Networks development between nicotinic chemical probes and Ca9-22 oral cancer cells by general proteomics analyses

• Published in: Electrophoresis Vol. 35; no. 15; pp. 2213 - 2221
• Main Authors: Li, Ruei-Nian, Wu, Chin-Jen, Yu, Zong-Jing, Chang, Hsueh-Wei, Liang, Shih-Shin
• Format: Journal Article
• Language: English
• Published: Germany Blackwell Publishing Ltd 01.08.2014
• Subjects: Biomarkers, Tumor - analysis; Biomarkers, Tumor - chemistry; Biomarkers, Tumor - metabolism; Biotechnology; Ca9-22; Cancer; Carcinoma, Squamous Cell - chemistry; Carcinoma, Squamous Cell - metabolism; Cell Line, Tumor; Chemical probes; Chemical-protein interaction; Diseases; Electrophoresis; Human oral squamous cell carcinoma; Humans; Molecular Probe Techniques; Mouth Neoplasms - chemistry; Mouth Neoplasms - metabolism; Networks; Niacin - analysis; Niacin - chemistry; Niacin - metabolism; Nicotinic acid; Nicotinic acid probes; Protein Interaction Maps - physiology; Proteins; Proteome - analysis; Proteome - chemistry; Proteome - metabolism; Proteomics; Target recognition; Nicotinic acid probes; Chemical-protein interaction; Ca9-22; Chemical probes; Human oral squamous cell carcinoma; Proteomics
• ISSN: 0173-0835; 1522-2683
• DOI: 10.1002/elps.201400150

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.