Proteomic analysis of mouse choroid plexus cell line ECPC-4 treated with lipid A
| Autor: | Michiko Hamada-Kanazawa, Mieko Otani, Masaoki Takano, Keiji Sano, Shogo Matsuyama, Takahiro Kaji |
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| Rok vydání: | 2015 |
| Předmět: |
0301 basic medicine
Gene isoform Proteomics Pathology medicine.medical_specialty Vacuolar Proton-Translocating ATPases Protein subunit Immunology Vimentin Coatomer Protein Cell Line Lipid A 03 medical and health sciences Mice 0302 clinical medicine Tandem Mass Spectrometry Medicine Animals Intermediate filament Cytoskeleton Pharmacology biology business.industry Epithelial Cells Phosphoproteins Cell biology 030104 developmental biology Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Proteome Choroid Plexus biology.protein Choroid plexus business 030217 neurology & neurosurgery |
| Zdroj: | Inflammation research : official journal of the European Histamine Research Society ... [et al.]. 65(4) |
| ISSN: | 1420-908X |
| Popis: | Choroid plexus (CP) epithelial cells have multiple functions in the cerebral ventricles, including cerebrospinal fluid (CSF) production and forming part of the blood–CSF barrier. They are also responsible for producing inflammatory mediators involved in meningitis. The present study aimed to elucidate the functions of the CP epithelial cells during CNS inflammation. We analyzed the proteome and phosphoproteome in lipid A-treated ECPC-4 mouse CP cells by gel electrophoresis and mass spectrometry. Levels of 10 proteins and seven phosphoproteins were significantly altered by lipid A in time-dependent manners, including V-type proton ATPase subunit B (ATP6V), protein 40 kD, elongation factor-1δ, coatomer subunit e (COPE), vimentin (isoform CRA a), purine nucleoside phosphorylase, eukaryotic initiation factor-4F splicing variant, put. β-actin, peroxiredoxin-6 isoform 1, and immunoglobulin heavy chain variable region. These proteins could be classified as having cytoskeleton/intermediate filament, protein-folding, signal-transduction, cell-growth, metabolism, and redox-regulation functions. The identified phosphoproteins were HSP 84, γ-actin, HSP 70 cognate, vimentin, tubulin β-4B chain, protein disulfide-isomerase A6 precursor, and heterogenous nuclear ribonucleoprotein, which could be classified as having cytoskeleton/intermediate filament, protein-folding, and metabolism functions. These results indicate that lipid A can change the levels of proteins and phosphoproteins in ECPC-4 cells, suggesting that the identified proteins and phosphoproteins may play important roles in inflammation of the CP. |
| Databáze: | OpenAIRE |
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