Evidence map›Paper›PMID 27728760›Full record

ArticleJournal of proteome research2017

Surface Glycoproteins of Exosomes Shed by Myeloid-Derived Suppressor Cells Contribute to Function.

Sitara Chauhan, Steven Danielson, Virginia Clements, Nathan Edwards, Suzanne Ostrand-Rosenberg, Catherine Fenselau

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

48 citing papers in PubMed, 73 citations in OpenAlex.

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  8. Tolerating CD47.Clinical and translational medicine · 2024
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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

6 authors at 4 institutions in 1 country.

Sitara ChauhanDepartment of Chemistry and Biochemistry, University of Maryland , College Park, Maryland 20742, United States.
Steven DanielsonThermo Fisher Scientific , 355 River Oaks Parkway, San Jose, California 95134, United States.
Virginia ClementsDepartment of Biological Sciences, University of Maryland Baltimore County , Baltimore, Maryland 21250, United States.
Nathan EdwardsDepartment of Biochemistry and Molecular & Cellular Biology, Georgetown University Medical Center , Washington, D.C. 20057, United States.
Suzanne Ostrand-RosenbergDepartment of Biological Sciences, University of Maryland Baltimore County , Baltimore, Maryland 21250, United States.
Catherine FenselauDepartment of Chemistry and Biochemistry, University of Maryland , College Park, Maryland 20742, United States.
University of Maryland, Baltimore County · USUniversity of Maryland, College Park · USGeorgetown University Medical Center · USThermo Fisher Scientific (United States) · US

Funding

Ubiquitinated Proteins in Exosomes of Immune Suppressive Myeloid CellsR01GM021248 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI FENSELAU, CATHERINE C, FUSHMAN, DAVID · 1985 to 2017
$4.6M
Tumor-Induced immune suppressionR01CA115880 · NCI · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI OSTRAND-ROSENBERG, SUZANNE · 2006 to 2010
$1.3M
Orbitrap Fusion Tribrid Mass SpectrometerS10OD019938 · OD · UNIV OF MARYLAND, COLLEGE PARK · PI FENSELAU, CATHERINE C · 2015 to 2015
$600k
APPLICATIONS OF MASS SPECTROMETRY IN PHARMACOLOGYR37GM021248 · NIGMS · UNIVERSITY OF MARYLAND COLLEGE PK CAMPUS · PI FENSELAU, CATHERINE C. · 1992 to 2001
$438k
NCI NIH HHS R01 CA115880NIGMS NIH HHS R01 GM021248NIGMS NIH HHS R37 GM021248NIH HHS S10 OD019938
6 · The paper itself

Abstract

In this report, we use a proteomic strategy to identify glycoproteins on the surface of exosomes derived from myeloid-derived suppressor cells (MDSCs), and then test if selected glycoproteins contribute to exosome-mediated chemotaxis and migration of MDSCs. We report successful modification of a surface chemistry method for use with exosomes and identify 21 surface N-glycoproteins on exosomes released by mouse mammary carcinoma-induced MDSCs. These glycoprotein identities and functionalities are compared with 93 N-linked glycoproteins identified on the surface of the parental cells. As with the lysate proteomes examined previously, the exosome surface N-glycoproteins are primarily a subset of the glycoproteins on the surface of the suppressor cells that released them, with related functions and related potential as therapeutic targets. The "don't eat me" molecule CD47 and its binding partners thrombospondin-1 (TSP1) and signal regulatory protein α (SIRPα) were among the surface N-glycoproteins detected. Functional bioassays using antibodies to these three molecules demonstrated that CD47, TSP1, and to a lesser extent SIRPα facilitate exosome-mediated MDSC chemotaxis and migration.

Indexed as

Gene Expression Regulation, NeoplasticAmino Acid SequenceAnimalsCD47 AntigenChemotaxisExosomesFemaleGlycosylationMammary Glands, AnimalMammary Neoplasms, ExperimentalMiceMice, Inbred BALB CMyeloid-Derived Suppressor CellsProteomeReceptors, ImmunologicThrombospondin 1CD47 AntigenCd47 protein, mouseProteomeReceptors, ImmunologicSirpa protein, mouseThbs1 protein, mouseThrombospondin 1cell surface captureexosomesmyeloid derived suppressor cellsN-glycoproteome

Identifiers

PMID27728760
PMCPMC6127855
OpenAlexW2531693716

What OpenQuestion holds

Textmetadata
LicenceTDM
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.