ParkinsonCanadaV1, Main, Exploration, bibRecord, 000523

Sustained Systemic Glucocerebrosidase Inhibition Induces Brain α-Synuclein Aggregation, Microglia and Complement C1q Activation in Mice.

Identifieur interne : 000523 ( Main/Exploration ); précédent : 000522; suivant : 000524

Sustained Systemic Glucocerebrosidase Inhibition Induces Brain α-Synuclein Aggregation, Microglia and Complement C1q Activation in Mice.

Auteurs : Emily M. Rocha [États-Unis] ; Gaynor A. Smith [États-Unis] ; Eric Park [États-Unis] ; Hongmei Cao [États-Unis] ; Anne-Renee Graham [États-Unis] ; Eilish Brown [États-Unis] ; Jesse R. Mclean [États-Unis] ; Melissa A. Hayes [États-Unis] ; Jonathan Beagan [États-Unis] ; Sarah C. Izen [États-Unis] ; Eduardo Perez-Torres [États-Unis] ; Penelope J. Hallett [États-Unis] ; Ole Isacson [États-Unis]

Source :

Antioxidants & redox signaling [ 1557-7716 ] ; 2015.

RBID : pubmed:26094487

English descriptors

KwdEn :
- Animals, Autophagy, Axonal Transport, Cerebral Cortex (metabolism), Cerebral Cortex (pathology), Complement Activation, Complement C1q (metabolism), Glucosylceramidase (antagonists & inhibitors), Glucosylceramidase (metabolism), Inositol (analogs & derivatives), Inositol (pharmacology), Male, Mice, Microglia (physiology), Parkinson Disease, Secondary (chemically induced), Parkinson Disease, Secondary (enzymology), Protein Aggregation, Pathological (chemically induced), Protein Aggregation, Pathological (enzymology), Proteins (metabolism), Synaptic Transmission, alpha-Synuclein (metabolism).
MESH :
- chemical , analogs & derivatives : Inositol.
- chemical , antagonists & inhibitors : Glucosylceramidase.
- chemical , metabolism : Complement C1q, Glucosylceramidase, Proteins, alpha-Synuclein.
- chemically induced : Parkinson Disease, Secondary, Protein Aggregation, Pathological.
- enzymology : Parkinson Disease, Secondary, Protein Aggregation, Pathological.
- metabolism : Cerebral Cortex.
- pathology : Cerebral Cortex.
- chemical , pharmacology : Inositol.
- physiology : Microglia.
- Animals, Autophagy, Axonal Transport, Complement Activation, Male, Mice, Synaptic Transmission.

Abstract

Loss-of-function mutations in GBA1, which cause the autosomal recessive lysosomal storage disease, Gaucher disease (GD), are also a key genetic risk factor for the α-synucleinopathies, including Parkinson's disease (PD) and dementia with Lewy bodies. GBA1 encodes for the lysosomal hydrolase glucocerebrosidase and reductions in this enzyme result in the accumulation of the glycolipid substrates glucosylceramide and glucosylsphingosine. Deficits in autophagy and lysosomal degradation pathways likely contribute to the pathological accumulation of α-synuclein in PD. In this report we used conduritol-β-epoxide (CBE), a potent selective irreversible competitive inhibitor of glucocerebrosidase, to model reduced glucocerebrosidase activity in vivo, and tested whether sustained glucocerebrosidase inhibition in mice could induce neuropathological abnormalities including α-synucleinopathy, and neurodegeneration.

DOI: 10.1089/ars.2015.6307
PubMed: 26094487

Affiliations:

Le document en format XML

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<term>Complement Activation</term>
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<front><div type="abstract" xml:lang="en">Loss-of-function mutations in GBA1, which cause the autosomal recessive lysosomal storage disease, Gaucher disease (GD), are also a key genetic risk factor for the α-synucleinopathies, including Parkinson's disease (PD) and dementia with Lewy bodies. GBA1 encodes for the lysosomal hydrolase glucocerebrosidase and reductions in this enzyme result in the accumulation of the glycolipid substrates glucosylceramide and glucosylsphingosine. Deficits in autophagy and lysosomal degradation pathways likely contribute to the pathological accumulation of α-synuclein in PD. In this report we used conduritol-β-epoxide (CBE), a potent selective irreversible competitive inhibitor of glucocerebrosidase, to model reduced glucocerebrosidase activity in vivo, and tested whether sustained glucocerebrosidase inhibition in mice could induce neuropathological abnormalities including α-synucleinopathy, and neurodegeneration.</div>
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<region><li>Massachusetts</li>
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<tree><country name="États-Unis"><region name="Massachusetts"><name sortKey="Rocha, Emily M" sort="Rocha, Emily M" uniqKey="Rocha E" first="Emily M" last="Rocha">Emily M. Rocha</name>
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<name sortKey="Beagan, Jonathan" sort="Beagan, Jonathan" uniqKey="Beagan J" first="Jonathan" last="Beagan">Jonathan Beagan</name>
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<name sortKey="Hayes, Melissa A" sort="Hayes, Melissa A" uniqKey="Hayes M" first="Melissa A" last="Hayes">Melissa A. Hayes</name>
<name sortKey="Isacson, Ole" sort="Isacson, Ole" uniqKey="Isacson O" first="Ole" last="Isacson">Ole Isacson</name>
<name sortKey="Izen, Sarah C" sort="Izen, Sarah C" uniqKey="Izen S" first="Sarah C" last="Izen">Sarah C. Izen</name>
<name sortKey="Mclean, Jesse R" sort="Mclean, Jesse R" uniqKey="Mclean J" first="Jesse R" last="Mclean">Jesse R. Mclean</name>
<name sortKey="Park, Eric" sort="Park, Eric" uniqKey="Park E" first="Eric" last="Park">Eric Park</name>
<name sortKey="Perez Torres, Eduardo" sort="Perez Torres, Eduardo" uniqKey="Perez Torres E" first="Eduardo" last="Perez-Torres">Eduardo Perez-Torres</name>
<name sortKey="Smith, Gaynor A" sort="Smith, Gaynor A" uniqKey="Smith G" first="Gaynor A" last="Smith">Gaynor A. Smith</name>
</country>
</tree>
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       | NlmPubMed2Wicri -a ParkinsonCanadaV1

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La maladie de Parkinson au Canada (serveur d'exploration)

Sustained Systemic Glucocerebrosidase Inhibition Induces Brain α-Synuclein Aggregation, Microglia and Complement C1q Activation in Mice.

Sustained Systemic Glucocerebrosidase Inhibition Induces Brain α-Synuclein Aggregation, Microglia and Complement C1q Activation in Mice.

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	La maladie de Parkinson au Canada (serveur d'exploration)
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