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Dougan, Stephanie

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Dougan

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Stephanie

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Dougan, Stephanie
Author's Publications: search.filters.isAuthorOfPublication.6dd79558-8bde-4335-9e63-34ed4c5cef87

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    PD-L1 is an activation-independent marker of brown adipocytes
    (Nature Publishing Group UK, 2017) Ingram, Jessica R.; Dougan, Michael; Rashidian, Mohammad; Knoll, Marko; Keliher, Edmund J.; Garrett, Sarah; Garforth, Scott; Blomberg, Olga S.; Espinosa, Camilo; Bhan, Atul; Almo, Steven C.; Weissleder, Ralph; Lodish, Harvey; Dougan, Stephanie; Ploegh, Hidde L.
    Programmed death ligand 1 (PD-L1) is expressed on a number of immune and cancer cells, where it can downregulate antitumor immune responses. Its expression has been linked to metabolic changes in these cells. Here we develop a radiolabeled camelid single-domain antibody (anti-PD-L1 VHH) to track PD-L1 expression by immuno-positron emission tomography (PET). PET-CT imaging shows a robust and specific PD-L1 signal in brown adipose tissue (BAT). We confirm expression of PD-L1 on brown adipocytes and demonstrate that signal intensity does not change in response to cold exposure or β-adrenergic activation. This is the first robust method of visualizing murine brown fat independent of its activation state.
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    Generation of Ca2+-independent sortase A mutants with enhanced activity for protein and cell surface labeling
    (Public Library of Science, 2017) Jeong, Hee-Jin; Abhiraman, Gita C.; Story, Craig M.; Ingram, Jessica; Dougan, Stephanie
    Sortase A, a calcium-dependent transpeptidase derived from Staphylococcus aureus, is used in a broad range of applications, such as the conjugation of fluorescent dyes and other moieties to proteins or to the surface of eukaryotic cells. In vivo and cell-based applications of sortase have been somewhat limited by the large range of calcium concentrations, as well as by the often transient nature of protein-protein interactions in living systems. In order to use sortase A for cell labeling applications, we generated a new sortase A variant by combining multiple mutations to yield an enzyme that was both calcium-independent and highly active. This variant has enhanced activity for both N- and C-terminal labeling, as well as for cell surface modification under physiological conditions.