Optimized proteomic analysis of a mouse model of cerebellar dysfunction using amine-specific isobaric tags.

ABSTRACT: Recent proteomic applications have demonstrated their potential for revealing the molecular mechanisms underlying neurodegeneration. The present study quantifies cerebellar protein changes in mice that are deficient in plasma membrane calcium ATPase 2 (PMCA2), an essential neuronal pump that extrudes calcium from cells and is abundantly expressed in Purkinje neurons. PMCA2-null mice display motor dyscoordination and unsteady gait deficits observed in neurological diseases such as multiple sclerosis and ataxia. We optimized an amine-specific isobaric tags (iTRAQ)-based shotgun proteomics workflow for this study. This workflow took consideration of analytical variance as a function of ion signal intensity and employed biological repeats to aid noise reduction. Even with stringent protein ide

SUBMITTER: Hu J 

PROVIDER: S-EPMC2553677 | biostudies-literature | 2006 Aug

REPOSITORIES: biostudies-literature