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dc.contributor.authorWu, Lidan
dc.contributor.authorClaas, Allison Mary
dc.contributor.authorSarkar, Aniruddh
dc.contributor.authorLauffenburger, Douglas A
dc.contributor.authorHan, Jongyoon
dc.date.accessioned2017-02-15T21:48:21Z
dc.date.available2017-02-15T21:48:21Z
dc.date.issued2015-03
dc.date.submitted2015-01
dc.identifier.issn1757-9694
dc.identifier.issn1757-9708
dc.identifier.urihttp://hdl.handle.net/1721.1/106950
dc.description.abstractAs key components of autocrine signaling, pericellular proteases, a disintegrin and metalloproteinases (ADAMs) in particular, are known to impact the microenvironment of individual cells and have significant implications in various pathological situations including cancer, inflammatory and vascular diseases. There is great incentive to develop a high-throughput platform for single-cell measurement of pericellular protease activity, as it is essential for studying the heterogeneity of protease response and the corresponding cell behavioral consequences. In this work, we developed a microfluidic platform to simultaneously monitor protease activity of many single cells in a time-dependent manner. This platform isolates individual microwells rapidly on demand and thus allows single-cell activity measurement of both cell-surface and secreted proteases by confining individual cells with diffusive FRET-based substrates. With this platform, we observed dose-dependent heterogeneous protease activation of HepG2 cells treated with phorbol 12-myristate 13-acetate (PMA). To study the temporal behavior of PMA-induced protease response, we monitored the pericellular protease activity of the same single cells during three different time periods and revealed the diversity in the dynamic patterns of single-cell protease activity profile upon PMA stimulation. The unique temporal information of single-cell protease response can help unveil the complicated functional role of pericellular proteases.en_US
dc.description.sponsorshipNational Institutes of Health (U.S.) (Grant R01-CA096504)en_US
dc.description.sponsorshipSingapore-MIT Alliance for Research and Technology (SMART)en_US
dc.language.isoen_US
dc.publisherRoyal Society of Chemistryen_US
dc.relation.isversionofhttp://dx.doi.org/10.1039/c5ib00019jen_US
dc.rightsCreative Commons Attribution-Noncommercial-Share Alikeen_US
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/en_US
dc.sourcePMCen_US
dc.titleHigh-throughput protease activity cytometry reveals dose-dependent heterogeneity in PMA-mediated ADAM17 activationen_US
dc.typeArticleen_US
dc.identifier.citationWu, Lidan et al. “High-Throughput Protease Activity Cytometry Reveals Dose-Dependent Heterogeneity in PMA-Mediated ADAM17 Activation.” Integr. Biol. 7.5 (2015): 513–524.en_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Biological Engineeringen_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Electrical Engineering and Computer Scienceen_US
dc.contributor.departmentMassachusetts Institute of Technology. Research Laboratory of Electronicsen_US
dc.contributor.departmentSingapore-MIT Alliance in Research and Technology (SMART)en_US
dc.contributor.mitauthorWu, Lidan
dc.contributor.mitauthorClaas, Allison Mary
dc.contributor.mitauthorSarkar, Aniruddh
dc.contributor.mitauthorLauffenburger, Douglas A
dc.contributor.mitauthorHan, Jongyoon
dc.relation.journalIntegrative Biologyen_US
dc.eprint.versionAuthor's final manuscripten_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dspace.orderedauthorsWu, Lidan; Claas, Allison M.; Sarkar, Aniruddh; Lauffenburger, Douglas A.; Han, Jongyoonen_US
dspace.embargo.termsNen_US
dc.identifier.orcidhttps://orcid.org/0000-0003-3150-6170
dc.identifier.orcidhttps://orcid.org/0000-0003-1224-8153
dc.identifier.orcidhttps://orcid.org/0000-0001-7215-1439
mit.licenseOPEN_ACCESS_POLICYen_US


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