Loss of porin function in dopaminergic neurons of Drosophila is suppressed by Buffy
Identifieur interne : 000296 ( Main/Exploration ); précédent : 000295; suivant : 000297Loss of porin function in dopaminergic neurons of Drosophila is suppressed by Buffy
Auteurs : P. Githure M Ngale ; Brian E. StaveleySource :
- Journal of Biomedical Science [ 1021-7770 ] ; 2016.
English descriptors
- KwdEn :
- Animals, Disease Models, Animal, Dopaminergic Neurons (metabolism), Dopaminergic Neurons (pathology), Drosophila Proteins (biosynthesis), Drosophila Proteins (genetics), Drosophila melanogaster (genetics), Gene Expression Regulation, Humans, Mitochondria (genetics), Mitochondria (pathology), Parkinson Disease (genetics), Parkinson Disease (pathology), Porins (genetics), Proto-Oncogene Proteins c-bcl-2 (biosynthesis), Proto-Oncogene Proteins c-bcl-2 (genetics).
- MESH :
- chemical , biosynthesis : Drosophila Proteins, Proto-Oncogene Proteins c-bcl-2.
- chemical , genetics : Drosophila Proteins, Porins, Proto-Oncogene Proteins c-bcl-2.
- genetics : Drosophila melanogaster, Mitochondria, Parkinson Disease.
- metabolism : Dopaminergic Neurons.
- pathology : Dopaminergic Neurons, Mitochondria, Parkinson Disease.
- Animals, Disease Models, Animal, Gene Expression Regulation, Humans.
Abstract
Mitochondrial porin, also known as the voltage-dependent anion channel (VDAC), is a multi-functional channel protein that shuttles metabolites between the mitochondria and the cytosol and implicated in cellular life and death decisions. The inhibition of
Loss of
The expression of
The inhibition of
Url:
DOI: 10.1186/s12929-016-0300-1
PubMed: 27881168
PubMed Central: 5122015
Affiliations:
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Le document en format XML
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function in dopaminergic neurons of Drosophila is suppressed by <italic>Buffy</italic>
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<author><name sortKey="M Ngale, P Githure" sort="M Ngale, P Githure" uniqKey="M Ngale P" first="P. Githure" last="M Ngale">P. Githure M Ngale</name>
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<wicri:noCountry code="subfield">Newfoundland & Labrador A1B 3X9 Canada</wicri:noCountry>
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<author><name sortKey="Staveley, Brian E" sort="Staveley, Brian E" uniqKey="Staveley B" first="Brian E." last="Staveley">Brian E. Staveley</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Loss of <italic>porin</italic>
function in dopaminergic neurons of Drosophila is suppressed by <italic>Buffy</italic>
</title>
<author><name sortKey="M Ngale, P Githure" sort="M Ngale, P Githure" uniqKey="M Ngale P" first="P. Githure" last="M Ngale">P. Githure M Ngale</name>
<affiliation><nlm:aff id="Aff1">Department of Biology, Memorial University of Newfoundland, St. John’s, Newfoundland & Labrador A1B 3X9 Canada</nlm:aff>
<wicri:noCountry code="subfield">Newfoundland & Labrador A1B 3X9 Canada</wicri:noCountry>
</affiliation>
</author>
<author><name sortKey="Staveley, Brian E" sort="Staveley, Brian E" uniqKey="Staveley B" first="Brian E." last="Staveley">Brian E. Staveley</name>
<affiliation><nlm:aff id="Aff1">Department of Biology, Memorial University of Newfoundland, St. John’s, Newfoundland & Labrador A1B 3X9 Canada</nlm:aff>
<wicri:noCountry code="subfield">Newfoundland & Labrador A1B 3X9 Canada</wicri:noCountry>
</affiliation>
</author>
</analytic>
<series><title level="j">Journal of Biomedical Science</title>
<idno type="ISSN">1021-7770</idno>
<idno type="eISSN">1423-0127</idno>
<imprint><date when="2016">2016</date>
</imprint>
</series>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term>
<term>Disease Models, Animal</term>
<term>Dopaminergic Neurons (metabolism)</term>
<term>Dopaminergic Neurons (pathology)</term>
<term>Drosophila Proteins (biosynthesis)</term>
<term>Drosophila Proteins (genetics)</term>
<term>Drosophila melanogaster (genetics)</term>
<term>Gene Expression Regulation</term>
<term>Humans</term>
<term>Mitochondria (genetics)</term>
<term>Mitochondria (pathology)</term>
