Search

Your search keyword '"Hoylaerts, M. F."' showing total 202 results
Start Over Author "Hoylaerts, M. F."
202 results on '"Hoylaerts, M. F."'

1. Haemostasis

Author

Arnout, J., Hoylaerts, M. F., Lijnen, H. R., Starke, K., editor, Born, G. V. R., editor, Duckles, S. P., editor, Eichelbaum, M., editor, Ganten, D., editor, Hofmann, F., editor, Rosenthal, W., editor, Rubanyi, G., editor, Moncada, Salvador, editor, and Higgs, Annie, editor

Published
2006
Full Text
View/download PDF

35. ZBTB12 DNA methylation is associated with coagulation- and inflammation-related blood cell parameters: findings from the Moli-family cohort

Author

Noro, F., Gianfagna, F., Gialluisi, A., De Curtis, A., Di Castelnuovo, A., Napoleone, E., Cerletti, C., Donati, M. B., de Gaetano, G., Hoylaerts, M. F., Iacoviello, L., Izzi, B., Vohnout, B., Arca, M., Lorenzet, R., di Castelnuovo, A., Costanzo, S., di Giuseppe, R., Cutrone, A., Magnacca, S., Crescente, M., Pampuch, A., Tamburrelli, C., Zurlo, F., and Nanni, L.

Subjects
Male, 0301 basic medicine, Myocardial Infarction, Cohort Studies, Pathogenesis, Blood cell, Leukocyte Count, 0302 clinical medicine, PLATELET, Genetics (clinical), Genetics & Heredity, DNA methylation, Granulocyte counts, White blood cell counts, Whole blood coagulation time, Zinc fingers, Cardiovascular risk, Principal Component Analysis, DNA methylation, TRANSCRIPTIONAL REGULATION, Methylation, Middle Aged, Blood Coagulation Factors, DNA-Binding Proteins, MEDITERRANEAN DIET, Haematopoiesis, Granulocyte counts, Zinc fingers, medicine.anatomical_structure, Oncology, CpG site, MONOCYTES, 030220 oncology & carcinogenesis, Female, Life Sciences & Biomedicine, Adult, Biology, Granulocyte, REGION, Young Adult, 03 medical and health sciences, ADHERENCE, White blood cell, Cardiovascular risk, White blood cell counts, Whole blood coagulation time, Genetics, medicine, Humans, Blood Coagulation, Molecular Biology, Science & Technology, Tumor Necrosis Factor-alpha, Research, 030104 developmental biology, TISSUE FACTOR, Immunology, CpG Islands, Granulocytes, Transcription Factors, Developmental Biology
Abstract

Background Zinc finger and BTB domain-containing protein 12 (ZBTB12) is a predicted transcription factor with potential role in hematopoietic development. Recent evidence linked low methylation level of ZBTB12 exon1 to myocardial infarction (MI) risk. However, the role of ZBTB12 in the pathogenesis of MI and cardiovascular disease in general is not yet clarified. We investigated the relation between ZBTB12 methylation and several blood parameters related to cardio-cerebrovascular risk in an Italian family-based cohort. Results ZBTB12 methylation was analyzed on white blood cells from the Moli-family cohort using the Sequenom EpiTYPER MassARRAY (Agena). A total of 13 CpG Sequenom units were analyzed in the small CpG island located in the only translated ZBTB12 exon. Principal component analysis (PCA) was performed to identify groups of CpG units with similar methylation estimates. Linear mixed effect regressions showed a positive association between methylation of ZBTB12 Factor 2 (including CpG units 8, 9–10, 16, 21) and TNF-ɑ stimulated procoagulant activity, a measure of procoagulant and inflammatory potential of blood cells. In addition, we also found a negative association between methylation of ZBTB12 Factor 1 (mainly characterized by CpG units 1, 3–4, 5, 11, and 26) and white blood cell and granulocyte counts. An in silico prediction analysis identified granulopoiesis- and hematopoiesis-specific transcription factors to potentially bind DNA sequences encompassing CpG1, CpG3–4, and CpG11. Conclusions ZBTB12 hypomethylation is linked to shorter TNF-ɑ stimulated whole blood coagulation time and increased WBC and granulocyte counts, further elucidating the possible link between ZBTB12 methylation and cardiovascular disease risk. Electronic supplementary material The online version of this article (10.1186/s13148-019-0665-6) contains supplementary material, which is available to authorized users.

