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207 results on '"Mazzanti B."'

3. A unique neuroendocrine cell model derived from the human foetal neural crest

Author

Rapizzi, E., Benvenuti, S., Deledda, C., Martinelli, S., Sarchielli, E., Fibbi, B., Luciani, P., Mazzanti, B., Pantaleo, M., Marroncini, G., Vannelli, G. B., Maggi, M., Mannelli, M., Luconi, M., and Peri, A.

Abstract

Purpose: Nowadays, no human neuroendocrine cell models derived from the neural crest are available. In this study, we present non-transformed long-term primary Neural Crest Cells (NCCs) isolated from the trunk region of the neural crest at VIII–XII gestational weeks of human foetuses obtained from voluntary legal abortion. Methods and results: In NCC, quantitative real-time RT PCR demonstrated the expression of neural crest specifier genes, such as Snail1, Snail2/SLUG, Sox10, FoxD3, c-Myc, and p75NTR. Moreover, these cell populations expressed stemness markers (such as Nanog and nestin), as well as markers of motility and invasion (TAGLN, MMP9, CXCR4, and CXCR7), and of neuronal/glial differentiation (MAP2, GFAP, SYP, and TAU). Functional analysis demonstrated that these cells not only possessed high migration properties, but most importantly, they expressed markers of sympatho-adrenal lineage, such as ASCL1 and tyrosine hydroxylase (TH). Moreover, the expression of TH increased after the induction with two different protocols of differentiation towards neuronal and sympatho-adrenal phenotypes. Finally, exposure to conditioned culture media from NCC induced a mature phenotype in a neuronal cell model (namely SH-SY5Y), suggesting that NCC may also act like Schwann precursors. Conclusion: This unique human cell model provides a solid tool for future studies addressing the bases of human neural crest-derived neuroendocrine tumours.

Published
2024
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26. Evidence of DMSO-Induced Protein Aggregation in Cells

Author

Giugliarelli, A., primary, Urbanelli, L., additional, Ricci, M., additional, Paolantoni, M., additional, Emiliani, C., additional, Saccardi, R., additional, Mazzanti, B., additional, Lombardini, L., additional, Morresi, A., additional, and Sassi, P., additional

Published
2016
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27. The glycopeptide CSF114(Glc) detects serum antibodies in multiple sclerosis

Author

Lolli, F, Mazzanti, B, Pazzagli, M, Peroni, E, Alcaro, Mc, Sabatino, G, Lanzillo, R, Morra, Vb, Santoro, L, Gasperini, C, Galgani, S, D'Elios, Mm, Zipoli, V, Sotgiu, S, Pugliatti, Maura, Rovero, P, Chelli, M, Papini, Am, RI Lolli Francesco/C 6439 2008, Lolli, F, Mazzanti, B, Pazzagli, M, Peroni, E, Alcaro, Mc, Sabatino, G, Lanzillo, Roberta, BRESCIA MORRA, Vincenzo, Santoro, L, Gasperini, C, Galgani, S, D'Elios, Mm, Zipoli, V, Sotgiu, S, Pugliatti, M, Rovero, P, Chelli, M, and Papini, Am

Subjects
Adult, Male, Multiple Sclerosis, Anti-nuclear antibody, Adolescent, diagnosis, Immunology, Enzyme-Linked Immunosorbent Assay, myelin autoantibodies, medicine.disease_cause, multiple sclerosis, glycosylated antigen, B cell, autoimmunity, Aged, Analysis of Variance, Antibodies, Female, Flow Cytometry, Humans, Middle Aged, ROC Curve, Sensitivity and Specificity, Glycopeptides, Subclass, Autoimmunity, medicine, Immunology and Allergy, biology, business.industry, Multiple sclerosis, medicine.disease, Glycopeptide, Neurology, biology.protein, Neurology (clinical), Antibody, business, Meningitis, Encephalitis
Abstract

Synthetic glycopeptides have the potential to detect antibodies in multiple sclerosis (MS). In the present study, we analyzed the antibodies (IgM class, IgG class and IgG subclasses) to the synthetic glycopeptide CSF114(Glc) in the serum of 186 MS patients, 166 blood donors (BDs), 25 patients affected by meningitis/encephalitis, 41 affected by systemic lupus erythematosus (SLE) and 49 affected by rheumatoid arthritis (RA). The IgM antibody level to CSF114(Glc) was significantly increased in MS patients versus BDs (p

Published
2005

28. Mesenchymal Stem Cell-Based Immunomodulation in Allogeneic Heterotopic Heart-Lung Transplantation

Author

Longoni, Biancamaria, Szilàgyi, E, Puviani, L, Mazzanti, B, Paoli, Gt, Urbani, S, Quaranta, P, Antonini, S, Tripodi, S, Caselli, C, Cintorino, M, Saccardi, R, Nardo, B, and Mosca, F.

