Skip to main content
Article thumbnail
Location of Repository

A large-scale electrophoresis- and chromatography-based determination of gene expression profiles in bovine brain capillary endothelial cells after the re-induction of blood-brain barrier properties

By Duban-Deweer Sophie, Deracinois Barbara, Pottiez Gwënaël, Cecchelli Roméo, Fenart Laurence, Karamanos Yannis and Flahaut Christophe

Abstract

<p>Abstract</p> <p>Background</p> <p>Brain capillary endothelial cells (BCECs) form the physiological basis of the blood-brain barrier (BBB). The barrier function is (at least in part) due to well-known proteins such as transporters, tight junctions and metabolic barrier proteins (e.g. monoamine oxidase, gamma glutamyltranspeptidase and P-glycoprotein). Our previous 2-dimensional gel proteome analysis had identified a large number of proteins and revealed the major role of dynamic cytoskeletal remodelling in the differentiation of bovine BCECs. The aim of the present study was to elaborate a reference proteome of Triton X-100-soluble species from bovine BCECs cultured in the well-established <it>in vitro </it>BBB model developed in our laboratory.</p> <p>Results</p> <p>A total of 215 protein spots (corresponding to 130 distinct proteins) were identified by 2-dimensional gel electrophoresis, whereas over 350 proteins were identified by a shotgun approach. We classified around 430 distinct proteins expressed by bovine BCECs. Our large-scale gene expression analysis enabled the correction of mistakes referenced into protein databases (e.g. bovine vinculin) and constitutes valuable evidence for predictions based on genome annotation.</p> <p>Conclusions</p> <p>Elaboration of a reference proteome constitutes the first step in creating a gene expression database dedicated to capillary endothelial cells displaying BBB characteristics. It improves of our knowledge of the BBB and the key proteins in cell structures, cytoskeleton organization, metabolism, detoxification and drug resistance. Moreover, our results emphasize the need for both appropriate experimental design and correct interpretation of proteome datasets.</p

Topics: Physiology, QP1-981, Science, Q, DOAJ:Physiology, DOAJ:Biology, DOAJ:Biology and Life Sciences, Cytology, QH573-671
Publisher: BioMed Central
Year: 2010
DOI identifier: 10.1186/1477-5956-8-57
OAI identifier: oai:doaj.org/article:3cf524f74eab4f4894e66a0e238411ad
Journal:
Download PDF:
Sorry, we are unable to provide the full text but you may find it at the following location(s):
  • https://doaj.org/toc/1477-5956 (external link)
  • http://www.proteomesci.com/con... (external link)
  • https://doaj.org/article/3cf52... (external link)
  • Suggested articles


    To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.