Evidence map›Paper›PMID 35606853›Full record

ArticleActa neuropathologica communications2022

Analysis of hemisphere-dependent effects of unilateral intrastriatal injection of α-synuclein pre-formed fibrils on mitochondrial protein levels, dynamics, and function.

Rose B Creed, Adeel A Memon, Sindhu P Komaragiri, Sandeep K Barodia, Matthew S Goldberg

Open access · goldAbstract read
In one paragraph

Article in Acta neuropathologica communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.4field-weighted citation impact, top 18% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

9 citing papers in PubMed, 13 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Rose B CreedCenter for Neurodegeneration and Experimental Therapeutics, The University of Alabama at Birmingham, Birmingham, AL, 35294, USA.
Adeel A MemonCenter for Neurodegeneration and Experimental Therapeutics, The University of Alabama at Birmingham, Birmingham, AL, 35294, USA.
Sindhu P KomaragiriCenter for Neurodegeneration and Experimental Therapeutics, The University of Alabama at Birmingham, Birmingham, AL, 35294, USA.
Sandeep K BarodiaCenter for Neurodegeneration and Experimental Therapeutics, The University of Alabama at Birmingham, Birmingham, AL, 35294, USA.
Matthew S GoldbergCenter for Neurodegeneration and Experimental Therapeutics, The University of Alabama at Birmingham, Birmingham, AL, 35294, USA. mattgoldberg@uab.edu.ORCID 0000-0002-5172-9841
University of Alabama at Birmingham · US

Funding

UAB Research Education Program for Residents and Fellows in NeuroscienceR25NS079188 · NINDS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI STANDAERT, DAVID G. · 2012 to 2022
$1.1M
Role of alpha synuclein in PINK1-linked Parkinson's diseaseF99NS108458 · NINDS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI CREED, ROSE BERTHE · 2018 to 2019
$74k
NINDS NIH HHS F99 NS108458NINDS NIH HHS F99NS108458NINDS NIH HHS R25 NS079188
6 · The paper itself

Abstract

Genetic and neuropathological evidence strongly implicates aberrant forms of α-synuclein in neurodegeneration. Antibodies specific for α-synuclein phosphorylated at serine 129 (pS129) are selective for the pathological protein aggregates that are characteristic of Parkinson's disease (PD) and other synucleinopathies, such as dementia with Lewy bodies (DLB) and multiple system atrophy (MSA). Although the etiology of most synucleinopathies remains uncertain, a large body of evidence points to mitochondrial dysfunction. The recent development of animal models based on intracranial injection of α-synuclein pre-formed fibrils (PFFs) has provided a valuable experimental system in which to study the spread and neurotoxicity of α-synuclein aggregates, yet the effects of PFF-induced protein aggregates on mitochondrial function and dynamics have not been rigorously examined in vivo. To help fill this knowledge gap, we injected the striatum of mice unilaterally with well-characterized small length (< 30 nm) PFFs or monomeric α-synuclein control and measured the distribution and extent of pS129 α-synuclein-immunoreactive aggregates, the loss of tyrosine hydroxylase-immunoreactive neurons in the substantia nigra, the abundance of mitochondrial proteins, and the activity of mitochondrial respiratory chain components at 3 months and 6 months post injection. Intrastriatal injection of small length PFFs, but not monomeric α-synuclein control, induced robust pS129 α-synuclein immunoreactive inclusions in the cortex, ventral midbrain, and striatum, as well as in rarely reported brain regions, such as the hippocampus, as early as 3 months post injection. Significant loss of nigral tyrosine hydroxylase-immunoreactive neurons was observed in the PFF-injected hemisphere at 3 months and 6 months post injection. The unilateral striatal injection of small length PFFs also caused hemisphere-dependent and treatment-dependent changes in the cortical levels of mitochondrial proteins such as VDAC1, COX-IV, and DRP-1, as well as functional changes in mitochondrial complex I activity in the contralateral striatum. Together, these data demonstrate that intrastriatal injection of mice with small length PFFs induces extensive bilateral protein aggregates, significant unilateral nigral cell loss, and altered contralateral levels of mitochondrial proteins and respiratory chain activity. Our data suggest this animal model may be useful for studying the role of mitochondrial dysfunction in α-synucleinopathies, for studying the hemisphere-dependent effects of α-synuclein aggregates, and for testing neuroprotective therapies that target mitochondrial dysfunction and protein aggregation.

Indexed as

alpha-SynucleinSynucleinopathiesAnimalsMiceMitochondrial ProteinsProtein AggregatesTyrosine 3-Monooxygenasealpha-SynucleinMitochondrial ProteinsProtein AggregatesTyrosine 3-MonooxygenaseAggregationLewy bodiesMitochondriaParkinson’s diseasePre-formed fibrilsSynuclein

Identifiers

PMID35606853
PMCPMC9125944
OpenAlexW4281291678

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.