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dc.contributor.authorChauhan, Sitara
dc.contributor.authorDanielson, Steven
dc.contributor.authorClements, Virginia
dc.contributor.authorEdwards, Nathan
dc.contributor.authorOstrand-Rosenberg, Suzanne
dc.contributor.authorFenselau, Catherine
dc.date.accessioned2019-03-04T14:49:27Z
dc.date.available2019-03-04T14:49:27Z
dc.date.issued2016-10-20
dc.description.abstractIn 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.en_US
dc.description.sponsorshipWe thank Dr.Yan Wang, Director of Proteomic Core Facility, Maryland Pathogen Research Institute, University of Maryland, College Park, for advice with the LC–MS/MS analysis. This work was supported by the National Institutes of Health, Grants GM021248 and RO1CA115880.en_US
dc.description.urihttps://pubs.acs.org/doi/10.1021/acs.jproteome.6b00811en_US
dc.format.extent22 pagesen_US
dc.genrejournal article postprintsen_US
dc.identifierdoi:10.13016/m2vd1o-qnhu
dc.identifier.citationSitara Chauhan, Steven Danielson, Virginia Clements, Nathan Edwards, Suzanne Ostrand-Rosenberg, and Catherine Fenselau, Surface Glycoproteins of Exosomes Shed by Myeloid-Derived Suppressor Cells Contribute to Function, J. Proteome Res., 2017, 16 (1), pp 238–246 DOI: 10.1021/acs.jproteome.6b00811en_US
dc.identifier.urihttps://dx.doi.org/10.1021%2Facs.jproteome.6b00811
dc.identifier.urihttp://hdl.handle.net/11603/12902
dc.language.isoen_USen_US
dc.publisherAmerican Chemical Societyen_US
dc.relation.isAvailableAtThe University of Maryland, Baltimore County (UMBC)
dc.relation.ispartofUMBC Biological Sciences Department Collection
dc.relation.ispartofUMBC Faculty Collection
dc.rightsThis item is likely protected under Title 17 of the U.S. Copyright Law. Unless on a Creative Commons license, for uses protected by Copyright Law, contact the copyright holder or the author.
dc.rightsThis document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of Proteome Research, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://pubs.acs.org/doi/10.1021/acs.jproteome.6b00811
dc.subjectexosomesen_US
dc.subjectmyeloid derived suppressor cellsen_US
dc.subjectN-glycoproteomeen_US
dc.subjectcell surface captureen_US
dc.titleSurface Glycoproteins of Exosomes Shed by Myeloid-Derived Suppressor Cells Contribute to Functionen_US
dc.typeTexten_US


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