title: An Overview of Advanced SILAC-Labeling Strategies for Quantitative Proteomics.
abstract: Comparative, quantitative mass spectrometry of proteins provides great insight to protein abundance and function, but some molecular characteristics related to protein dynamics are not so easily obtained. Because the metabolic incorporation of stable amino acid isotopes allows the extraction of distinct temporal and spatial aspects of protein dynamics, the SILAC methodology is uniquely suited to be adapted for advanced labeling strategies. New SILAC strategies have emerged that allow deeper foraging into the complexity of cellular proteomes. Here, we review a few advanced SILAC-labeling strategies that have been published during last the years. Among them, different subsaturating-labeling as well as dual-labeling schemes are most prominent for a range of analyses including those of neuronal proteomes, secretion, or cell-cell-induced stimulations. These recent developments suggest that much more information can be gained from proteomic analyses if the labeling strategies are specifically tailored toward the experimental design.
authors.affiliation: Institute of Cell Biology and Anatomy, University of Heidelberg, Heidelberg, Germany.
authors.forename: F
authors.initials: F
authors.lastname: Terzi
authors.affiliation: Institute of Cell Biology and Anatomy, University of Heidelberg, Heidelberg, Germany. Electronic address: cambridge@ana.uni-heidelberg.de.
authors.forename: S
authors.initials: S
authors.lastname: Cambridge
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D013058:Mass Spectrometry; D040901:Proteomics / Q000379:methods*
chemical_list: D000596:Amino Acids
keywords: Cell culture; Labeling strategies; Mass spectrometry; Quantitative proteomics; SILAC