Evidence map›Paper›PMID 36590238›Full record

ArticleJournal of extracellular biology2022

Secretion of the disulfide bond generating catalyst QSOX1 from pancreatic tumor cells into the extracellular matrix: association with extracellular vesicles and matrix proteins.

Catherine S Millar-Haskell, John L Sperduto, John H Slater, Colin Thorpe, Jason P Gleghorn

Erratum issuedOpen access · diamondAbstract read
In one paragraph

Article in Journal of extracellular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

10 citing papers in PubMed, 17 citations in OpenAlex.

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  8. Enhanced secretion of promyogenic exosomes by quiescent muscle cells.Frontiers in cell and developmental biology · 2024
    Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Catherine S Millar-HaskellDepartments of Biomedical Engineering, University of Delaware, Newark, DE 19716.
John L SperdutoDepartments of Biomedical Engineering, University of Delaware, Newark, DE 19716.
John H SlaterDepartments of Biomedical Engineering, University of Delaware, Newark, DE 19716.
Colin ThorpeChemistry & Biochemistry, University of Delaware, Newark, DE 19716.
Jason P GleghornDepartments of Biomedical Engineering, University of Delaware, Newark, DE 19716.
University of Delaware · US

Funding

Predictive Modeling & Optimal Control Framework for Model-Based Epidemic Response in DelawareP20GM103446 · NIGMS · UNIVERSITY OF DELAWARE · PI Shawn W Polson · 2012 to 2026
$67.2M
Subproject Title: Clinical Research Education, Mentoring and Career Development CoreU54GM104941 · NIGMS · UNIVERSITY OF DELAWARE · PI Megan M Wenner · 2013 to 2026
$60.5M
Flavoproteins in Oxidative Protein FoldingR01GM026643 · NIGMS · UNIVERSITY OF DELAWARE · PI THORPE, COLIN · 1985 to 2019
$6.6M
NIGMS NIH HHS P20 GM103446NIGMS NIH HHS R01 GM026643NIGMS NIH HHS U54 GM104941
6 · The paper itself

Abstract

Quiescin sulfhydryl oxidase 1 (QSOX1) is a disulfide bond generating catalyst that is overexpressed in solid tumors. Expression of QSOX1 is linked to cancer cell invasion, tumor grade, and extracellular matrix (ECM) protein deposition. While the secreted version of QSOX1 is known to be present in various fluids and secretory tissues, its presence in the ECM of cancer is less understood. To characterize secreted QSOX1, we separated conditioned media based on size and density. We discovered that the majority of secreted QSOX1 resides in the EV-depleted fraction and in the soluble protein fraction. Very little QSOX1 could be detected in the EVP fraction. We used immunofluorescence to image subpopulations of EVs and found QSOX1 in Golgi-derived vesicles and medium/large vesicles, but in general, most extracellular QSOX1 was not attributed to these vesicles. Next, we quantified QSOX1 co-localization with the EV marker Alix. For the medium/large EVs, ~98% contained QSOX1 when fibronectin was used as a coating. However, on collagen coatings, only ~60% of these vesicles contained QSOX1, suggesting differences in EV cargo based on ECM coated surfaces. About 10% of small EVs co-localized with QSOX1 on every ECM protein surface except for collagen (0.64%). We next investigated adhesion of QSOX1 to ECM proteins

Indexed as

collagendisulfide bondsextracellular matrixextracellular vesicles and particlesfibronectinimmunofluorescencelamininQSOX1quiescin sulfhydryl oxidasesecreted proteinssoluble factorstangential flow filtrationthiolsultracentrifugation

Identifiers

PMID36590238
PMCPMC9797115
OpenAlexW4283788620

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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.