Published
2019

36. Variation of PEAR1 DNA methylation influences platelet and leukocyte function

Author

Izzi, B., Gianfagna, F., Yang, W. -Y., Cludts, K., De Curtis, A., Verhamme, P., Di Castelnuovo, A., Cerletti, C., Donati, M. B., De Gaetano, G., Staessen, J. A., Hoylaerts, M. F., Iacoviello, L., Vohnout, B., Arca, M., Lorenzet, R., Costanzo, S., Di Giuseppe, R., Cutrone, A., Magnacca, S., Crescente, M., Pampuch, A., Tamburrelli, C., Napoleone, E., Zurlo, F., and Nanni, L.

Subjects
Adult, Blood Platelets, Male, 0301 basic medicine, medicine.medical_specialty, Population, Receptors, Cell Surface, DNA methylation, leukocyte function, platelet, PEAR1, 030204 cardiovascular system & hematology, Biology, Epigenesis, Genetic, Cohort Studies, Young Adult, 03 medical and health sciences, 0302 clinical medicine, Internal medicine, Leukocytes, Genetics, medicine, Humans, Platelet, Platelet activation, Epigenetics, education, Molecular Biology, Genetics (clinical), epidemiology, public health, epigenetics, platelet aggregation, inflammation, education.field_of_study, Research, Platelet Distribution Width, Methylation, DNA Methylation, Middle Aged, Blood Cell Count, Pedigree, 030104 developmental biology, Endocrinology, Italy, CpG site, Moli-family Investigators, DNA methylation, Female, Developmental Biology
Abstract

BackgroundPlatelet-endothelial aggregation receptor 1 (PEAR-1) is a transmembrane receptor involved in platelet activation and megakaryopoiesis whose expression is driven by DNA methylation.PEAR1variants were associated with differential platelet response to activation and cardiovascular outcomes. We aimed at investigating the link betweenPEAR1methylation and platelet and leukocyte function markers in a family-based population.ResultsWe measuredPEAR1methylation in 605 Moli-family participants with available blood counts, plasma P-selectin and C-reactive protein, whole blood platelet P-selectin, and platelet-leukocyte mixed conjugate measurements. We performed principal component analysis (PCA) to identify groups of highly correlated CpG sites. We used linear mixed regression models (using age, gender, BMI, smoking, alcohol drinking, being a proband for family recruitment, being a member of myocardial infarction (MI) family as fixed effects, and family as a random effect) to evaluate associations betweenPEAR1methylation and phenotypes.PEAR1methylation Factor2, characterized by the previously identified megakaryocyte-specific CpG sites, was inversely associated with platelet-monocyte conjugates, P-selectin, and WBC counts, while positively associated with the platelet distribution width (PDW) and with leukocyte CD11b and L-selectin. Moreover,PEAR1Factor2 methylation was negatively associated with INFLAscore, a low-grade inflammation score. The latter was partially mediated by thePEAR1methylation effect on platelet variables.PEAR1methylation association with WBC measurements and INFLAscore was confirmed in the independent cohort FLEMENGHO.ConclusionsWe report a significant link between epigenetic signatures in a platelet functional gene and inflammation-dependent platelet function variability measured in two independent cohorts.

Published
2019

37. P1576Association of colorectal cancer with genetic and epigenetic variation in PEAR1 - a population-based cohort study

Author

Yang, W.-Y, primary, Izzi, B, additional, Zhang, Z.-Y, additional, Thijs, L, additional, Citterio, L, additional, Wei, F.-F, additional, Salvi, E, additional, Delli Carpini, S, additional, Manuta, P, additional, Kuznetsova, T, additional, Cusi, D, additional, Hoylaerts, M F, additional, Luttun, A, additional, Verhamme, P, additional, and Staessen, J A, additional

Published
2019
Full Text
View/download PDF

38. Leukocyte-derived microparticles in vascular homeostasis

Author

Angelillo-Scherrer Anne, Van Kruchten R, Olieslagers S, Schurgers L J, Verheyen F K, Munnix I C A, Waltenberger J, Angelillo-Scherrer A, Hoylaerts M F, Carmeliet P, and Heemskerk J W M

Subjects
Endothelium, Physiology, Angiogenesis, 030204 cardiovascular system & hematology, Biology, medicine.disease_cause, Proinflammatory cytokine, Neovascularization, 03 medical and health sciences, 0302 clinical medicine, Cell-Derived Microparticles, medicine, Leukocytes, Animals, Homeostasis, Humans, Platelet activation, Endothelial dysfunction, 030304 developmental biology, 0303 health sciences, medicine.disease, Vulnerable plaque, 3. Good health, medicine.anatomical_structure, Cardiovascular Diseases, Hemostasis, Immunology, Disease Progression, Blood Vessels, medicine.symptom, Inflammation Mediators, Cardiology and Cardiovascular Medicine
Abstract

