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Dive into the research topics where Bettina Drisaldi is active.

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Featured researches published by Bettina Drisaldi.


Proceedings of the National Academy of Sciences of the United States of America | 2003

In vivo reduction of amyloid-β by a mutant copper transporter

Amie L. Phinney; Bettina Drisaldi; Stephen D. Schmidt; Stan Lugowski; Veronica A. Coronado; Yan Liang; Patrick Horne; Jing Yang; Joannis Sekoulidis; Janaky Coomaraswamy; M. Azhar Chishti; Diane W. Cox; Paul M. Mathews; Ralph A. Nixon; George A. Carlson; Peter St George-Hyslop; David Westaway

Cu ions have been suggested to enhance the assembly and pathogenic potential of the Alzheimers disease amyloid-β (Aβ) peptide. To explore this relationship in vivo, toxic-milk (txJ) mice with a mutant ATPase7b transporter favoring elevated Cu levels were analyzed in combination with the transgenic (Tg) CRND8 amyloid precursor protein mice exhibiting robust Aβ deposition. Unexpectedly, TgCRND8 mice homozygous for the recessive txJ mutation examined at 6 months of age exhibited a reduced number of amyloid plaques and diminished plasma Aβ levels. In addition, homozygosity for txJ increased survival of young TgCRND8 mice and lowered endogenous CNS Aβ at times before detectable increases in Cu in the CNS. These data suggest that the beneficial effect of the txJ mutation on CNS Aβ burden may proceed by a previously undescribed mechanism, likely involving increased clearance of peripheral pools of Aβ peptide.


Journal of Virology | 2003

Molecular Distinction between Pathogenic and Infectious Properties of the Prion Protein

Roberto Chiesa; Pedro Piccardo; Elena Quaglio; Bettina Drisaldi; San Ling Si-Hoe; Masaki Takao; Bernardino Ghetti; David A. Harris

ABSTRACT Tg(PG14) mice express a prion protein (PrP) with a nine-octapeptide insertion associated with a human familial prion disease. These animals spontaneously develop a fatal neurodegenerative disorder characterized by ataxia, neuronal apoptosis, and accumulation in the brain of an aggregated and weakly protease-resistant form of mutant PrP (designated PG14spon). Brain homogenates from Tg(PG14) mice fail to transmit disease after intracerebral inoculation into recipient mice, indicating that PG14spon, although pathogenic, is distinct from PrPSc, the infectious form of PrP. In contrast, inoculation of Tg(PG14) mice with exogenous prions of the RML strain induces accumulation of PG14RML, a PrPSc form of the mutant protein that is infectious and highly protease resistant. Like PrPSc, both PG14spon and PG14RML display conformationally masked epitopes in the central and octapeptide repeat regions. However, these two forms differ profoundly in their oligomeric states, with PG14RML aggregates being much larger and more resistant to dissociation. Our analysis provides new molecular insight into an emerging puzzle in prion biology, the discrepancy between the infectious and neurotoxic properties of PrP.


The EMBO Journal | 2007

The CNS glycoprotein Shadoo has PrPC-like protective properties and displays reduced levels in prion infections

Joel C. Watts; Bettina Drisaldi; Vivian Ng; Jing Yang; Bob Strome; Patrick Horne; Man-Sun Sy; Larry Yoong; Rebecca Young; Peter Mastrangelo; Catherine Bergeron; Paul E. Fraser; George A. Carlson; Howard T.J. Mount; Gerold Schmitt-Ulms; David Westaway

The cellular prion protein, PrPC, is neuroprotective in a number of settings and in particular prevents cerebellar degeneration mediated by CNS‐expressed Doppel or internally deleted PrP (‘ΔPrP’). This paradigm has facilitated mapping of activity determinants in PrPC and implicated a cryptic PrPC‐like protein, ‘π’. Shadoo (Sho) is a hypothetical GPI‐anchored protein encoded by the Sprn gene, exhibiting homology and domain organization similar to the N‐terminus of PrP. Here we demonstrate Sprn expression and Sho protein in the adult CNS. Sho expression overlaps PrPC, but is low in cerebellar granular neurons (CGNs) containing PrPC and high in PrPC‐deficient dendritic processes. In Prnp0/0 CGNs, Sho transgenes were PrPC‐like in their ability to counteract neurotoxic effects of either Doppel or ΔPrP. Additionally, prion‐infected mice exhibit a dramatic reduction in endogenous Sho protein. Sho is a candidate for π, and since it engenders a PrPC‐like neuroprotective activity, compromised neuroprotective activity resulting from reduced levels may exacerbate damage in prion infections. Sho may prove useful in deciphering several unresolved facets of prion biology.


