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Differentially expressed proteins are caused by increased chemokine ligand 2 in mice hippocampi after alcohol treatment
Author(s) -
Cook Rachel,
Lawrence James,
Bray Jennifer
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.802.14
Subject(s) - proteome , hippocampus , transgene , biology , chemokine , ccl2 , chemistry , central nervous system , genetically modified mouse , microbiology and biotechnology , biochemistry , neuroscience , receptor , gene
When alcohol enters the central nervous system (CNS) it disrupts the physiological balance, producing several negative effects on the nervous system, specifically learning and memory. It has been shown that the neuroimmune protein Chemokine (CC motif) Ligand 2 (CCL2), perturbs the negative effects alcohol has on the hippocampus, the region of the brain associated with learning and memory. CCL2 transgenic mice that overexpress this protein have been used to study the phenotypical and behavioral effects of alcohol use. Although the signaling cascade initiated by CCL2 is currently unknown, identification of proteins responsible for these effects is possible through the combination of SDS‐PAGE and high‐resolution mass spectrometry. Using these techniques, a molecular fingerprint was produced by identification of differentially expressed proteins located in hippocampus of CCL2‐transgenic mice when compared to wild type mice. Over a time course of ten days mice of varying ages consumed 1g/kg of 20% ethanol every day. After the alcohol treatment, the left‐hemisphere hippocampus was extracted for proteomic analysis and the right‐hemisphere hippocampus was used for quantification of CCL2 concentration. This ensured identical biological samples for cross‐comparison between CCL2 expression and the effects this had on the proteome of the hippocampus. ELISA was used to quantify CCL2 concentration. Proteins from the left hemisphere were extracted and subsequently resolved using large format SDS‐PAGE analysis. Differentially expressed proteins were identified by Quadropole‐Time of Flight tandem mass spectrometry. Identification of proteins was done using a combination of MassHunter Qualitative, ProFinder, and NCBI databases. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .