Evidence map›Paper›PMID 35112150›Full record

ArticleAnalytical and bioanalytical chemistry2022

Matrisome changes in Parkinson's disease.

Margaret Downs, Manveen K Sethi, Rekha Raghunathan, Matthew D Layne, Joseph Zaia

Open access · greenAbstract read
In one paragraph

Article in Analytical and bioanalytical chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 1 pooled it
3.2field-weighted citation impact, top 7% 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

21 citing papers in PubMed, 1 synthesis or guideline pooled it, 28 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.

Margaret DownsDepartment of Biochemistry, Boston University, Boston, MA, 02118, USA.
Manveen K SethiDepartment of Biochemistry, Boston University, Boston, MA, 02118, USA.
Rekha RaghunathanDepartment of Biochemistry, Boston University, Boston, MA, 02118, USA.
Matthew D LayneDepartment of Biochemistry, Boston University, Boston, MA, 02118, USA.
Joseph ZaiaDepartment of Biochemistry, Boston University, Boston, MA, 02118, USA. jzaia@bu.edu.ORCID http://orcid.org/0000-0001-9497-8701
Boston University · US

Funding

Cerebrovascular Remodeling and Neurodegenerative Changes in Alzheimer's DiseaseR01AG075876 · NIA · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI Thor Stein, JOSEPH ZAIA · 2022 to 2026
$3.9M
Methods for measuring matrisome molecule similarity during disease processesR35GM144090 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI JOSEPH ZAIA · 2022 to 2026
$2.1M
Methods for determination of glycoprotein glycosylation similarities among disease statesR01GM133963 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI ZAIA, JOSEPH · 2019 to 2021
$1.4M
A Thermo-Fisher Scientific Q-Exactive HF Mass Spectrometry SystemS10OD021651 · OD · BOSTON UNIVERSITY MEDICAL CAMPUS · PI ZAIA, JOSEPH · 2016 to 2016
$580k
NIA NIH HHS R01 AG075876NIGMS NIH HHS R01 GM133963NIGMS NIH HHS R35 GM144090NIH HHS R01GM133963 and S10OD021651NIH HHS S10 OD021651
6 · The paper itself

Abstract

Extracellular matrix (ECM) proteins, collectively known as the matrisome, include collagens, glycoproteins, and proteoglycans. Alterations in the matrisome have been implicated in the neurodegenerative pathologies including Parkinson's disease (PD). In this work, we utilized our previously published PD and control proteomics data from human prefrontal cortex and focused our analysis on the matrisome. Among matrisome proteins, we observed a significant enrichment in the expression of type I collagen in PD vs. control samples. We then performed histological analysis on the same samples used for proteomics study, and examined collagen expression using picrosirius red staining. Interestingly, we observed similar trends in collagen abundance in PD vs. control as in our matrisome analysis; thus, this and other histological analyses will be useful as a complementary technique in the future to study the matrisome in PD with a larger cohort, and it may aid in choosing regions of interest for proteomic analysis. Additionally, collagen hydroxyprolination was less variable in PD compared to controls. Glycoproteomic changes in matrisome molecules were also observed in PD relative to aged individuals, especially related to type VI collagen and versican. We further examined the list of differentially expressed matrisome molecules using network topology-based analysis and found that angiogenesis indicated by alterations in decorin and several members of the collagen family was affected in PD. These findings collectively identified matrisome changes associated with PD; further studies with a larger cohort are required to validate the current results.

Indexed as

Extracellular Matrix ProteinsParkinson DiseaseProteomicsAgedExtracellular MatrixHumansProteoglycansExtracellular Matrix ProteinsProteoglycansExtracellular matrixGlycoproteinsMass spectrometryMatrisomeParkinson’s diseasePicrosirius red stainingProteoglycansProteomicsType I collagen

Identifiers

PMID35112150
PMCPMC8944212
OpenAlexW4210301208

What OpenQuestion holds

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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.