Quantitative mass spectrometry-based proteomics reveals the dynamic range of primary mouse astrocyte protein secretion.

ABSTRACT: Growing appreciation for astrocytes as active participants in nervous system development, neurovascular metabolic coupling, and neurological disease progression has stimulated recent investigation into specific astrocyte-secreted proteins that may mediate these functions. The current work utilized SILAC-generated isotope reference proteomes to quantify relative protein abundances between the astrocyte proteome and secretome. Multidimensional GeLC-MS/MS analysis of astrocyte conditioned media and cell lysates resulted in the relative quantification of 516 proteins, 92 of which were greater than 1.5-fold enriched in astrocyte-conditioned media (ACM). Eighty of the ACM-enriched proteins had N-terminal signal peptides, comprising well-known classically secreted proteins, such as apolipoprotein

SUBMITTER: Greco TM 

PROVIDER: S-EPMC2866110 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature