Temporal proteomic changes induced by nicotine in human cells: A quantitative proteomics approach.

Area of Science:

• Proteomics and phosphoproteomics
• Cellular biology
• Molecular mechanisms of nicotine action

Background:

• Nicotine is the primary addictive compound in tobacco smoke.
• While nicotine's effects are known, temporal proteomic and phosphoproteomic changes are poorly understood.
• Smoking is linked to numerous chronic diseases and infections.

Purpose of the Study:

• To investigate time-dependent proteomic and phosphoproteomic changes induced by nicotine exposure.
• To profile protein and phosphorylation events in human cell lines (SH-SY5Y and A549) under acute and chronic nicotine treatment.
• To explore potential links between nicotine, host proteins, and SARS-CoV-2.

Main Methods:

• Quantitative proteomic and phosphoproteomic profiling using TMTpro16 labeling.
• Exposure of SH-SY5Y and A549 cell lines to nicotine for various durations (15 min to 48 h).
• Analysis of over 9000 proteins and 7000 phosphorylation sites per cell line.

Main Results:

• Nicotine exposure led to decreased mitochondrial protein abundance in SH-SY5Y cells.
• Alterations in immune pathways, including the complement system, were observed in A549 cells.
• Nicotine affected host proteins interacting with viral proteins in a time-dependent manner.

Conclusions:

• Nicotine induces significant temporal changes in cellular proteomes and phosphoproteomes.
• Findings suggest nicotine's role in mitochondrial function, immune responses, and potential interactions with viral pathogens like SARS-CoV-2.
• The generated dataset offers a valuable resource for further research into nicotine's biological roles.