Leukocyte-derived microparticles (LMPs) may originate from neutrophils, monocytes/macrophages, and lymphocytes. They express markers from their parental cells and harbor membrane and cytoplasmic proteins as well as bioactive lipids implicated in a variety of mechanisms, maintaining or disrupting vascular homeostasis. When they carry tissue factor or coagulation inhibitors, they participate in hemostasis and pathological thrombosis. Both proinflammatory and anti-inflammatory processes can be affected by LMPs, thus ensuring an appropriate inflammatory response. LMPs also play a dual role in the endothelium by either improving the endothelial function or inducing an endothelial dysfunction. LMPs are implicated in all stages of atherosclerosis. They circulate at a high level in the bloodstream of patients with high atherothrombotic risk, such as smokers, diabetics, and subjects with obstructive sleep apnea, where their prolonged contact with the vessel wall may contribute to its overall deterioration. Numbering microparticles, including LMPs, might be useful in predicting cardiovascular events. LMPs modify the endothelial function and promote the recruitment of inflammatory cells in the vascular wall, necessary processes for the progression of the atherosclerotic lesion. In addition, LMPs favor the neovascularization within the vulnerable plaque and, in the ruptured plaque, they take part in coagulation and platelet activation. Finally, LMPs participate in angiogenesis. They might represent a novel therapeutic tool to reset the angiogenic switch in pathologies with altered angiogenesis. Additional studies are needed to further investigate the role of LMPs in cardiovascular diseases. However, large-scale studies are currently difficult to set up because microparticle measurement still requires elaborate techniques which lack standardization.

Published
2012
Full Text
View/download PDF

44. Cell signalling

Author

Tsuchiya, K., primary, Shiohira, S., additional, Sugiura, H., additional, Suzuki, M., additional, Okano, K., additional, Nitta, K., additional, Kaesler, N., additional, Immendorf, S., additional, Ouyang, C., additional, Carmeliet, P., additional, Floege, J., additional, Kruger, T., additional, Schlieper, G., additional, Georgescu, A., additional, Kalucka, J., additional, Olbrich, S., additional, Baumgartl, J., additional, Hackenbeck, T., additional, Eckardt, K.-U., additional, Weidemann, A., additional, Chmielewski, S., additional, Olejnik, A., additional, Sikorski, K., additional, Heemann, U., additional, Wesoly, J., additional, Bluyssen, H., additional, Baumann, M., additional, Mekahli, D., additional, Decuypere, J.-P., additional, Missiaen, L., additional, Levtchenko, E., additional, De Smedt, H., additional, Stasi, A., additional, Castellano, G., additional, Gigante, M., additional, Intini, A., additional, Pontrelli, P., additional, Divella, C., additional, Curci, C., additional, Grandaliano, G., additional, Gesualdo, L., additional, Vizza, D., additional, Perri, A., additional, Lofaro, D., additional, Toteda, P., additional, Lupinacci, S., additional, Leone, F., additional, Gigliotti, P., additional, Papalia, T., additional, Bonofiglio, R., additional, Vatazin, A. V., additional, Astakhov, P. V., additional, Zulkarnaev, A. B., additional, Parodi, E., additional, Verzola, D., additional, D'Amato, E., additional, Viazzi, F., additional, Gonnella, A., additional, Garneri, D., additional, Pontremoli, R., additional, Garibotto, G., additional, Chen, T.-H., additional, Chen, C.-H., additional, Chen, Y.-C., additional, Sue, Y.-M., additional, Cheng, C.-Y., additional, Guiying, L., additional, Ying, L., additional, Pozzoli, S., additional, Lino, M., additional, Delli Carpini, S., additional, Ferrandi, M., additional, Zerbini, G., additional, Simonini, M., additional, Zagato, L., additional, Molinari, I., additional, Citterio, L., additional, Manunta, P., additional, Feng, X., additional, Pan, X., additional, Wang, W., additional, Chen, N., additional, Chen, Y.-x., additional, Wang, W.-M., additional, Tanaka, S., additional, Yano, S., additional, Sugimoto, T., additional, Noh, H., additional, Yu, M. R., additional, Kim, H. J., additional, Woo, S. A., additional, Cho, Y. J., additional, Kwon, S. H., additional, Jeon, J. S., additional, Han, D. C., additional, Shimizu, H., additional, Yisireyili, M., additional, Nishijima, F., additional, Niwa, T., additional, Koh, E. S., additional, Chung, S., additional, Kim, S. J., additional, Yoon, H. E., additional, Park, C. W., additional, Chang, Y. S., additional, Shin, S. J., additional, Seong, E. Y., additional, Rhee, H., additional, Shin, M. J., additional, Yang, B. Y., additional, Jung, Y. S., additional, Lee, D. W., additional, Lee, S. B., additional, Kwak, I. S., additional, Kim, I. Y., additional, Sancho-Martinez, S. M., additional, Prieto-Garcia, L., additional, Lopez-Hernandez, F. J., additional, Lopez-Novoa, J. M., additional, Bae, E. H., additional, Choi, H. S., additional, Joo, S. Y., additional, Kim, I. J., additional, Kim, C. S., additional, Choi, J. S., additional, Ma, S. K., additional, Lee, J., additional, Kim, S. W., additional, Humanes, B., additional, Sonia, C., additional, Jado, J., additional, Mojena, M., additional, Lara, J., additional, Alvarez-Sala, L., additional, Tejedor, A., additional, Lazaro, A., additional, Wada, Y., additional, Iyoda, M., additional, Matsumoto, K., additional, Shindo-Hirai, Y., additional, Kuno, Y., additional, Yamamoto, Y., additional, Suzuki, T., additional, Shibata, T., additional, Akizawa, T., additional, Faubel, S., additional, Edelstein, C. L., additional, Cano Penalver, J. L., additional, de Frutos Garcia, S., additional, Griera Merino, M., additional, Luengo Rodriguez, A., additional, Garcia Jerez, A., additional, Bohorquez Magro, L., additional, Medrano, D., additional, Calleros Basilio, L., additional, Rodriguez Puyol, M., additional, Thilo, F., additional, Liu, Y., additional, Tepel, M., additional, Hsu, H.-H., additional, Chen, K.-H., additional, Hung, C.-C., additional, Yang, C.-W., additional, Endlich, N., additional, Lin, J.-L., additional, Pavenstadt, H., additional, Rodrigues Diez, R. R., additional, Mezzano, S., additional, Ruiz-Ortega, M., additional, Rodrigues Diez, R., additional, Lavoz, C., additional, Nakayama, Y., additional, Fukami, K., additional, Yamagishi, S.-i., additional, Obara, N., additional, Yokoro, M., additional, Ando, R., additional, Kaida, Y., additional, Toyonaga, M., additional, Kaifu, K., additional, Takeuchi, M., additional, Ueda, S., additional, Okuda, S., additional, Daenen, K., additional, Hoylaerts, M. F., additional, Bammens, B., additional, Liu, J., additional, Zhong, F., additional, Dai, Q., additional, Xu, L., additional, Zaravinos, A., additional, and Deltas, C. C., additional

