Ubiquitin Conjugation Probed by Inflammation in Myeloid-Derived Suppressor Cell Extracellular Vesicles

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dc.contributor.authorAdams, Katherine R.
dc.contributor.authorChauhan, Sitara
dc.contributor.authorPatel, Divya B.
dc.contributor.authorClements, Virginia K.
dc.contributor.authorWang, Yan
dc.contributor.authorJay, Steven M.
dc.contributor.authorEdwards, Nathan J.
dc.contributor.authorOstrand-Rosenberg, Suzanne
dc.contributor.authorFenselau, Catherine
dc.date.accessioned2019-03-05T19:24:57Z
dc.date.available2019-03-05T19:24:57Z
dc.date.issued2017-10-23
dc.description.abstractUbiquitinated proteins carried by the extracellular vesicles (EV) released by myeloid-derived suppressor cells (MDSC) have been investigated using proteomic strategies to examine the effect of tumor-associated inflammation. EV were collected from MDSC directly following isolation from tumor-bearing mice with low and high inflammation. Among the 1092 proteins (high inflammation) and 925 proteins (low inflammation) identified, more than 50% were observed as ubiquitinated proteoforms. More than three ubiquitin-attachment sites were characterized per ubiquitinated protein, on average. Multiple ubiquitination sites were identified in the pro-inflammatory proteins S100 A8 and S100 A9, characteristic of MDSC and in histones and transcription regulators among other proteins. Spectral counting and pathway analysis suggest that ubiquitination occurs independently of inflammation. Some ubiquitinated proteins were shown to cause the migration of MDSC, which has been previously connected with immune suppression and tumor progression. Finally, MDSC EV are found collectively to carry all the enzymes required to catalyze ubiquitination, and the hypothesis is presented that a portion of the ubiquitinated proteins are produced in situ.en_US
dc.description.sponsorshipThe research was supported by grants from the National Institutes of Health (grant nos. GM021248, HL112905, and OD019938) and a fellowship from the American Heart Association 16PRE30770016. We thank Mr. Arsh Chauhan for assistance with some of the figures and Dr. Meghan Burke for helpful discussionsen_US
dc.description.urihttps://pubs.acs.org/doi/10.1021/acs.jproteome.7b00585en_US
dc.format.extent25 pagesen_US
dc.genrejournal articles preprintsen_US
dc.identifierdoi:10.13016/m2ifoc-94iu
dc.identifier.citationKatherine R. Adams, Sitara Chauhan, Divya B. Patel, Virginia K. Clements, Yan Wang, Steven M. Jay , Nathan J. Edwards, Suzanne Ostrand-Rosenberg, and Catherine Fenselau, Ubiquitin Conjugation Probed by Inflammation in Myeloid-Derived Suppressor Cell Extracellular Vesicles, J. Proteome Res., 2018, 17 (1), pp 315–324 DOI: 10.1021/acs.jproteome.7b00585en_US
dc.identifier.urihttps://dx.doi.org/10.1021%2Facs.jproteome.7b00585
dc.identifier.urihttp://hdl.handle.net/11603/12935
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 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.7b00585
dc.subjectextracellular vesiclesen_US
dc.subjectubiquitome; inflammationen_US
dc.subjectMDSCen_US
dc.subjectLC−MS/MSen_US
dc.subjecttumor-induced immune suppressionen_US
dc.subjecttop-down proteomicsen_US
dc.subjectspectral countingen_US
dc.titleUbiquitin Conjugation Probed by Inflammation in Myeloid-Derived Suppressor Cell Extracellular Vesiclesen_US
dc.typeTexten_US

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