J., Fladby, Tormod, Rowe, Christopher C., Drzezga, Alexander, Verbeek, Marcel M., Sarazin, Marie, Wolk, David A., Fleisher, Adam S., Klunk, William E., Na, Duk L., Sánchez-Juan, Pascual, Lee, Dong Young, Nordberg, Agneta, Tsolaki, Magda, Camus, Vincent, Rinne, Juha O., Fagan, Anne M., Zetterberg, Henrik, Blennow, Kaj, Rabinovici, Gil D., Hansson, Oskar, van Berckel, Bart N.M., van der Flier, Wiesje M., Scheltens, Philip, Visser, Pieter Jelle, and Ossenkoppele, Rik

Published
2018
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31. Cerebral tryptophan metabolism and outcome of tuberculous meningitis: an observational cohort study

Author

van Laarhoven, Arjan, Dian, Sofiati, Aguirre-Gamboa, Raúl, Avila-Pacheco, Julian, Ricaño-Ponce, Isis, Ruesen, Carolien, Annisa, Jessi, Koeken, Valerie A C M, Chaidir, Lidya, Li, Yang, Achmad, Tri Hanggono, Joosten, Leo A B, Notebaart, Richard A, Ruslami, Rovina, Netea, Mihai G, Verbeek, Marcel M, Alisjahbana, Bachti, Kumar, Vinod, Clish, Clary B, Ganiem, A Rizal, and van Crevel, Reinout

Published
2018
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40. Validation of a quantitative cerebrospinal fluid alpha-synuclein assay in a European-wide interlaboratory study

Author

Kruse, Niels, Persson, Staffan, Alcolea, Daniel, Bahl, Justyna M.C., Baldeiras, Ines, Capello, Elisabetta, Chiasserini, Davide, Bocchio Chiavetto, Luisella, Emersic, Andreja, Engelborghs, Sebastiaan, Eren, Erden, Fladby, Tormod, Frisoni, Giovanni, García-Ayllón, María-Salud, Genc, Sermin, Gkatzima, Olymbia, Heegaard, Niels H.H., Janeiro, André M., Kováčech, Branislav, Kuiperij, H. Bea, Leitão, Maria J., Lleó, Alberto, Martins, Madalena, Matos, Mafalda, Mollergard, Hanne M., Nobili, Flavio, Öhrfelt, Annika, Parnetti, Lucilla, de Oliveira, Catarina Resende, Rot, Uros, Sáez-Valero, Javier, Struyfs, Hanne, Tanassi, Julia T., Taylor, Peggy, Tsolaki, Magda, Vanmechelen, Eugeen, Verbeek, Marcel M., Zilka, Norbert, Blennow, Kaj, Zetterberg, Henrik, and Mollenhauer, Brit

Published
2015
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42. Activation of TNF Receptor 2 Improves Synaptic Plasticity and Enhances Amyloid-β Clearance in an Alzheimer's Disease Mouse Model with Humanized TNF Receptor 2.

Author

Ortí-Casañ, Natalia, Wajant, Harald, Kuiperij, H. Bea, Hooijsma, Annelien, Tromp, Leon, Poortman, Isabelle L., Tadema, Norick, de Lange, Julia H.E., Verbeek, Marcel M., De Deyn, Peter P., Naud, Petrus J.W., and Eisel, Ulrich L.M.

Subjects
ALZHEIMER'S disease, TUMOR necrosis factor receptors, NEUROPLASTICITY, LABORATORY mice, ANIMAL disease models
Abstract

Background: Tumor necrosis factor-alpha (TNF-α) is a master cytokine involved in a variety of inflammatory and neurological diseases, including Alzheimer's disease (AD). Therapies that block TNF-α proved ineffective as therapeutic for neurodegenerative diseases, which might be explained by the opposing functions of the two receptors of TNF (TNFRs): while TNFR1 stimulation mediates inflammatory and apoptotic pathways, activation of TNFR2 is related to neuroprotection. Despite the success of targeting TNFR2 in a transgenic AD mouse model, research that better mimics the human context is lacking. Objective: The aim of this study is to investigate whether stimulation of TNFR2 with a TNFR2 agonist is effective in activating human TNFR2 and attenuating AD neuropathology in the J20xhuTNFR2-k/i mouse model. Methods: Transgenic amyloid-β (Aβ)-overexpressing mice containing a human extracellular TNFR2 domain (J20xhuTNFR2-k/i) were treated with a TNFR2 agonist (NewStar2). After treatment, different behavioral tests and immunohistochemical analysis were performed to assess different parameters, such as cognitive functions, plaque deposition, synaptic plasticity, or microglial phagocytosis. Results: Treatment with NewStar2 in J20xhuTNFR2-k/i mice resulted in a drastic decrease in plaque load and beta-secretase 1 (BACE-1) compared to controls. Moreover, TNFR2 stimulation increased microglial phagocytic activity, leading to enhanced Aβ clearance. Finally, activation of TNFR2 rescued cognitive impairments and improved synaptic plasticity. Conclusion: Our findings demonstrate that activation of human TNFR2 ameliorates neuropathology and improves cognitive functions in an AD mouse model. Moreover, our study confirms that the J20xhuTNFR2-k/i mouse model is suitable for testing human TNFR2-specific compounds. [ABSTRACT FROM AUTHOR]

Published
2023
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43. Plasma amyloid beta 42 is a biomarker for patients with hereditary, but not sporadic, cerebral amyloid angiopathy.

