Measuring Proteome Dynamics in Vivo

• DOI: 10.1074/mcp.m900026-mcp200
• Publication Date: 2009-09-02T03:13:39Z
• Authors: Nadia Rachdaoui; Leanne Austin; Eric Kramer; Michael J. Previs; Vernon E. Anderson; Takhar Kasumov; Stephen F. Previs
• Keywords: Proteome

Proteomics investigations typically yield information regarding static gene expression profiles. The central issues that limit the study of proteome dynamics include how to (i) administer a labeled amino acid in vivo, (ii) measure isotopic labeling protein(s) (which may be low), and (iii) reliably interpret precursor/product relationships. In this study, we demonstrate potential quantifying by coupling administration stable isotopes with mass spectrometric assays. Although direct acid(s) is used protein synthesis, explain application water, comparing (2)H(2)O versus H(2)(18)O for measuring albumin biosynthesis vivo. This emphasizes two distinct advantages using water over acid(s). First, long term studies (e.g. days or weeks), it not practical continuously acid(s); however, presence organisms will generate acids. Second, calculate rates synthesis short hours), one must utilize ratio; when possible identify easily precursor (i.e. water). We permits mice) during metabolic "steady-state" "non-steady-state" conditions, i.e. integrating transitions between fed fasted state an acute perturbation following meal), respectively. expect use applicable wide scale can therein obtain functional image