Proteomics-based identification of tumor relevant proteins in lung adenocarcinoma

Zhou, Xin; Xue, Liyan; Hao, Lihong; Liu, Shuqing; Zhou, Fachen; Xiong, Hai; Qi, Xiaoyu; Lin, Dongmei; Shao, Shujuan

doi:10.1016/j.biopha.2013.06.005

Cited by 11 publications

(10 citation statements)

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“…Chen et al used 2D-PAGE, MALDI MS to analyze Stage I and III lung adenocarcinomas and found proteins that were heavily implicated in antioxidant response systems and cellular metabolism [45] consistent with our findings. Zhou et al used 2D-DIGE with followed-up by TMA IHC and blood studies of TyrRS and MACF-1 [46]. However, Zhou et al evaluated tissues from stage II and III lung adenocarcinoma and thus might not be directly compared to our results for stage IA or IB given the inherent heterogeneity that exists among different tumor stages.…”

Section: Discussionmentioning

confidence: 99%

Proteomic profiling of lung adenocarcinoma indicates heightened DNA repair, antioxidant mechanisms and identifies LASP1 as a potential negative predictor of survival

et al. 2016

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BackgroundLung cancer is the leading cause of cancer mortality in the United States. Non-small cell lung cancer accounts for 85% of all lung cancers for which adenocarcinoma is the most common histological type. Management of lung cancer is hindered by high false-positive rates due to difficulty resolving between benign and malignant tumors. Better molecular analysis comparing malignant and non-malignant tissues will provide important evidence of the underlying biology contributing to tumorigenesis.MethodsWe utilized a proteomics approach to analyze 38 malignant and non-malignant paired tissue samples obtained from current or former smokers with early stage (Stage IA/IB) lung adenocarcinoma. Statistical mixed effects modeling and orthogonal partial least squares discriminant analysis were used to identify key cancer-associated perturbations in the adenocarcinoma proteome. Identified proteins were subsequently assessed against clinicopathological variables.ResultsTop cancer-associated protein alterations were characterized by: (1) elevations in APEX1, HYOU1 and PDIA4, indicative of increased DNA repair machinery and heightened anti-oxidant defense mechanisms; (2) increased LRPPRC, STOML2, COPG1 and EPRS, suggesting altered tumor metabolism and inflammation; (3) reductions in SPTB, SPTA1 and ANK1 implying dysregulation of membrane integrity; and (4) decreased SLCA41 suggesting altered pH regulation. Increased protein levels of HYOU1, EPRS and LASP1 in NSCLC adenocarcinoma was independently validated by tissue microarray immunohistochemistry. Immunohistochemistry for HYOU1 and EPRS indicated AUCs of 0.952 and 0.841, respectively, for classifying tissue as malignant. Increased LASP1 correlated with poor overall survival (HR 3.66 per unit increase; CI 1.37–9.78; p = 0.01).ConclusionThese results reveal distinct proteomic changes associated with early stage lung adenocarcinoma that may be useful prognostic indicators and therapeutic targets.Electronic supplementary materialThe online version of this article (doi:10.1186/s12014-016-9132-y) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Proteomic profiling of lung adenocarcinoma indicates heightened DNA repair, antioxidant mechanisms and identifies LASP1 as a potential negative predictor of survival

et al. 2016

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“…К числу экзосомных белков также относятся Ras-related protein (P51149) и Threonine-tRNA ligase (P26639), для которых отмечено увеличение и снижение содержания Phospholipid scramblase (O15162), Monoacylglycerol lipase (Q8N2K0) у больных по сравнению с контролем, соответсвенно. Среди секретируемых, также как и в наших экспериментах, ранее было определено повышенное содержание Haptoglobin и Complement factor H (P08603) в образцах сыворотки пациентов с немелкоклеточным раком лёгких по сравнению со здоровыми индивидуумами [12], в то время как экспрессия Lumican (P51884) была снижена [13].…”

Section: Discussionunclassified

Quantitative targeted screening of proteins associated with lung adenocarcinoma cancer by the method of selected reaction monitoring

et al. 2018

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In the present study, we applied selected reaction monitoring (SRM) to a group of proteins that were previously reported to be associated with lung cancer (Novikova S.E. et al. (2017) Biomeditsinskaya khimiya, 63, 181-210. [1]). Measurements were performed on 59 plasma samples. These samples included: 23 samples of plasma of patients diagnosed with lung adenocarcinoma (LAC), 11 samples of plasma of patients diagnosed with squamous cell lung carcinoma (SqCC), 25 samples of donors with no previous history of oncological diseases, and one pooled sample from each of the above group. As a result of the SRM measurements 52 proteins were detected at least in one individual plasma sample. Statistical analysis showed that there were two groups confidently differentiated by the concentration value of 8 proteins wherein 5 proteins displayed increased level (P00738, P26639, P21926, P08603, P51149) in LAC group and 3 proteins (P51884, O15162, Q8N2K0) indicated diminishing the concentration level towards the control level. Data on protein concentrations obtained for LAC and SqCC did not distinguish the samples by statistical clustering analysis. These potential biomarkers can be used for further development of methods for early diagnostics of lung cancer.

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“…Importantly, the growth and migration of LRS knockdown A549 cells were inhibited, indicating that this molecule played an important role in the development of lung cancer ( Shin et al, 2008 ). Furthermore, tyrosyl-tRNA synthetase (TyrRS) and microtubule-actin crosslinking factor 1 (MACF-1) were at higher abundance in lung adenocarcinoma tissues than adjacent normal tissues ( Zhou et al, 2013 ). Among them, the levels of TyrRS were difference between N1, N2, and N3, while the levels of MACF-1 were associated with T stage, N stage and clinical stage.…”

Section: Roles Of Arss In Cancermentioning

confidence: 99%

Roles of Aminoacyl-tRNA Synthetases in Cancer

Zhou

Sun

Nie

et al. 2020

Front. Cell Dev. Biol.

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Aminoacyl-tRNA synthetases (ARSs) catalyze the ligation of amino acids to their cognate transfer RNAs (tRNAs), thus playing an important role in protein synthesis. In eukaryotic cells, these enzymes exist in free form or in the form of multi-tRNA synthetase complex (MSC). The latter contains nine cytoplasmic ARSs and three ARS-interacting multifunctional proteins (AIMPs). Normally, ARSs and AIMPs are regarded as housekeeping molecules without additional functions. However, a growing number of studies indicate that ARSs are involved in a variety of physiological and pathological processes, especially tumorigenesis. Here, we introduce the roles of ARSs and AIMPs in certain cancers, such as colon cancer, lung cancer, breast cancer, gastric cancer and pancreatic cancer. Furthermore, we particularly focus on their potential clinical applications in cancer, aiming at providing new insights into the pathogenesis and treatment of cancer.

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Proteomics-based identification of tumor relevant proteins in lung adenocarcinoma

Cited by 11 publications

References 32 publications

Proteomic profiling of lung adenocarcinoma indicates heightened DNA repair, antioxidant mechanisms and identifies LASP1 as a potential negative predictor of survival

Proteomic profiling of lung adenocarcinoma indicates heightened DNA repair, antioxidant mechanisms and identifies LASP1 as a potential negative predictor of survival

Quantitative targeted screening of proteins associated with lung adenocarcinoma cancer by the method of selected reaction monitoring

Roles of Aminoacyl-tRNA Synthetases in Cancer

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