Author

de Kort, Anna M., Kuiperij, H. Bea, Jäkel, Lieke, Kersten, Iris, Rasing, Ingeborg, van Etten, Ellis S., van Rooden, Sanneke, van Osch, Matthias J. P., Wermer, Marieke J. H., Terwindt, Gisela M., Schreuder, Floris H. B. M., Klijn, Catharina J. M., and Verbeek, Marcel M.

Subjects
CEREBRAL amyloid angiopathy, AMYLOID, BIOMARKERS
Abstract

Background: The diagnosis of probable cerebral amyloid angiopathy (CAA) is currently mostly based on characteristics of brain MRI. Blood biomarkers would be a cost-effective, easily accessible diagnostic method that may complement diagnosis by MRI and aid in monitoring disease progression. We studied the diagnostic potential of plasma Aβ38, Aβ40, and Aβ42 in patients with hereditary Dutch-type CAA (D-CAA) and sporadic CAA (sCAA). Methods: All Aβ peptides were quantified in the plasma by immunoassays in a discovery cohort (11 patients with presymptomatic D-CAA and 24 patients with symptomatic D-CAA, and 16 and 24 matched controls, respectively) and an independent validation cohort (54 patients with D-CAA, 26 presymptomatic and 28 symptomatic, and 39 and 46 matched controls, respectively). In addition, peptides were quantified in the plasma in a group of 61 patients with sCAA and 42 matched controls. We compared Aβ peptide levels between patients and controls using linear regression adjusting for age and sex. Results: In the discovery cohort, we found significantly decreased levels of all Aβ peptides in patients with presymptomatic D-CAA (Aβ38: p < 0.001; Aβ40: p = 0.009; Aβ42: p < 0.001) and patients with symptomatic D-CAA (Aβ38: p < 0.001; Aβ40: p = 0.01; Aβ42: p < 0.001) compared with controls. In contrast, in the validation cohort, plasma Aβ38, Aβ40, and Aβ42 were similar in patients with presymptomatic D-CAA and controls (Aβ38: p = 0.18; Aβ40: p = 0.28; Aβ42: p = 0.63). In patients with symptomatic D-CAA and controls, plasma Aβ38 and Aβ40 were similar (Aβ38: p = 0.14; Aβ40: p = 0.38), whereas plasma Aβ42 was significantly decreased in patients with symptomatic D-CAA (p = 0.033). Plasma Aβ38, Aβ40, and Aβ42 levels were similar in patients with sCAA and controls (Aβ38: p = 0.092; Aβ40: p = 0.64. Aβ42: p = 0.68). Conclusions: Plasma Aβ42 levels, but not plasma Aβ38 and Aβ40, may be used as a biomarker for patients with symptomatic D-CAA. In contrast, plasma Aβ38, Aβ40, and Aβ42 levels do not appear to be applicable as a biomarker in patients with sCAA. [ABSTRACT FROM AUTHOR]

Published
2023
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45. Time trends in demographic characteristics of participants and outcome measures in Parkinson’s disease research: A 19-year single-center experience

Author

Maas, Bart R., Bloem, Bastiaan R., Ben-Shlomo, Yoav, Evers, Luc J.W., Helmich, Rick C., Kalf, Johanna G., van der Marck, Marjolein A., Meinders, Marjan J., Nieuwboer, Alice, Nijkrake, Maarten J., Nonnekes, Jorik, Post, Bart, Sturkenboom, Ingrid H.W.M., Verbeek, Marcel M., de Vries, Nienke M., van de Warrenburg, Bart, van de Zande, Tessa, Munneke, Marten, and Darweesh, Sirwan K.L.

Published
2023
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49. Mutations in CYB561 Causing a Novel Orthostatic Hypotension Syndrome

Author

van den Berg, Maarten P., Almomani, Rowida, Biaggioni, Italo, van Faassen, Martijn, van der Harst, Pim, Silljé, Herman H.W., Mateo Leach, Irene, Hemmelder, Marc H., Navis, Gerjan, Luijckx, Gert Jan, de Brouwer, Arjan P.M., Venselaar, Hanka, Verbeek, Marcel M., van der Zwaag, Paul A., Jongbloed, Jan D.H., van Tintelen, J. Peter, Wevers, Ron A., and Kema, Ido P.

Published
2018
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50. Multicenter evaluation of neurofilaments in early symptom onset amyotrophic lateral sclerosis

Author

Feneberg, Emily, Oeckl, Patrick, Steinacker, Petra, Verde, Federico, Barro, Christian, Van Damme, Philip, Gray, Elizabeth, Grosskreutz, Julian, Jardel, Claude, Kuhle, Jens, Koerner, Sonja, Lamari, Foudil, Amador, Maria del Mar, Mayer, Benjamin, Morelli, Claudia, Muckova, Petra, Petri, Susanne, Poesen, Koen, Raaphorst, Joost, Salachas, François, Silani, Vincenzo, Stubendorff, Beatrice, Turner, Martin R., Verbeek, Marcel M., Weishaupt, Jochen H., Weydt, Patrick, Ludolph, Albert C., and Otto, Markus

Published
2018
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