Search results for: Giuseppe Legname

Items from 1 to 20 out of 55 results

article

Expression pattern of perilipins in human brain during aging and in Alzheimer's disease

Maria Conte, Valentina Medici, Davide Malagoli, Antonio Chiariello, more

Neuropathology and Applied Neurobiology > 48 > 1 > n/a - n/a

Aims Perilipins are conserved proteins that decorate intracellular lipid droplets and are essential for lipid metabolism. To date, there is limited knowledge on their expression in human brain or their involvement in brain aging and neurodegeneration. The aim of this study was to characterise the expression levels of perilipins (Plin1–Plin5) in different cerebral areas from subjects of different...

article

The uptake of tau amyloid fibrils is facilitated by the cellular prion protein and hampers prion propagation in cultured cells

Elena De Cecco, Luigi Celauro, Silvia Vanni, Micaela Grandolfo, more

Journal of Neurochemistry > 155 > 5 > 577 - 591

Tauopathies are prevalent, invariably fatal brain diseases for which no cure is available. Tauopathies progressively affect the brain through cell‐to‐cell transfer of tau protein amyloids, yet the spreading mechanisms remain unknown. Here we show that the cellular prion protein (PrP^C) facilitates the uptake of tau aggregates by cultured cells, possibly by acting as an endocytic receptor. In mouse...

article

Brain aging: A Ianus‐faced player between health and neurodegeneration

Silvia Vanni, Arianna Colini Baldeschi, Marco Zattoni, Giuseppe Legname

Journal of Neuroscience Research > 98 > 2 > 299 - 311

Neurodegenerative diseases are incurable debilitating disorders characterized by structural and functional neuronal loss. Approximately 30 million people are affected worldwide, and this number is predicted to reach more than 150 million by 2050. Neurodegenerative disorders include Alzheimer’s, Parkinson’s, and prion diseases among others. These disorders are characterized by the accumulation of aggregating...

article

Efficient RT-QuIC seeding activity for α-synuclein in olfactory mucosa samples of patients with Parkinson’s disease and multiple system atrophy

Chiara Maria Giulia De Luca, Antonio Emanuele Elia, Sara Maria Portaleone, Federico Angelo Cazzaniga, more

Translational Neurodegeneration > 2019 > 8 > 1 > 1-14

Background Parkinson’s disease (PD) is a neurodegenerative disorder whose diagnosis is often challenging because symptoms may overlap with neurodegenerative parkinsonisms. PD is characterized by intraneuronal accumulation of abnormal α-synuclein in brainstem while neurodegenerative parkinsonisms might be associated with accumulation of either α-synuclein, as in the case of Multiple System Atrophy...

article

Prion Efficiently Replicates in α-Synuclein Knockout Mice

Edoardo Bistaffa, Martina Rossi, Chiara Maria Giulia Luca, Federico Cazzaniga, more

Molecular Neurobiology > 2019 > 56 > 11 > 7448-7457

Prion diseases are a group of neurodegenerative disorders associated with the conformational conversion of the cellular prion protein (PrP^C) into an abnormal misfolded form named PrP^Sc. Other than accumulating in the brain, PrP^Sc can bind PrP^C and force it to change conformation to PrP^Sc. The exact mechanism which underlies the process of PrP^C/PrP^Sc conversion still needs to be defined and many molecules...

article

Copper Binding Regulates Cellular Prion Protein Function

Xuan T. A. Nguyen, Thanh Hoa Tran, Dan Cojoc, Giuseppe Legname

Molecular Neurobiology > 2019 > 56 > 9 > 6121-6133

The cellular prion protein (PrP^C), mainly known for its role in neurodegenerative diseases, is involved in several physiological processes including neuritogenesis. In addition, its ability to bind copper or zinc has been suggested for its role in metal homeostasis. Although PrP^C has been known as a copper-binding molecule, little is known about how copper can affect PrP^C physiological functions....

article

Prions Strongly Reduce NMDA Receptor S-Nitrosylation Levels at Pre-symptomatic and Terminal Stages of Prion Diseases

Elisa Meneghetti, Lisa Gasperini, Tommaso Virgilio, Fabio Moda, more

Molecular Neurobiology > 2019 > 56 > 9 > 6035-6045

Prion diseases are fatal neurodegenerative disorders characterized by the cellular prion protein (PrP^C) conversion into a misfolded and infectious isoform termed prion or PrP^Sc. The neuropathological mechanism underlying prion toxicity is still unclear, and the debate on prion protein gain- or loss-of-function is still open. PrP^C participates to a plethora of physiological mechanisms. For instance,...