<term>Parkinson Disease (genetics)</term>
<term>Parkinson Disease (pathology)</term>
<term>Porins (genetics)</term>
<term>Proto-Oncogene Proteins c-bcl-2 (biosynthesis)</term>
<term>Proto-Oncogene Proteins c-bcl-2 (genetics)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Drosophila Proteins</term>
<term>Proto-Oncogene Proteins c-bcl-2</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Drosophila Proteins</term>
<term>Porins</term>
<term>Proto-Oncogene Proteins c-bcl-2</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Drosophila melanogaster</term>
<term>Mitochondria</term>
<term>Parkinson Disease</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Dopaminergic Neurons</term>
</keywords>
<keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Dopaminergic Neurons</term>
<term>Mitochondria</term>
<term>Parkinson Disease</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Disease Models, Animal</term>
<term>Gene Expression Regulation</term>
<term>Humans</term>
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<front><div type="abstract" xml:lang="en"><sec><title>Background</title>
<p>Mitochondrial porin, also known as the voltage-dependent anion channel (VDAC), is a multi-functional channel protein that shuttles metabolites between the mitochondria and the cytosol and implicated in cellular life and death decisions. The inhibition of <italic>porin</italic>
under the control of neuronal <italic>Ddc-Gal4</italic>
result in short lifespan and in an age-dependent loss in locomotor function, phenotypes that are strongly associated with Drosophila models of Parkinson disease.</p>
</sec>
<sec><title>Methods</title>
<p>Loss of <italic>porin</italic>
function was achieved through exploitation of RNA interference while derivative lines were generated by homologous recombination and tested by PCR. The <italic>UAS/Gal4</italic>
expression system was exploited with directed expression in neurons achieved with the use of the <italic>Dopa decarboxylase</italic>
and in the developing eye with the <italic>Glass multiple reporter</italic>
transgenes. Statistical analyses for ageing assay employed Log rank (Mantel-Cox) test, climbing indices were fitted with a non-linear curve and confidence intervals compared at 95%. Biometric analysis of the eye phenotypes was obtained by unpaired student <italic>T</italic>
-test.</p>
</sec>
<sec><title>Results</title>
<p>The expression of <italic>α-synuclein</italic>
in neuronal populations that include dopamine producing neurons under the control of <italic>Ddc-Gal4</italic>
produces a robust Parkinson disease model, and results in severely reduced lifespan and locomotor dysfunction. In addition, the <italic>porin</italic>
-induced phenotypes are greatly suppressed when the pro-survival <italic>Bcl-2</italic>
homologue <italic>Buffy</italic>
is overexpressed in these neurons and in the developing eye adding to the cellular advantages of altered expression of this anti-apoptotic gene. When we co-expressed <italic>α-synuclein</italic>
along with <italic>porin</italic>
, it results in a decrease in lifespan and impaired climbing ability. This enhancement of the <italic>α-synuclein-</italic>
induced phenotypes observed in neurons was demonstrated in the neuron rich eye, where the simultaneous co-expression of <italic>porin-RNAi</italic>
and <italic>α-synuclein</italic>
resulted in an enhanced eye phenotype, marked by reduced number of ommatidia and increased disarray of the ommatidia.</p>
</sec>
<sec><title>Conclusions</title>
<p>The inhibition of <italic>porin</italic>
in dopaminergic neurons among others result in reduced lifespan and age-dependent loss in climbing ability, phenotypes that are suppressed by the overexpression of the sole pro-survival <italic>Bcl-2</italic>
homologue <italic>Buffy</italic>
. The inhibition of <italic>porin</italic>
phenocopies Parkinson disease phenotypes in Drosophila, while the overexpression of <italic>Buffy</italic>
can counteract these phenotypes to improve the overall “healthspan” of the organism.</p>
</sec>
</div>
</front>
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