Alterations in serum protein glycopatterns related to small cell lung cancer, adenocarcinoma and squamous carcinoma of the lung

Jia, Liyuan; Ma, Tianran; Liang, Yiqian; Du, Haoqi; Shu, Jiwu; Li, Zheng; Zhang, Zhiwei; Yu, Hanjie; Chen, Mingwei

doi:10.1039/c9ra10077f

Cited by 7 publications

(6 citation statements)

References 43 publications

(42 reference statements)

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“…These unique findings could facilitate the study of biomarkers in the saliva of patients with ADC, SCC, and SCLC based on the precise alteration of galactosylated N‐glycans. Previously, with the use of serum microarray technology, we found that the expression levels of protein glycopatterns identified by BS‐I were significantly increased in the sera of SCLC compared to HV [20]. Our present findings were generally consistent with aberrant galactosylation in the serum of patients with SCLC, and we infer that this may be the result of many components of the blood entering the saliva by active transport, passive diffusion, or extracellular ultrafiltration [15].…”

Section: Discussionsupporting

confidence: 84%

“…Our previous studies have shown that salivary proteoglycan patterns change differently in the saliva of patients with different diseases (e.g., Gastric Cancer, Breast Cancer, Liver Cancer) [17–19]. In our previous study, we found altered serum glycosylation levels in patients with benign pulmonary disease (BPD) and LC [20]. However, so far it is not clear whether there are associated glycosylation changes in the saliva of patients with lung disease.…”

Section: Introductionmentioning

confidence: 99%

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Integrated glycomics strategy for galactosylated‐N‐glycans recognized by Bandeiraea Simplicifolia Lectin I in salivary proteins associated with lung cancer

Zhang

Xie

Tang

et al. 2022

Proteomics Clinical Apps

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Purpose Lung cancer (LC) is the leading cause of cancer‐related deaths worldwide, mainly due to late diagnosis and poor prognosis. Saliva is an important source for discovering biomarkers and contains an abundance of biological information. The purpose of this study was to determine whether galactosylation levels of salivary proteins are associated with LC. Experimental design First, we analyzed the alterations of the glycopatterns recognized by Bandeiraea Simplicifolia Lectin I (BS‐I) in five groups (healthy volunteers [HV]: 28, benign pulmonary disease [BPD]: 27, lung adenocarcinoma [ADC]: 39, squamous cell carcinoma [SCC]: 28, small‐cell lung cancer [SCLC]: 22) of 144 saliva samples using lectin microarrays. Pooled samples from each group were subsequently validated by the lectin blotting technique. Finally, the N‐glycan profiles of their salivary glycoproteins isolated by the BS‐I‐magnetic particle conjugates from pooled samples for each group were analyzed by MALDI‐TOF/TOF‐MS. Results The results showed that the expression level of galactosylated glycans recognized by BS‐I was significantly increased in patients with LC compared with BPD and HV. Receiver operating characteristic (ROC) analysis indicated that the levels of salivary glycopattern recognized by BS‐I could discriminate lung disease (BPD, ADC, SCC, and SCLC) and HV with an AUC of 0.700 (95% CI: 0.589–0.812), and discriminate LC and BPD with an AUC of 0.860 (95% CI: 0.763–0.956). Also, the proportion of galactosylated N‐glycans in ADC (38.4%), SCC (43.1%), and SCLC (39.5%) increased compared to HV (30.1%) and BPD (33.7%), and two galactosylated N‐glycan peaks (m/z 1828.683, 2418.853) could be identified only in the LC groups (ADC, SCC, and SCLC). Conclusions and clinical relevance These findings could provide crucial information on galactosylated N‐linked glycans associated with LC and facilitate the study of LC biomarkers based on precise alterations of galactosylated N‐glycans in saliva.

