Integrated global proteomic and phosphoproteomic analysis of cisplatin-induced apoptosis in A549 cells.
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Biochemical and biophysical research communications
2024
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| author | Qi, Luyu Zhu, Jun Cheng, Zhongyi Yuan, Zhiyi Qi, Wulin Wu, JiaHuan Qin, Yifeng Yang, Jingbo Luo, Tao Wang, Minkun Weng, Yejing Shao, Jianzhong |
| author_facet | Qi, Luyu Zhu, Jun Cheng, Zhongyi Yuan, Zhiyi Qi, Wulin Wu, JiaHuan Qin, Yifeng Yang, Jingbo Luo, Tao Wang, Minkun Weng, Yejing Shao, Jianzhong Qi, Luyu Zhu, Jun Cheng, Zhongyi Yuan, Zhiyi Qi, Wulin Wu, JiaHuan Qin, Yifeng Yang, Jingbo Luo, Tao Wang, Minkun Weng, Yejing Shao, Jianzhong |
| collection | PubMed - marine biology |
| contents | Integrated global proteomic and phosphoproteomic analysis of cisplatin-induced apoptosis in A549 cells. Qi, Luyu Zhu, Jun Cheng, Zhongyi Yuan, Zhiyi Qi, Wulin Wu, JiaHuan Qin, Yifeng Yang, Jingbo Luo, Tao Wang, Minkun Weng, Yejing Shao, Jianzhong Cisplatin Humans A549 Cells Proteomics Apoptosis Phosphoproteins Antineoplastic Agents Proteome Phosphorylation Protein phosphorylation, a widely occurring and significant post-translational modification, is integral to various biological processes. We previously utilized a protein affinity probe to identify genes damaged by cisplatin, revealing that it inflicts substantial damage on protein kinase and protein phosphatase genes. In this study, we investigated cisplatin-induced alterations in the global proteome and phosphoproteome of A549 cells. Employing Fe-IMAC beads and tyrosine phosphorylation enrichment antibodies, we identified 6944 protein groups and 18,274 phosphorylation sites on 4915 proteins across three biological replicates of both cisplatin-treated A549 cells and control cells. Among these, 730 tyrosine phosphorylation sites were identified-marking the most substantial discovery of such sites in A549 cells following cisplatin treatment. Bioinformatics analysis indicated that the proteins exhibiting significant phosphorylation level changes predominantly involved in RNA processing, modification, transcription, translation, and the spliceosome. This suggests that cisplatin-induced damage to protein kinases and phosphatases may disrupt the normal function of these proteins, consequently impairing DNA replication, RNA translation, and shearing, ultimately culminating in tumor cell death. Moreover, we cross-referenced our proteomic data with our previously obtained cisplatin-damaged genes, observing that the majority of down-regulated proteins derived from cisplatin-induced gene damage. The data are available on ProteomeXchange under the identifier PXD053902. |
| format | Artículo científico |
| id | pubmed_39432924 |
| institution | PubMed |
| language | en |
| publishDate | 2024 |
| publisher | Biochemical and biophysical research communications |
| record_format | pubmed |
| spellingShingle | Integrated global proteomic and phosphoproteomic analysis of cisplatin-induced apoptosis in A549 cells. Qi, Luyu Zhu, Jun Cheng, Zhongyi Yuan, Zhiyi Qi, Wulin Wu, JiaHuan Qin, Yifeng Yang, Jingbo Luo, Tao Wang, Minkun Weng, Yejing Shao, Jianzhong Cisplatin Humans A549 Cells Proteomics Apoptosis Phosphoproteins Antineoplastic Agents Proteome Phosphorylation Integrated global proteomic and phosphoproteomic analysis of cisplatin-induced apoptosis in A549 cells. Qi, Luyu Zhu, Jun Cheng, Zhongyi Yuan, Zhiyi Qi, Wulin Wu, JiaHuan Qin, Yifeng Yang, Jingbo Luo, Tao Wang, Minkun Weng, Yejing Shao, Jianzhong Cisplatin Humans A549 Cells Proteomics Apoptosis Phosphoproteins Antineoplastic Agents Proteome Phosphorylation Protein phosphorylation, a widely occurring and significant post-translational modification, is integral to various biological processes. We previously utilized a protein affinity probe to identify genes damaged by cisplatin, revealing that it inflicts substantial damage on protein kinase and protein phosphatase genes. In this study, we investigated cisplatin-induced alterations in the global proteome and phosphoproteome of A549 cells. Employing Fe-IMAC beads and tyrosine phosphorylation enrichment antibodies, we identified 6944 protein groups and 18,274 phosphorylation sites on 4915 proteins across three biological replicates of both cisplatin-treated A549 cells and control cells. Among these, 730 tyrosine phosphorylation sites were identified-marking the most substantial discovery of such sites in A549 cells following cisplatin treatment. Bioinformatics analysis indicated that the proteins exhibiting significant phosphorylation level changes predominantly involved in RNA processing, modification, transcription, translation, and the spliceosome. This suggests that cisplatin-induced damage to protein kinases and phosphatases may disrupt the normal function of these proteins, consequently impairing DNA replication, RNA translation, and shearing, ultimately culminating in tumor cell death. Moreover, we cross-referenced our proteomic data with our previously obtained cisplatin-damaged genes, observing that the majority of down-regulated proteins derived from cisplatin-induced gene damage. The data are available on ProteomeXchange under the identifier PXD053902. |
| title | Integrated global proteomic and phosphoproteomic analysis of cisplatin-induced apoptosis in A549 cells. |
| topic | Cisplatin Humans A549 Cells Proteomics Apoptosis Phosphoproteins Antineoplastic Agents Proteome Phosphorylation |
| url | https://pubmed.ncbi.nlm.nih.gov/39432924/ |