alexa Secretomic Analysis of Mouse Choroid Plexus Cell Line E
ISSN: 0974-276X

Journal of Proteomics & Bioinformatics
Open Access

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Research Article

Secretomic Analysis of Mouse Choroid Plexus Cell Line ECPC-4 Using Two-Dimensional Gel Electrophoresis Coupled to Mass Spectrometry

Masaoki Takano1*, Mari Uramoto1, Mieko Otani1, Kenji Matsuura2, Keiji Sano1 and Shogo Matsuyama2

1Laboratory of Molecular Cell Biology , School of Pharmaceutical Sciences, Kobe Gakuin University, 1-1-3 Minatojima, Chuo-ku, Kobe 650-8586, Japan

2Faculty of Pharmaceutical Sciences, Himeji Dokkyo University, 7-2-1 Kamiohno, Himeji, 670-8524 Japan

*Corresponding Author:
Masaoki Takano
Laboratory of Molecular Cell Biology
School of Pharmaceutical Sciences
Kobe Gakuin University, 1-1-3 Minatojima
Chuo-ku, Kobe 650-8586, Japan
Tel (or) Fax: +81-78-974-4716
E-mail: [email protected]

Received Date: August 15, 2014; Accepted Date: October 14, 2014; Published Date: October 20, 2014

Citation: Takano M, Uramoto M, Otani M, Matsuura K, Sano K, et al. (2014) Secretomic Analysis of Mouse Choroid Plexus Cell Line ECPC-4 Using Two- Dimensional Gel Electrophoresis Coupled to Mass Spectrometry. J Proteomics Bioinform 7: 347-352. doi: 10.4172/jpb.1000338

Copyright: © 2014 Takano M, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited



Choroid plexus (CP), the main production site of cerebrospinal fluid (CSF), is responsible for the inflammatory mediators involved in meningitis and immune systems. The mouse choroid plexus cell line ECPC-4 is known to be useful for analyses of CP functions. In this study, we performed the secretome analysis of ECPC-4 using two-dimensional gel electrophoresis (2-DE) followed by mass spectrometry. Twenty-two secreted proteins were identified in the conditioned medium of ECPC-4. They were a secreted protein acidic and rich in cysteine (SPARC), plasminogen activator inhibitor 1 (PAI-1), and others (vinculin, heat shock protein cognate 71 kDa, moesin, tubulin ß2A, fascin, calreticulin, gamma actin, alcohol dehydrogenase, malate dehydrogenase, Rho GDP dissociation inhibitor alpha, phosphoglyceratemutase 1, translationally controlled tumor protein, phosphatidylethanolamin binding protein1, peroxiredoxin1 type II, peroxiredoxin1, myosin light polypeptide 6, cofilin-1, nucleoside diphosphate kinase A, peptidyl-prolylcis-trans isomerase A[PPI-A], and galectin1). These proteins could be classified as cytoskeleton/ intermediate filament, protein folding, signal transduction, cell growth, metabolism, and redox regulation groups, suggesting that they could be related to the CP functions. Furthermore, the level of four proteins was changed in the conditioned medium of ECPC-4 treated with lipidA. Proteasome subunit alpha type-1 and nucleoside diphosphate kinase A were significantly increased and gamma-actin and galectin-1 were significantly decreased, as compared withthose in the conditioned medium of non-treated ECPC-4. Also, Western Blotting also validated the changes in proteasome subunit alpha type-1, galectin-1 and nucleoside diphosphate kinase A. Thus, it is suggested that these proteins play an important role in inflammation such as meningitis. ECPC-4, like CP epithelial cells,is useful to analyze the CP functions.


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