Lysosomal hydrolases in cerebrospinal fluid from subjects with Parkinson's disease.
Identifieur interne : 001C85 ( Ncbi/Curation ); précédent : 001C84; suivant : 001C86Lysosomal hydrolases in cerebrospinal fluid from subjects with Parkinson's disease.
Auteurs : Chiara Balducci [Italie] ; Laura Pierguidi ; Emanuele Persichetti ; Lucilla Parnetti ; Michele Sbaragli ; Carmelo Tassi ; Aldo Orlacchio ; Paolo Calabresi ; Tommaso Beccari ; Aroldo RossiSource :
- Movement disorders : official journal of the Movement Disorder Society [ 0885-3185 ] ; 2007.
English descriptors
- KwdEn :
- MESH :
- chemical , cerebrospinal fluid : Hyaluronoglucosaminidase.
- cerebrospinal fluid : Parkinson Disease.
- methods : Chromatography, Ion Exchange.
- Aged, Female, Humans, Male, Middle Aged, Statistics, Nonparametric.
Abstract
Recent studies have shown a genetic association between glucocerebrosidase deficiencies and Parkinson's disease (PD). To further explore this issue the activity of beta-glucocerebrosidase and the activities of other lysosomal enzymes, alpha-mannosidase, beta-mannosidase, beta-hexosaminidase, and beta-galactosidase have been evaluated in the cerebrospinal fluid (CSF) of PD patients. The activities of alpha-mannosidase, beta-mannosidase, beta-glucocerebrosidase, and beta-hexosaminidase were substantially decreased in the CSF of PD patients, while levels of beta-galactosidase were essentially identical to controls. This study indicates that in PD several lysosomal hydrolases have decreased activities, further supporting a possible link between pathophysiological mechanisms underlying PD and lysosomal hydrolases.
DOI: 10.1002/mds.21399
PubMed: 17546678
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pubmed:17546678Le document en format XML
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<author><name sortKey="Pierguidi, Laura" sort="Pierguidi, Laura" uniqKey="Pierguidi L" first="Laura" last="Pierguidi">Laura Pierguidi</name>
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<affiliation wicri:level="1"><nlm:affiliation>Dipartimento di Medicina Interna, Università degli Studi di Perugia, Perugia, Italy.</nlm:affiliation>
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<author><name sortKey="Parnetti, Lucilla" sort="Parnetti, Lucilla" uniqKey="Parnetti L" first="Lucilla" last="Parnetti">Lucilla Parnetti</name>
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<author><name sortKey="Sbaragli, Michele" sort="Sbaragli, Michele" uniqKey="Sbaragli M" first="Michele" last="Sbaragli">Michele Sbaragli</name>
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<author><name sortKey="Tassi, Carmelo" sort="Tassi, Carmelo" uniqKey="Tassi C" first="Carmelo" last="Tassi">Carmelo Tassi</name>
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<author><name sortKey="Orlacchio, Aldo" sort="Orlacchio, Aldo" uniqKey="Orlacchio A" first="Aldo" last="Orlacchio">Aldo Orlacchio</name>
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<author><name sortKey="Beccari, Tommaso" sort="Beccari, Tommaso" uniqKey="Beccari T" first="Tommaso" last="Beccari">Tommaso Beccari</name>
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<author><name sortKey="Rossi, Aroldo" sort="Rossi, Aroldo" uniqKey="Rossi A" first="Aroldo" last="Rossi">Aroldo Rossi</name>
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<series><title level="j">Movement disorders : official journal of the Movement Disorder Society</title>
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<term>Humans</term>
<term>Hyaluronoglucosaminidase (cerebrospinal fluid)</term>
<term>Male</term>
<term>Middle Aged</term>
<term>Parkinson Disease (cerebrospinal fluid)</term>
<term>Statistics, Nonparametric</term>
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<keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Chromatography, Ion Exchange</term>
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<keywords scheme="MESH" xml:lang="en"><term>Aged</term>
<term>Female</term>
<term>Humans</term>
<term>Male</term>
<term>Middle Aged</term>
<term>Statistics, Nonparametric</term>
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<front><div type="abstract" xml:lang="en">Recent studies have shown a genetic association between glucocerebrosidase deficiencies and Parkinson's disease (PD). To further explore this issue the activity of beta-glucocerebrosidase and the activities of other lysosomal enzymes, alpha-mannosidase, beta-mannosidase, beta-hexosaminidase, and beta-galactosidase have been evaluated in the cerebrospinal fluid (CSF) of PD patients. The activities of alpha-mannosidase, beta-mannosidase, beta-glucocerebrosidase, and beta-hexosaminidase were substantially decreased in the CSF of PD patients, while levels of beta-galactosidase were essentially identical to controls. This study indicates that in PD several lysosomal hydrolases have decreased activities, further supporting a possible link between pathophysiological mechanisms underlying PD and lysosomal hydrolases.</div>
</front>
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</record>
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