University of Pennsylvania ScholarlyCommons Publicly Accessible Penn Dissertations Summer 2009 Mass Spectrometry-Based Proteomics Reveals Distinct Mechanisms of Astrocyte Protein Secretion Todd M. Greco University of Pennsylvania,
[email protected] Follow this and additional works at: https://repository.upenn.edu/edissertations Part of the Cell Biology Commons, and the Molecular and Cellular Neuroscience Commons Recommended Citation Greco, Todd M., "Mass Spectrometry-Based Proteomics Reveals Distinct Mechanisms of Astrocyte Protein Secretion" (2009). Publicly Accessible Penn Dissertations. 22. https://repository.upenn.edu/edissertations/22 This paper is posted at ScholarlyCommons. https://repository.upenn.edu/edissertations/22 For more information, please contact
[email protected]. Mass Spectrometry-Based Proteomics Reveals Distinct Mechanisms of Astrocyte Protein Secretion Abstract The ability of astrocytes to secrete proteins subserves many of its known function, such as synapse formation during development and extracellular matrix remodeling after cellular injury. Protein secretion may also play an important, but less clear, role in the propagation of inflammatory responses and neurodegenerative disease pathogenesis. While potential astrocyte-secreted proteins may number in the thousands, known astrocyte-secreted proteins are less than 100. To address this fundamental deficiency, mass spectrometry-based proteomics and bioinformatic tools were utilized for global discovery, comparison, and quantification of astrocyte-secreted proteins. A primary mouse astrocyte cell culture model was used to generate a collection of astrocyte-secreted proteins termed the astrocyte secretome. A multidimensional protein and peptide separation approach paired with mass spectrometric analysis interrogated the astrocyte secretome under control and cytokine-exposed conditions, identifying cytokine- induced secreted proteins, while extending the depth of known astrocyte-secreted proteins to 169.