Cell type-selective secretome profiling in vivo.

Nature chemical biology (2020-11-18)
Wei Wei, Nicholas M Riley, Andrew C Yang, Joon T Kim, Stephanie M Terrell, Veronica L Li, Marta Garcia-Contreras, Carolyn R Bertozzi, Jonathan Z Long

Secreted polypeptides are a fundamental axis of intercellular and endocrine communication. However, a global understanding of the 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 proteins from blood plasma. Our secretome dataset 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 the increased unconventional secretion of the cytosolic enzyme betaine-homocysteine S-methyltransferase (BHMT). This secretome profiling strategy enables dynamic and cell type-specific dissection of the plasma proteome and the secreted polypeptides that mediate intercellular signaling.

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Insulin from bovine pancreas, ≥25 USP units/mg (HPLC), powder
Monoclonal ANTI-FLAG® M2 antibody produced in mouse, 1 mg/mL, clone M2, affinity isolated antibody, buffered aqueous solution (50% glycerol, 10 mM sodium phosphate, and 150 mM NaCl, pH 7.4)
Oil Red O solution, 0.5% in isopropanol
Iodoacetamide, Single use vial of 56 mg
Oleic acid, Selectophore, ≥99.0%