Clinics in Laboratory Medicine | 2003

A murine model of a familial prion disease

David A. Harris; Roberto Chiesa; Bettina Drisaldi; Elena Quaglio; Antonio Migheli; Pedro Piccardo; Bernardino Ghetti

We have produced a mouse model of a familial prion disorder by introduction of a transgene that encodes the moPrP homolog of a nine-octapeptide insertional mutant associated with an inherited form of CJD in humans. These mice develop progressive neurologic symptoms, display neuropathologic changes, and accumulate a form of mutant PrP in their brains and peripheral tissues that displays some of the biochemical properties of PrPSc. These mice have been extremely valuable for analyzing the cellular and biochemical mechanisms involved in inherited prion disorders and correlating the appearance of the PrPSc-like form with clinical and neuropathologic findings. Because the mutant protein in the mice is highly neurotoxic but appears to lack infectivity, further analysis of its properties promises to shed new light on the molecular distinction between pathogenic and infectious forms of PrP.


Neurobiology of Aging | 2000

A transgenic model of a familial prion disease

David A. Harris; Roberto Chiesa; Bettina Drisaldi; Elena Quaglio; Antonio Migheli; Pedro Piccardo; Bernardino Ghetti

We have generated lines of transgenic mice that express a mutant prion protein containing 14 octapeptide repeats whose human homologue is associated with an inherited prion dementia. These mice develop an ataxic illness that begins at 65 days of age when the transgene array is homozygous, and results in death by 115-138 days. Starting from birth, mutant PrP is converted into a protease-resistant and detergent-insoluble form that resembles PrP(Sc), and this form accumulates dramatically in many brain regions throughout the lifetime of the mice. As PrP accumulates, there is massive apoptosis of cerebellar granule cells, as well as astrocytosis and deposition of PrP in a punctate pattern. These results establish a new transgenic animal model of an inherited human prion disease, and provide important insights into the molecular pathogenesis of these disorders.


Journal of Biological Chemistry | 2003

Mutant PrP is delayed in its exit from the endoplasmic reticulum, but neither wild-type nor mutant PrP undergoes retrotranslocation prior to proteasomal degradation.

Bettina Drisaldi; Richard S. Stewart; Cheryl Adles; Leanne R. Stewart; Elena Quaglio; Emiliano Biasini; Luana Fioriti; Roberto Chiesa; David A. Harris


Proceedings of the National Academy of Sciences of the United States of America | 2000

Accumulation of protease-resistant prion protein (PrP) and apoptosis of cerebellar granule cells in transgenic mice expressing a PrP insertional mutation

Roberto Chiesa; Bettina Drisaldi; Elena Quaglio; Antonio Migheli; Pedro Piccardo; Bernardino Ghetti; David A. Harris


Molecular Biology of the Cell | 2001

A Transmembrane Form of the Prion Protein Contains an Uncleaved Signal Peptide and Is Retained in the Endoplasmic Reticululm

Richard S. Stewart; Bettina Drisaldi; David A. Harris


Archive | 2007

The CNS glycoprotein Shadoo has PrP C -like protective properties and displays reduced levels in prion infections This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits distribution, and reproduction in any medium, provided the original author and source are credited. This license does not permit commercial exploitation or the creation of derivative works without specific permission.

Joel C. Watts; Bettina Drisaldi; Vivian Ng; Jing Yang; Bob Strome; Patrick Horne; Larry K.K. Yoong; Rebecca Young; Peter Mastrangelo; Catherine Bergeron; Paul E. Fraser; Howard T.J. Mount; Gerold Schmitt-Ulms; David Westaway


Alzheimers & Dementia | 2006

P4-282: Effects of indirubin, a GSK3/CDK5 inhibitor, on the Aβ and tau pathways of Alzheimer’s Disease

Sun-Kyong Lee; Erwan Paitel; Bettina Drisaldi; Agnès Petit; Stephen D. Schmidt; Paul M. Mathews; Fusheng Chen; Paul E. Fraser; Peter St George-Hyslop; Laurent Meijer; David Westaway

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Elena Quaglio

Washington University in St. Louis

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Roberto Chiesa

Mario Negri Institute for Pharmacological Research

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Jing Yang

University of Alberta

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