Subjects
Lung, business.industry, Mesenchymal stem cell, Cell, Hematopoietic stem cell, In vitro, medicine.anatomical_structure, In vivo, Immunology, Cancer research, medicine, Cytokine secretion, business, Heart-Lung Transplantation
Abstract

Mesenchymal stem cells are able to differentiate in various cell lineages and they have shown immunomodulatory properties in vitro, altering the cytokine secretion profile of T helper, T effector and dendritic cells and stimulating natural killer cells towards an anti-inflammatory and tolerant phenotype. In vivo they prolong skin allograft survival and may decrease graft-versus-host disease after hematopoietic stem cell transplants. In this work we studied the effects of mesenchymal stem cell treatment in an allogeneic heterotopic heart-lung transplant model. The following experimental groups were formed: A) Control B) Immunosuppressive therapy (Cyclosporine A) C) Mesenchymal stem-cell intravenous infusion D) Mesenchymal stem-cell infusion plus immunosuppressive treatment. The infusion of mesenchymal stem cells improved the mean graft survival up to 14.5±3.7 days with respect to the control group (3±0.6 days). Treatment with Cyclosporine A plus mesenchymal stem cells (group D) produced a mean survival time of 18.25±4.9 days, and was not significantly different to the results for group B (21.75±3.5 days). Furthermore, in the immunosuppressive treatment and the mesenchymal stem cell treatment, histological analysis revealed a reduction in the grade of rejection in heart and lung grafts. This decrease was most significant in group D. In conclusion, mesenchymal stem cells alone or in combination with Cyclosporine A were able to prolong graft survival time. These data suggest that, in vivo, mesenchymal stem cells retain their ability, already shown in vitro, to suppress lymphocyte activation and proliferation.

Published
2012
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38. Dalla scala locale alla scala regionale: la pluviometria del bacino del fiume Arno come segnale del cambiamento climatico del Mediterraneo

Author

Gozzini B., Baldi M., Maracchi G., Meneguzzo F., Pasqui M., Piani F., Crisci A., Magno R., Guarnieri F., Genesio L., De Chiara G., Fibbi L., Marrese F., Mazzanti B., and Menduni G.

Abstract

Notevole è stato negli ultimi anni lo sforzo dell'intera comunità scientifica nel valutare l'impatto dei cambiamenti climatici nel ciclo dell'acqua soprattutto a scala regionale e locale. L'interesse pratico infatti risiede a scala di bacino laddove la gestione della risorsa acqua è più critica. Questo lavoro rappresenta lo sforzo congiunto di stimare i cambiamenti climatici in atto e futuri sul bacino del fiume Arno a partire dai dati in situ, dataset globali e scenari climatici in relazione al fenomeno climatico del Monsone dell'Africa occidentale. In particolare si è cercato di caratterizzare la distribuzione di precipitazione stagionale nella sua evoluzione passata e futura.

Published
2007

50. A synthetic glycopeptide of human myelin oligodendrocyte glycoprotein to detect antibody responses in multiple sclerosis and other neurological diseases

Author

Mazzucco, S, Mat, S, Vergelli, M, Fioresi, R, Nardi, E, Mazzanti, B, Chelli, M, Lolli, Francesco, Ginanneschi, M, Pinto, F, Massacesi, Luca, Papini, A. M., and Papini, Anna Maria

Subjects
Multiple Sclerosis, Clinical Biochemistry, Pharmaceutical Science, Enzyme-Linked Immunosorbent Assay, Biochemistry, Antibodies, Myelin oligodendrocyte glycoprotein, Myelin, Drug Discovery, medicine, Humans, Amino Acids, Molecular Biology, Glycopeptides, MOG, Multiple sclerosis, chemistry.chemical_classification, biology, Chemistry, Organic Chemistry, Amyotrophic Lateral Sclerosis, Syndrome, Myelitis, medicine.disease, Molecular biology, Molecular medicine, Oligodendrocyte, Glycopeptide, carbohydrates (lipids), Myelin-Associated Glycoprotein, medicine.anatomical_structure, Mutagenesis, Immunology, biology.protein, Molecular Medicine, Encephalitis, Myelin-Oligodendrocyte Glycoprotein, Antibody, Glycoprotein, Myelin Proteins
Abstract

Glycopeptides of hMOG(30-50) containing a glucosyl moiety on the side-chains of Asn, Ser or Hyp at position 31 were synthesised. Antibody titres to hMOG(30-50) and to its glucoderivatives were measured by ELISA in sera of patients affected by different neurological diseases. Anti-hMOG(30-50) antibodies were detected only using the glycopeptide [Asn31(N-Glc)]hMOG(30-50).

Published
1999

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