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Published on: February 20, 2018
Networks development between nicotinic chemical probes and Ca9-22 oral cancer cells by general proteomics analyses
Ruei-Nian Li1, Chin-Jen Wu, Zong-Jing Yu
1Department of Biomedical Science and Environmental Biology, Kaohsiung Medical University, Kaohsiung, Taiwan; Cancer Center, Kaohsiung Medical University Hospital, Kaohsiung Medical University, Kaohsiung, Taiwan.
Abstract:
Tobacco includes thousands of chemicals such as nicotine, which causes numerous diseases including oral cancer. We synthesized nicotinic acid based probes by chemical modification to identify the proteins expressed by the oral cancer cell line Ca9-22 that interact with the nicotinic functional group. Proteins belonging to human oral squamous cell carcinoma were pulled down by a probe carrier based on nicotinic acid, which was reacted with 3-aminopropyltriethoxysilane to compose nicotinic acid linked 3-aminopropyltriethoxysilane exposed on the SiO2 surface. Oral cancer cell lysates were incubated with the nicotinic acid chemical probes to identify the interactions between the nicotinic group and oral cancer cell line extracted proteins. The interactions between the chemical probes and proteins identified as their targets were confirmed by consulting chemicals databases. Interestingly, chaperone proteins (e.g., heat-shock proteins and endoplasmin) that were found to interact with nicotinic acid were identified as binding partners in ribosomal and nucleosome assembly complexes.
Insights
Researchers developed nicotinic acid probes to identify oral cancer proteins interacting with nicotine. These probes revealed chaperone proteins, like heat-shock proteins, binding to nicotine-related molecules in oral cancer cells.
Area of Science:
- Biochemistry
- Oncology
- Chemical Biology
Background:
- Tobacco use is a major cause of oral cancer, linked to thousands of chemicals including nicotine.
- Nicotine and its derivatives are implicated in various diseases, necessitating a deeper understanding of their molecular interactions in cancer.
Purpose of the Study:
- To synthesize and utilize nicotinic acid-based chemical probes to identify proteins interacting with the nicotinic functional group in oral cancer cells.
- To elucidate the specific protein targets within the Ca9-22 oral cancer cell line that bind to nicotinic acid derivatives.
Main Methods:
- Chemical synthesis of nicotinic acid-based probes functionalized with 3-aminopropyltriethoxysilane on a SiO2 surface.
- Incubation of oral cancer cell lysates (Ca9-22) with the synthesized chemical probes to capture interacting proteins.
- Confirmation of protein-probe interactions using chemical databases.
Main Results:
- Successful pull-down of proteins from human oral squamous cell carcinoma cell line Ca9-22 using the nicotinic acid probes.
- Identification of chaperone proteins, including heat-shock proteins and endoplasmin, as binding partners.
- These chaperone proteins were found to be involved in ribosomal and nucleosome assembly complexes.
Conclusions:
- Nicotinic acid-based probes are effective tools for identifying protein interactions with nicotinic moieties in oral cancer.
- Chaperone proteins, crucial for cellular processes, interact with nicotinic acid derivatives, suggesting a potential role in oral cancer pathogenesis.
- Further investigation into these interactions could reveal novel therapeutic targets for oral cancer treatment.
