Nicotine-induced protein expression profiling reveals mutually altered proteins across four human cell lines
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Updated: Mar 11, 2026
Spectral Confocal Imaging of Fluorescently tagged Nicotinic Receptors in Knock-in Mice with Chronic Nicotine Administration
Published on: February 10, 2012
1Department of Cell Biology, Harvard Medical School, Boston, MA, USA.
Abstract:
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.
Insights
Nicotine alters protein expression in human cells. This study identified key proteins, like APP and NCOA4, dysregulated by nicotine, potentially impacting cellular signaling and autophagy.
Area of Science:
- Proteomics
- Cellular Biology
- Biochemistry
Background:
- Nicotine impacts cellular pathways, but its global proteomic effects across human cell lines are not fully understood.
- Understanding nicotine's influence on protein expression is crucial for elucidating its cellular mechanisms.
Purpose of the Study:
- To comprehensively profile nicotine-induced proteomic alterations in multiple human cell lines.
- To identify common protein expression changes across different cell types in response to nicotine.
Main Methods:
- Utilized tandem mass tags (TMT10-plex) and high-resolution mass spectrometry for quantitative proteomic analysis.
- Investigated protein expression changes in four human cell lines (HEK, HeLa, PaSC, SH-SY5Y) after nicotine treatment.
Main Results:
- Quantified 8590 proteins across all cell lines.
- Identified 31 proteins with increased abundance (≥1.5-fold) in all cell lines upon nicotine exposure.
- Found 64 up-regulated and 1 down-regulated protein in at least three cell lines; many involved in transmembrane signaling and receptor activity.
Conclusions:
- Nicotine significantly dysregulates specific proteins, including APP, APLP2, LAPTM4B, and NCOA4, across diverse human cell lines.
- These identified proteins, particularly those involved in membrane-bound functions, may play critical roles in nicotine-mediated cellular responses, including autophagy.
- The findings suggest a conserved molecular response to nicotine, warranting further investigation in primary cells and additional cell lines.
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