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Section: Discussionsupporting

confidence: 84%

Section: Introductionmentioning

confidence: 99%

Integrated glycomics strategy for galactosylated‐N‐glycans recognized by Bandeiraea Simplicifolia Lectin I in salivary proteins associated with lung cancer

Zhang

Xie

Tang

et al. 2022

Proteomics Clinical Apps

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“…Our previous study revealed that mutations in oncogenic drivers are associated with the progression and metastasis of LUAD, and the resulting alterations can be identified from circulating glycoproteins . Unique changes have been identified in serum glycoprotein glycoforms among small cell lung cancer (SCLC), LUAD, and squamous cell carcinoma (SCC) . Serum samples from lung cancer patients and age-matched controls revealed substantial increases in glycans containing sialyl Lewis X (sLe X ), monoantennary glycans, and highly sialylated glycans, whereas core-fucosylated biantennary N-glycans were diminished in lung cancer patients .…”

Section: Introductionmentioning

confidence: 99%

“…36 Unique changes have been identified in serum glycoprotein glycoforms among small cell lung cancer (SCLC), LUAD, and squamous cell carcinoma (SCC). 37 Serum samples from lung cancer patients and age-matched controls revealed substantial increases in glycans containing sialyl Lewis X (sLe X ), monoantennary glycans, and highly sialylated glycans, whereas core-fucosylated biantennary N-glycans were diminished in lung cancer patients. 38 However, using certain subsets of N-glycans, such as disialylated, tri-or tetra-antennary, or core-fucosylated glycans, as disease biomarkers results in poor sensitivity and specificity.…”

Section: ■ Introductionmentioning

confidence: 99%

Diagnostic Potential of Serum Glycome Analysis in Lung Cancer: A Glycopattern Study

Hu,

Ge,

Xia

et al. 2023

J. Proteome Res.

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Lung cancer is the leading cause of cancer-related death, with high morbidity and mortality rates due to the lack of reliable methods for diagnosing lung cancer at an early stage. Lowdose computed tomography can help detect abnormal areas in the lungs, but only 16% of cases are diagnosed early. Tests for lung cancer markers are often employed to determine genetic expression or mutations in lung carcinogenesis. Serum glycome analysis is a promising new method for early lung cancer diagnosis as glycopatterns exhibit significant differences in lung cancer patients. In this study, we employed a solid-phase chemoenzymatic method to systematically compare glycopatterns in benign cases, adenocarcinoma before and after surgery, and advanced stages of adenocarcinoma. Our findings indicate that serum high-mannose levels are elevated in both benign cases and adenocarcinoma, while complex N-glycans, including fucose and 2,6-linked sialic acid, are downregulated in the serum. Subsequently, we developed an algorithm that utilizes 16 altered N-glycans, 7 upregulated and 9 downregulated, to generate a score based on their intensity. This score can predict the stages of cancer progression in patients through glycan characterization. This methodology offers a potential means of diagnosing lung cancer through serum glycome analysis.

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“…1 Lung cancer patients have a poor prognosis and a 5 year survival rate of less than 20%. 2 However, patients diagnosed at an early stage and who have surgery experience an 86% overall 5 year survival. Early diagnosis and therapy is critical to improving the survival rate of lung cancer.…”

Section: Introductionmentioning

confidence: 99%

Identification of a novel DNA aptamer that selectively targets lung cancer serum

Zhao

Huang

et al. 2021

RSC Adv.

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Alterations in serum protein glycopatterns related to small cell lung cancer, adenocarcinoma and squamous carcinoma of the lung

Abstract: The main reason why lung cancer has maintained a high rate of morbidity and mortality is that its early diagnosis is difficult.

Cited by 7 publications

References 43 publications

Integrated glycomics strategy for galactosylated‐N‐glycans recognized by Bandeiraea Simplicifolia Lectin I in salivary proteins associated with lung cancer

Integrated glycomics strategy for galactosylated‐N‐glycans recognized by Bandeiraea Simplicifolia Lectin I in salivary proteins associated with lung cancer

Diagnostic Potential of Serum Glycome Analysis in Lung Cancer: A Glycopattern Study

Identification of a novel DNA aptamer that selectively targets lung cancer serum

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