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Nicotine‐induced protein expression profiling reveals mutually altered proteins across four human cell lines
Author(s) -
Paulo Joao A.,
Gygi Steven P.
Publication year - 2017
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201600319
Subject(s) - proteome , chinese hamster ovary cell , hek 293 cells , cell culture , proteomics , microbiology and biotechnology , tandem mass tag , biology , nicotine , signal transduction , stable isotope labeling by amino acids in cell culture , transmembrane protein , cell , cell signaling , membrane protein , chemistry , quantitative proteomics , receptor , biochemistry , gene , genetics , neuroscience , membrane
Mass spectrometry‐based proteomic strategies can profile the expression level of proteins in response to external stimuli. Nicotine affects diverse cellular pathways, however, the nicotine‐induced alterations on the global proteome across human cell lines have not been fully elucidated. We measured perturbations in protein levels resulting from nicotine treatment in four cell lines—HEK, HeLa, PaSC, and SH‐SY5Y—in a single experiment using tandem mass tags (TMT10‐plex) and high‐resolution mass spectrometry. We quantified 8590 proteins across all cell lines. Of these, nicotine increased the abundance of 31 proteins 1.5‐fold or greater in all cell lines. Likewise, considering proteins with altered levels in at least three of the four cell lines, 64 were up‐regulated, while one was down‐regulated. Gene ontology analysis revealed that ∼40% of these proteins were membrane bound, and functioned in transmembrane signaling and receptor activity. We highlighted proteins, including APP, APLP2, LAPTM4B, and NCOA4, which were dysregulated by nicotine in all cell lines investigated and may have implications in downstream signaling pathways, particularly autophagy. Using the outlined methodology, studies in additional (including primary) cell lines will provide further evidence that alterations in the levels of these proteins are indeed a general response to nicotine and thereby merit further investigation.