Nucleophosmin contains amyloidogenic regions that are able to form toxic aggregates under physiological conditions (551 views)
The Faseb Journal (ISSN: 1530-6860, 1530-6860electronic), 2015 Sep; 29(9): 3689-3701.
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Paper type: Journal Article,
Impact factor: 5.043, 5-year impact factor: 5.639
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84942900341&partnerID=q2rCbXpz
Keywords: Acute Myeloid Leukemia, Circular Dichroism Spectroscopy, Mtt Assay, Aggregate, Beta Aggregate,
Affiliations:
*** IBB - CNR ***
Department of Pharmacy, Diagnostica e Farmaceutica Molecolari-Società Cooperativa A Responsabilità Limitata, University of Naples Federico II, Via Mezzocannone, 16, Naples, 80134, Italy
Centro Interuniversitario di Ricerca sui Peptidi Bioattivi, University of Naples Federico II, Naples, Italy
Section of Biochemistry, Department of Biomedical Experimental and Clinical Sciences Mario Serio, University of Florence, Florence, Italy
Institute of Biostructures and Bioimaging, Consiglio Nazionale Delle Ricerche, Naples, Italy
Department of Physics, University of Genoa, Genoa, Italy
Department of Medical, Oral, and Biotechnological Sciences, University of Chieti G. d'Annunzio, Chieti, Italy
Institute of Molecular Biology and Pathology, Consiglio Nazionale Delle Ricerche, Rome, Italy
Center for Advanced Biomaterials for Healthcare, Centro Interdipartimentale di Ricerca sui Biomateriali, Istituto Italiano di Tecnologia, Naples, Italy
*Department of Pharmacy, Diagnostica e Farmaceutica Molecolari-Societa Cooperativa a Responsabilita Limitata, Centro Interuniversitario di Ricerca sui Peptidi Bioattivi, University of Naples "Federico II," Naples, Italy; Section of Biochemistry, Department of Biomedical Experimental and Clinical Sciences "Mario Serio," University of Florence, Florence, Italy; Institute of Biostructures and Bioimaging, Consiglio Nazionale delle Ricerche, Naples, Italy; Department of Physics, University of Genoa, Genoa, Italy; Department of Medical, Oral, and Biotechnological Sciences, University of Chieti "G. d'Annunzio," Chieti, Italy; and Institute of Molecular Biology and Pathology, Consiglio Nazionale delle Ricerche, Rome, Italy., *Department of Pharmacy, Diagnostica e Farmaceutica Molecolari-Societa Cooperativa a Responsabilita Limitata, Centro Interuniversitario di Ricerca sui Peptidi Bioattivi, University of Naples "Federico II," Naples, Italy; Section of Biochemistry, Department of Biomedical Experimental and Clinical Sciences "Mario Serio," University of Florence, Flo
References:
Not available.
The Faseb Journal (ISSN: 1530-6860, 1530-6860electronic), 2015 Sep; 29(9): 3689-3701.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 5.043, 5-year impact factor: 5.639
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84942900341&partnerID=q2rCbXpz
Keywords: Acute Myeloid Leukemia, Circular Dichroism Spectroscopy, Mtt Assay, Aggregate, Beta Aggregate,
Affiliations:
*** IBB - CNR ***
Department of Pharmacy, Diagnostica e Farmaceutica Molecolari-Società Cooperativa A Responsabilità Limitata, University of Naples Federico II, Via Mezzocannone, 16, Naples, 80134, Italy
Centro Interuniversitario di Ricerca sui Peptidi Bioattivi, University of Naples Federico II, Naples, Italy
Section of Biochemistry, Department of Biomedical Experimental and Clinical Sciences Mario Serio, University of Florence, Florence, Italy
Institute of Biostructures and Bioimaging, Consiglio Nazionale Delle Ricerche, Naples, Italy
Department of Physics, University of Genoa, Genoa, Italy
Department of Medical, Oral, and Biotechnological Sciences, University of Chieti G. d'Annunzio, Chieti, Italy
Institute of Molecular Biology and Pathology, Consiglio Nazionale Delle Ricerche, Rome, Italy
Center for Advanced Biomaterials for Healthcare, Centro Interdipartimentale di Ricerca sui Biomateriali, Istituto Italiano di Tecnologia, Naples, Italy
*Department of Pharmacy, Diagnostica e Farmaceutica Molecolari-Societa Cooperativa a Responsabilita Limitata, Centro Interuniversitario di Ricerca sui Peptidi Bioattivi, University of Naples "Federico II," Naples, Italy; Section of Biochemistry, Department of Biomedical Experimental and Clinical Sciences "Mario Serio," University of Florence, Florence, Italy; Institute of Biostructures and Bioimaging, Consiglio Nazionale delle Ricerche, Naples, Italy; Department of Physics, University of Genoa, Genoa, Italy; Department of Medical, Oral, and Biotechnological Sciences, University of Chieti "G. d'Annunzio," Chieti, Italy; and Institute of Molecular Biology and Pathology, Consiglio Nazionale delle Ricerche, Rome, Italy., *Department of Pharmacy, Diagnostica e Farmaceutica Molecolari-Societa Cooperativa a Responsabilita Limitata, Centro Interuniversitario di Ricerca sui Peptidi Bioattivi, University of Naples "Federico II," Naples, Italy; Section of Biochemistry, Department of Biomedical Experimental and Clinical Sciences "Mario Serio," University of Florence, Flo
References:
Not available.
Nucleophosmin contains amyloidogenic regions that are able to form toxic aggregates under physiological conditions
Nucleophosmin (NPM)-1 is a multifunctional protein involved in a variety of biologic processes and has been implicated in the pathogenesis of several human malignancies. To gain insight into the role of isolated fragments in NPM1 activities, we dissected the C-terminal domain (CTD) into its helical fragments. In this study, we observed the unexpected structural behavior of the peptide fragment corresponding to helix (H)2 (residues 264-277). This peptide has a strong tendency to form amyloidlike assemblies endowed with fibrillar morphology and beta-sheet structure, under physiologic conditions, as shown by circular dichroism, thioflavin T, and Congo red binding assays; dynamic light scattering; and atomic force microscopy. The aggregates are also toxic to neuroblastoma cells, as determined using 3-(4;5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide reduction and Ca(2+) influx assays. We also found that the extension of the H2 sequence beyond its N terminus, comprising the connecting loop with H1, delayed aggregation and its associated cytotoxicity, suggesting that contiguous regions of H2 have a protective role in preventing aggregation. Our findings and those in the literature suggest that the helical structures present in the CTD are important in preventing harmful aggregation. These findings could elucidate the pathogenesis of acute myeloid leukemia (AML) caused by NPM1 mutants. Because the CTD is not properly folded in these mutants, we hypothesize that the aggregation propensity of this NPM1 region is involved in the pathogenesis of AML. Preliminary assays on NPM1-Cter-MutA, the most frequent AML-CTD mutation, revealed its significant propensity for aggregation. Thus, the aggregation phenomena should be seriously considered in studies aimed at unveiling the molecular mechanisms of this pathology.-Di Natale, C., Scognamiglio, P. L., Cascella, R., Cecchi, C., Russo, A., Leone, M., Penco, A., Relini, A., Federici, L., Di Matteo, A., Chiti, F., Vitagliano, L., Marasco, D. Nucleophosmin contains amyloidogenic regions that are able to form toxic aggregates under physiological conditions.
Nucleophosmin (NPM)-1 is a multifunctional protein involved in a variety of biologic processes and has been implicated in the pathogenesis of several human malignancies. To gain insight into the role of isolated fragments in NPM1 activities, we dissected the C-terminal domain (CTD) into its helical fragments. In this study, we observed the unexpected structural behavior of the peptide fragment corresponding to helix (H)2 (residues 264-277). This peptide has a strong tendency to form amyloidlike assemblies endowed with fibrillar morphology and beta-sheet structure, under physiologic conditions, as shown by circular dichroism, thioflavin T, and Congo red binding assays; dynamic light scattering; and atomic force microscopy. The aggregates are also toxic to neuroblastoma cells, as determined using 3-(4;5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide reduction and Ca(2+) influx assays. We also found that the extension of the H2 sequence beyond its N terminus, comprising the connecting loop with H1, delayed aggregation and its associated cytotoxicity, suggesting that contiguous regions of H2 have a protective role in preventing aggregation. Our findings and those in the literature suggest that the helical structures present in the CTD are important in preventing harmful aggregation. These findings could elucidate the pathogenesis of acute myeloid leukemia (AML) caused by NPM1 mutants. Because the CTD is not properly folded in these mutants, we hypothesize that the aggregation propensity of this NPM1 region is involved in the pathogenesis of AML. Preliminary assays on NPM1-Cter-MutA, the most frequent AML-CTD mutation, revealed its significant propensity for aggregation. Thus, the aggregation phenomena should be seriously considered in studies aimed at unveiling the molecular mechanisms of this pathology.-Di Natale, C., Scognamiglio, P. L., Cascella, R., Cecchi, C., Russo, A., Leone, M., Penco, A., Relini, A., Federici, L., Di Matteo, A., Chiti, F., Vitagliano, L., Marasco, D. Nucleophosmin contains amyloidogenic regions that are able to form toxic aggregates under physiological conditions.
Nucleophosmin contains amyloidogenic regions that are able to form toxic aggregates under physiological conditions
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Nucleophosmin contains amyloidogenic regions that are able to form toxic aggregates under physiological conditions
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View Export to BibTeX Export to EndNote
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Impact Factor: 2.425
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11 Records (11 excluding Abstracts).
Total impact factor: 45.482 (45.482 excluding Abstracts).
Total 5 year impact factor: 40.879 (40.879 excluding Abstracts).
Total impact factor: 45.482 (45.482 excluding Abstracts).
Total 5 year impact factor: 40.879 (40.879 excluding Abstracts).
551 views. Last view on Thursday 16 January 2025, 6:20:36
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