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Relative quantification of membrane proteins in wild-type and prion protein (PrP)-knockout cerebellar granule neurons.

Abstract：

:Approximately 25% of eukaryotic proteins possessing homology to at least two transmembrane domains are predicted to be embedded in biological membranes. Nevertheless, this group of proteins is not usually well represented in proteome-wide experiments due to their refractory nature. Here we present a quantitative mass spectrometry-based comparison of membrane protein expression in cerebellar granule neurons grown in primary culture that were isolated from wild-type mice and mice lacking the cellular prion protein. This protein is a cell-surface glycoprotein that is mainly expressed in the central nervous system and is involved in several neurodegenerative disorders, though its physiological role is unclear. We used a low specificity enzyme α-chymotrypsin to digest membrane proteins preparations that had been separated by SDS-PAGE. The resulting peptides were labeled with tandem mass tags and analyzed by MS. The differentially expressed proteins identified using this approach were further analyzed by multiple reaction monitoring to confirm the expression level changes.

journal_name

J Proteome Res

journal_title

Journal of proteome research

authors

Stella R,Cifani P,Peggion C,Hansson K,Lazzari C,Bendz M,Levander F,Sorgato MC,Bertoli A,James P

doi

10.1021/pr200759m

subject

Has Abstract

pub_date

2012-02-03 00:00:00

pages

523-36

issue

2

eissn

1535-3893

issn

1535-3907

journal_volume

11

pub_type

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