Search results for: Amanda N. Sacino

Items from 1 to 9 out of 9 results

article

Fragile X-associated tremor ataxia syndrome with co-occurrent progressive supranuclear palsy-like neuropathology

Amanda N. Sacino, Stefan Prokop, Meggen A. Walsh, Jennifer Adamson, more

Acta Neuropathologica Communications > 2019 > 7 > 1 > 1-4

Co-occurrence of multiple neuropathologic changes is a common phenomenon, most prominently seen in Alzheimer’s disease (AD) and Parkinson’s disease (PD), complicating clinical diagnosis and patient management. Reports of co-occurring pathological processes are emerging in the group of genetically defined repeat-associated non-AUG (RAN)-translation related diseases. Here we report a case of Fragile...

article

Comparative analyses of the in vivo induction and transmission of α-synuclein pathology in transgenic mice by MSA brain lysate and recombinant α-synuclein fibrils

Jess-Karan S. Dhillon, Jorge A. Trejo-Lopez, Cara Riffe, Yona Levites, more

Acta Neuropathologica Communications > 2019 > 7 > 1 > 1-13

α-synuclein (αS) is the major component of several types of brain pathological inclusions that define neurodegenerative diseases termed synucleinopathies. Central nervous system (CNS) inoculation studies using either in vitro polymerized αS fibrils or in vivo derived lysates containing αS aggregates to induce the progressive spread of αS inclusion pathology in animal disease models have supported...

article

Proteolysis of α‐synuclein fibrils in the lysosomal pathway limits induction of inclusion pathology

Amanda N. Sacino, Mieu M. Brooks, Paramita Chakrabarty, Kaustuv Saha, more

Journal of Neurochemistry > 140 > 4 > 662 - 678

Progression of α‐synuclein inclusion pathology may occur through cycles of release and uptake of α‐synuclein aggregates, which induce additional intracellular α‐synuclein inclusion pathology. This process may explain (i) the presence of α‐synuclein inclusion pathology in grafted cells in human brains, and (ii) the slowly progressive nature of most human α‐synucleinopathies. It also provides a rationale...

article

Non-prion-type transmission in A53T α-synuclein transgenic mice: a normal component of spinal homogenates from naïve non-transgenic mice induces robust α-synuclein pathology

Amanda N. Sacino, Jacob I. Ayers, Mieu M. T. Brooks, Paramita Chakrabarty, more

Acta Neuropathologica > 2016 > 131 > 1 > 151-154

Electronic supplementary material The online version of this article (doi: 10.1007/s00401-015-1505-1 ) contains supplementary material, which is available to authorized users.

article

Inefficient induction and spread of seeded tau pathology in P301L mouse model of tauopathy suggests inherent physiological barriers to transmission

Paramita Chakrabarty, Vincent J. Hudson III, Amanda N. Sacino, Mieu My Thi Brooks, more

Acta Neuropathologica > 2015 > 130 > 2 > 303-305

Electronic supplementary material The online version of this article (doi: 10.1007/s00401-015-1444-x ) contains supplementary material, which is available to authorized users.

article

Studies of lipopolysaccharide effects on the induction of α-synuclein pathology by exogenous fibrils in transgenic mice

Nicola J. Rutherford, Amanda N. Sacino, Mieu Brooks, Carolina Ceballos-Diaz, more

Molecular Neurodegeneration > 2015 > 10 > 1 > 1-13

Background Parkinson’s disease (PD) is a progressive neurodegenerative disorder that is pathologically characterized by loss of dopaminergic neurons from the substantia nigra, the presence of aggregated α-synuclein (αS) and evidence of neuroinflammation. Experimental studies have shown that the cerebral injection of recombinant fibrillar αS, especially in αS transgenic mouse models, can...

article

Amyloidogenic α-synuclein seeds do not invariably induce rapid, widespread pathology in mice

Amanda N. Sacino, Mieu Brooks, Michael A. Thomas, Alex B. McKinney, more

Acta Neuropathologica > 2014 > 127 > 5 > 645-665

In order to further evaluate the parameters whereby intracerebral administration of recombinant α-synuclein (αS) induces pathological phenotypes in mice, we conducted a series of studies where αS fibrils were injected into the brains of M83 (A53T) and M47 (E46K) αS transgenic (Tg) mice, and non-transgenic (nTg) mice. Using multiple markers to assess αS inclusion formation, we find that injected fibrillar...

article

Erratum to: Amyloidogenic α-synuclein seeds do not invariably induce rapid, widespread pathology in mice

Amanda N. Sacino, Mieu Brooks, Michael A. Thomas, Alex B. McKinney, more

Acta Neuropathologica > 2014 > 128 > 6 > 897-898

article

Does a prion-like mechanism play a major role in the apparent spread of α-synuclein pathology?

Amanda N Sacino, Benoit I Giasson

Alzheimer's Research & Therapy > 2012 > 4 > 6 > 1-5

Parkinson's disease, the most common movement disorder, results in an insidious reduction for patients in quality of life and ability to function. A hallmark of Parkinson's disease is the brain accumulation of neuronal cytoplasmic inclusions comprised of the protein α-synuclein. The presence of α-synuclein brain aggregates is observed in several neurodegenerative diseases, including dementia with...

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