article

Clinical and neuropathological phenotype associated with the novel V189I mutation in the prion protein gene

Giuseppe Di Fede, Marcella Catania, Cristiana Atzori, Fabio Moda, more

Acta Neuropathologica Communications > 2019 > 7 > 1 > 1-11

Prion diseases are neurodegenerative disorders which are caused by an accumulation of the abnormal, misfolded prion protein known as scrapie prion protein (PrP^Sc). These disorders are unique as they occur as sporadic, genetic and acquired forms. Sporadic Creutzfeldt-Jakob Disease (CJD) is the most common human prion disease, accounting for approximately 85–90% of cases, whereas autosomal dominant...

article

Synthetic Prion Selection and Adaptation

Edoardo Bistaffa, Fabio Moda, Tommaso Virgilio, Ilaria Campagnani, more

Molecular Neurobiology > 2019 > 56 > 4 > 2978-2989

Prion pathologies are characterized by the conformational conversion of the cellular prion protein (PrP^C) into a pathological infectious isoform, known as PrP^Sc. The latter acquires different abnormal conformations, which are associated with specific pathological phenotypes. Recent evidence suggests that prions adapt their conformation to changes in the context of replication. This phenomenon is known...

article

Glia-to-neuron transfer of miRNAs via extracellular vesicles: a new mechanism underlying inflammation-induced synaptic alterations

Ilaria Prada, Martina Gabrielli, Elena Turola, Alessia Iorio, more

Acta Neuropathologica > 2018 > 135 > 4 > 529-550

Recent evidence indicates synaptic dysfunction as an early mechanism affected in neuroinflammatory diseases, such as multiple sclerosis, which are characterized by chronic microglia activation. However, the mode(s) of action of reactive microglia in causing synaptic defects are not fully understood. In this study, we show that inflammatory microglia produce extracellular vesicles (EVs) which are enriched...

article

Identification of novel fluorescent probes preventing PrPSc replication in prion diseases

Ludovica Zaccagnini, Simone Brogi, Margherita Brindisi, Sandra Gemma, more

European Journal of Medicinal Chemistry > 2017 > 127 > C > 859-873

Prion diseases are serious, not curable neurodegenerative disorders caused by the accumulation of the misfolded protein PrP^Sc that represents the pathological variant of the normally folded cellular protein PrP^C. Molecules that bind the cellular isoform PrP^C preventing its misfolding, could arrest the progression of pathological conditions related to the abnormal PrP protein. In this context, by combining...

article

Synthetic prions and other human neurodegenerative proteinopathies

Nhat Tran Thanh Le, Joanna Narkiewicz, Suzana Aulić, Giulia Salzano, more

Virus Research > 2015 > 207 > Complete > 25-37

Transmissible spongiform encephalopathies (TSE) are a heterogeneous group of neurodegenerative disorders. The common feature of these diseases is the pathological conversion of the normal cellular prion protein (PrP^C) into a β-structure-rich conformer-termed PrP^Sc. The latter can induce a self-perpetuating process leading to amplification and spreading of pathological protein assemblies. Much evidence...

article

Gene expression profiling of cjd brains: Validation of a novel disease signature for neurodegeneration in primates

Silvia Vanni, Maura Barbisin, Fabio Moda, Tommaso Virgilio, more

Alzheimer's & Dementia: The Journal of the Alzheimer's Association > 2015 > 11 > 7 Supplement > P646

article

Fibrils of alpha-synuclein interact with prion protein: A putative overlap of two neurodegenerative diseases

Suzana Aulic, Elisa Isopi, Lara Masperone, Giuseppe Legname

Alzheimer's & Dementia: The Journal of the Alzheimer's Association > 2015 > 11 > 7 Supplement > P363

article

Effect of extracellular vesicles derived from distinct brain cells on Aβ toxicity and assembly: focus on Microglia derived vesicles

Pooja Joshi, Elena Turola, Ana Ruiz, Alessandra Bergami, more

SpringerPlus > 2015 > 4 > 1 > 1-32

article

Structural Determinants in Prion Protein Folding and Stability

Federico Benetti, Xevi Biarnés, Francesco Attanasio, Gabriele Giachin, more

Journal of Molecular Biology > 2014 > 426 > 22 > 3796-3810

Prions are responsible for a heterogeneous group of fatal neurodegenerative diseases, involving post-translational modifications of the cellular prion protein. Epidemiological studies on Creutzfeldt-Jakob disease, a prototype prion disorder, show a majority of cases being sporadic, while the remaining occurrences are either genetic or iatrogenic. The molecular mechanisms by which PrP^C is converted...

