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Quantitative proteomics analysis of mitochondrial proteins in lung adenocarcinomas and normal lung tissue using iTRAQ and tandem mass spectrometry.

ABSTRACT: Lung adenocarcinoma is the most common type of lung cancer. Unfortunately, lung adenocarcinoma has a poor prognosis and the pathogenesis remains unclear. Mitochondria are important mediators of tumorigenesis. However, the proteomics profile of lung adenocarcinoma mitochondrial proteins has not been elucidated. In this study, we investigated differences in the mitochondrial protein profiles between lung adenocarcinomas and normal tissue. Laser capture microdissection (LCM) was used to isolate the target cells from lung adenocarcinomas and normal tissue. The differential expression of mitochondrial proteins was determined using isobaric tags for relative and absolute quantitation (iTRAQ) combined with two-dimensional liquid chromatography-tandem mass spectrometry (2D-LC-MS/MS). Bioinformatics analysis was performed using Gene Ontology and KEGG databases. As a result, 510 differentially expressed proteins were identified, 315 of which were upregulated and 195 that were downregulated. Of these proteins, 35.5% were mitochondrial or mitochondrial-related and were involved in binding, catalysis, molecular transduction, transport, and molecular structure. Based on the differentially expressed proteins, 63 pathways were significantly enriched through KEGG. The overexpression and cellular distribution of the mitochondrial protein C1QBP in the lung cancer samples was confirmed and verified by Western blotting. The relationship between C1QBP expression and clinicopathological features in lung cancer patients was likewise evaluated using immunohistochemistry, which revealed that the upregulation of C1QBP was associated with lymph node metastasis, pathological grade and clinical stage of TNM. The results indicate that the iTRAQ 2D-LC-MS/MS technique is a potential method for comparing mitochondrial protein profiles between tumor and normal tissue and could aid in identifying novel biomarkers and the mechanisms underlying carcinogenesis.

SUBMITTER: Li W

PROVIDER: S-EPMC5622239 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature

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Quantitative proteomics analysis of mitochondrial proteins in lung adenocarcinomas and normal lung tissue using iTRAQ and tandem mass spectrometry.

Li Wei W Zhang Xuede X Wang Wei W Sun Ruiying R Liu Boxuan B Ma Yuefeng Y Zhang Wei W Ma Li L Jin Yaofeng Y Yang Shuanying S

American journal of translational research 20170915 9

Lung adenocarcinoma is the most common type of lung cancer. Unfortunately, lung adenocarcinoma has a poor prognosis and the pathogenesis remains unclear. Mitochondria are important mediators of tumorigenesis. However, the proteomics profile of lung adenocarcinoma mitochondrial proteins has not been elucidated. In this study, we investigated differences in the mitochondrial protein profiles between lung adenocarcinomas and normal tissue. Laser capture microdissection (LCM) was used to isolate the ...[more]

PMID: 28979670

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Project description:Canine oral tumors are relatively common neoplasms in dogs. For disease monitoring and early diagnosis, salivary biomarkers are appropriate because saliva collection is non-invasive and requires no professional skills. In the era of omics, matrix-assisted laser desorption/ionization with time-of-flight mass spectrometry (MALDI-TOF MS) coupled with liquid chromatography-tandem MS (LC-MS/MS) are suitable to identify potential disease-associated peptides and proteins. The present study aimed to use MALDI-TOF MS and LC-MS/MS to search for particular peptide mass fingerprints (PMFs) and conceivable biomarkers in saliva of dogs with early- and late-stage oral melanoma (EOM and LOM, respectively), oral squamous cell carcinoma (OSCC), benign oral tumors (BN), and periodontitis and healthy controls (CP). Pooled saliva samples in each group were used to be representative of population change. Unique PMFs were obtained and specific peptide fragments were sequenced by LC-MS/MS and BLAST-searched with mammalian protein databases. Seven peptide fragments appeared in the tumor groups (EOM, LOM, OSCC and BN) at 1096, 1208, 1322, 1794, 1864, 2354 and 2483 Da, two peptide fragments appeared in the LOM and OSCC groups at 2450 and 3492 Da, and in the CP controls at 2544 and 3026 Da. Also, protein-chemotherapy drug interaction networks were exhibited. Using western blot analysis, the expression of sentrin-specific protease 7 (SENP7), a peptide fragment at 1096 Da, in OSCC was significantly increased, as was the expression of TLR4, a peptide fragment at 3492 Da, in LOM and OSCC, compared with the CP group. The expression of nuclear factor kappa B (NF-κB), a TLR4 partner, was notably increased in OSCC compared with CP, BN and EOM. The expression was also enhanced in LOM compared with EOM. Expressed protein sequences from western blots were verified by LC-MS/MS. Western blots were then performed with individual samples in each group. The results showed the elevated expression of TLR4 in LOM and OSCC, compared with that in CP and BN, the increased expression of NF-κB in LOM and OSCC, compared with CP and in LOM compared with BN, and the enhanced expression of SENP7 in LOM and OSCC, compared with that in CP and BN. In conclusion, discrete clusters of EOM, LOM, OSCC, BN and CP groups and potential protein candidates associated with the diseases were demonstrated by salivary proteomics. Western blot analysis verified SENP7, TLR4 and NF-κB as potential salivary biomarkers of canine oral tumors.

Dataset Information

Quantitative proteomics analysis of mitochondrial proteins in lung adenocarcinomas and normal lung tissue using iTRAQ and tandem mass spectrometry.

Publications

Quantitative proteomics analysis of mitochondrial proteins in lung adenocarcinomas and normal lung tissue using iTRAQ and tandem mass spectrometry.

Similar Datasets

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