Published
2013
Full Text
View/download PDF

50. Haemostasis.

Author

Starke, K., Born, G. V. R., Duckles, S. P., Eichelbaum, M., Ganten, D., Hofmann, F., Rosenthal, W., Rubanyi, G., Moncada, Salvador, Higgs, Annie, Arnout, J., Hoylaerts, M. F., and Lijnen, H. R.

Abstract

When the continuity of the vascular endothelium is disrupted, platelets and fibrin seal off the defect. Haemostatic processes are classified as primary (mainly involving platelets) and secondary (mainly related to fibrin formation or blood coagulation). When the blood clot is no longer required for haemostasis, the fibrinolytic system will dissolve it. The pivotal ligand for initial platelet recruitment to injured vessel wall components is von Willebrand factor (vWF), a multimeric protein present in the subendothelium and in plasma, where it is conformationally activated by shear forces. Adhering activated platelets recruit additional platelets, which are in turn activated and form a platelet aggregate. Coagulation is initiated by a reaction, activating factors IX and X. Once critical amounts of factor Xa are generated, thrombin generation is initiated and soluble fibrinogen is converted into insoluble fibrin. Excessive thrombin generation is prevented via inhibition by antithrombin and also via downregulation of its further generation by activation of the protein C pathway. Activation of the fibrinolytic system results from conversion of the proenzyme plasminogen into the active serine proteinase plasmin by tissue-type or urokinase-type plasminogen activators. Plasmin digests the fibrin component of a blood clot. Inhibition of the fibrinolytic system occurs at the level of the plasminogen activator (by plasminogen activator inhibitors) or at the level of plasmin (by α2-antiplasmin). Together, these physiological processes act to maintain normal functioning blood vessels and a non-thrombotic state. [ABSTRACT FROM AUTHOR]

Published
2006
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results