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Cell type-selective secretome profiling in vivo

By Wei Wei, Nicholas McIlvain Riley, Andrew C Yang, Joon T. Kim, Stephanie M Terrell, Veronica L. Li, Marta Garcia-Contreras, Carolyn R Bertozzi, Jonathan Z Long

Posted 20 Sep 2020
bioRxiv DOI: 10.1101/2020.09.18.303909

Secreted polypeptides are a fundamental biochemical axis of intercellular and endocrine communication. However, a global understanding of composition and dynamics of cellular secretomes in intact mammalian organisms has been lacking. Here, we introduce a proximity biotinylation strategy that enables labeling, detection, and enrichment of secreted polypeptides in a cell type-selective manner in mice. We generate a proteomic atlas of hepatocyte, myocyte, pericyte, and myeloid cell secretomes by direct purification of biotinylated secreted polypeptides from blood. Our secretome atlas validates known cell type-protein pairs, reveals secreted polypeptides that distinguish between cell types, and identifies new cellular sources for classical plasma proteins. Lastly, we uncover a dynamic and previously undescribed nutrient-dependent reprogramming of the hepatocyte secretome characterized by increased unconventional secretion of the cytosolic enzyme BHMT. This secretome profiling strategy enables dynamic and cell-type dissection of the plasma proteome and the secreted polypeptides that mediate intercellular signaling. ### Competing Interest Statement The authors have declared no competing interest.

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