article

Humic substances interfere with detection of pathogenic prion protein

Christen B. Smith, Clarissa J. Booth, Tyler J. Wadzinski, Giuseppe Legname, more

Soil Biology and Biochemistry > 2014 > 68 > Complete > 309-316

Studies examining the persistence of prions (the etiological agent of transmissible spongiform encephalopathies) in soil require accurate quantification of pathogenic prion protein (PrP^TSE) extracted from or in the presence of soil particles. Here, we demonstrate that natural organic matter (NOM) in soil impacts PrP^TSE detection by immunoblotting. Methods commonly used to extract PrP^TSE from soils...

article

Corrigendum to “Common Structural Traits across Pathogenic Mutants of the Human Prion Protein and Their Implications for Familial Prion Diseases” [J. Mol. Biol. 411 (2011) 700–712]

Giulia Rossetti, Xiaojing Cong, Rocco Caliandro, Giuseppe Legname, more

Journal of Molecular Biology > 2012 > 422 > 1 > 157

article

A small chemical library of 2-aminoimidazole derivatives as BACE-1 inhibitors: Structure-based design, synthesis, and biological evaluation

Gianpaolo Chiriano, Angela De Simone, Francesca Mancini, Daniel I. Perez, more

European Journal of Medicinal Chemistry > 2012 > 48 > Complete > 206-213

In this work, we report a rational structure-based approach aimed at the discovery of new 2-aminoimidazoles as β-secretase inhibitors. Taking advantage of a microwave-assisted synthetic protocol, a small library of derivatives was obtained and biologically evaluated. Two compounds showed promising activities in both enzymatic and cellular assays. Moreover, one of them exhibited the capability to cross...

article

Toward the Molecular Basis of Inherited Prion Diseases: NMR Structure of the Human Prion Protein with V210I Mutation

Ivana Biljan, Gregor Ilc, Gabriele Giachin, Andrea Raspadori, more

Journal of Molecular Biology > 2011 > 412 > 4 > 660-673

The development of transmissible spongiform encephalopathies (TSEs) is associated with the conversion of the cellular prion protein (PrP ^C ) into a misfolded, pathogenic isoform (PrP ^Sc ). Spontaneous generation of PrP ^Sc in inherited forms of disease is caused by mutations in gene coding for PrP (PRNP). In this work, we describe the NMR solution-state structure of the truncated...

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INFONA - science communication portal

Search results for: Giuseppe Legname

Expression pattern of perilipins in human brain during aging and in Alzheimer's disease

The uptake of tau amyloid fibrils is facilitated by the cellular prion protein and hampers prion propagation in cultured cells

Brain aging: A Ianus‐faced player between health and neurodegeneration

Efficient RT-QuIC seeding activity for α-synuclein in olfactory mucosa samples of patients with Parkinson’s disease and multiple system atrophy

Prion Efficiently Replicates in α-Synuclein Knockout Mice

Copper Binding Regulates Cellular Prion Protein Function

Prions Strongly Reduce NMDA Receptor S-Nitrosylation Levels at Pre-symptomatic and Terminal Stages of Prion Diseases

Clinical and neuropathological phenotype associated with the novel V189I mutation in the prion protein gene

Synthetic Prion Selection and Adaptation

Glia-to-neuron transfer of miRNAs via extracellular vesicles: a new mechanism underlying inflammation-induced synaptic alterations

Identification of novel fluorescent probes preventing PrPSc replication in prion diseases

Synthetic prions and other human neurodegenerative proteinopathies

Gene expression profiling of cjd brains: Validation of a novel disease signature for neurodegeneration in primates

Fibrils of alpha-synuclein interact with prion protein: A putative overlap of two neurodegenerative diseases

Effect of extracellular vesicles derived from distinct brain cells on Aβ toxicity and assembly: focus on Microglia derived vesicles

Structural Determinants in Prion Protein Folding and Stability

Humic substances interfere with detection of pathogenic prion protein

Corrigendum to “Common Structural Traits across Pathogenic Mutants of the Human Prion Protein and Their Implications for Familial Prion Diseases” [J. Mol. Biol. 411 (2011) 700–712]

A small chemical library of 2-aminoimidazole derivatives as BACE-1 inhibitors: Structure-based design, synthesis, and biological evaluation

Toward the Molecular Basis of Inherited Prion Diseases: NMR Structure of the Human Prion Protein with V210I Mutation

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