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

Background: The main reason why lung cancer has maintained a high rate of morbidity and mortality is that its early diagnosis is difficult. No current lung cancer screening is recommended by any major medical organization due to the lack of sensitive and specific screening technologies. Thus, this s...

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Autores principales: Jia, Liyuan, Ma, Tianran, Liang, Yiqian, Du, Haoqi, Shu, Jian, Liu, Xiawei, Zhang, Zhiwei, Yu, Hanjie, Chen, Mingwei, Li, Zheng
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9049724/
https://www.ncbi.nlm.nih.gov/pubmed/35493902
http://dx.doi.org/10.1039/c9ra10077f
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author Jia, Liyuan
Ma, Tianran
Liang, Yiqian
Du, Haoqi
Shu, Jian
Liu, Xiawei
Zhang, Zhiwei
Yu, Hanjie
Chen, Mingwei
Li, Zheng
author_facet Jia, Liyuan
Ma, Tianran
Liang, Yiqian
Du, Haoqi
Shu, Jian
Liu, Xiawei
Zhang, Zhiwei
Yu, Hanjie
Chen, Mingwei
Li, Zheng
author_sort Jia, Liyuan
collection PubMed
description Background: The main reason why lung cancer has maintained a high rate of morbidity and mortality is that its early diagnosis is difficult. No current lung cancer screening is recommended by any major medical organization due to the lack of sensitive and specific screening technologies. Thus, this study aimed to systematically investigate the correlation between the alterations in serum glycosylation and three main types of lung cancers (SCLC, ADC and SqCC). Materials and methods: We investigated the protein glycopatterns in sera from 333 subjects (65 healthy volunteers, 38 benign lung disease patients, 49 small cell lung cancer patients, and 181 NSCLC patients) using a lectin microarray. A serum microarray was produced to evaluate and verify the terminal carbohydrate moieties of the glycoproteins in individual serum samples from 30 cases simultaneously. Results: There were 16 lectins (e.g., RCA120, BS-I, and UEA-I), 24 lectins (e.g., HHL, PTL-I, and MAL-II), and 18 lectins (e.g., GSL-I, LEL, and ACA) that exhibited significant differences in serum protein glycopatterns in the patients with SCLC, ADC and SqCC compared with the controls (HV and BPD). There were 6 lectins (e.g., EEL, NPA, and LEL) that exhibited significantly increased NFIs in ADC and SqCC compared with SCLC. Also, there were 5 lectins (e.g., Jacalin, BS-I, and UEA-I) that exhibited significantly decreased NFIs in ADC compared with SCLC and SqCC. Conclusions: This study can facilitate the discovery of potential biomarkers for the differential diagnosis of lung cancer based on the precise alteration in serum protein glycopatterns.
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spelling pubmed-90497242022-04-29 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, Jian Liu, Xiawei Zhang, Zhiwei Yu, Hanjie Chen, Mingwei Li, Zheng RSC Adv Chemistry Background: The main reason why lung cancer has maintained a high rate of morbidity and mortality is that its early diagnosis is difficult. No current lung cancer screening is recommended by any major medical organization due to the lack of sensitive and specific screening technologies. Thus, this study aimed to systematically investigate the correlation between the alterations in serum glycosylation and three main types of lung cancers (SCLC, ADC and SqCC). Materials and methods: We investigated the protein glycopatterns in sera from 333 subjects (65 healthy volunteers, 38 benign lung disease patients, 49 small cell lung cancer patients, and 181 NSCLC patients) using a lectin microarray. A serum microarray was produced to evaluate and verify the terminal carbohydrate moieties of the glycoproteins in individual serum samples from 30 cases simultaneously. Results: There were 16 lectins (e.g., RCA120, BS-I, and UEA-I), 24 lectins (e.g., HHL, PTL-I, and MAL-II), and 18 lectins (e.g., GSL-I, LEL, and ACA) that exhibited significant differences in serum protein glycopatterns in the patients with SCLC, ADC and SqCC compared with the controls (HV and BPD). There were 6 lectins (e.g., EEL, NPA, and LEL) that exhibited significantly increased NFIs in ADC and SqCC compared with SCLC. Also, there were 5 lectins (e.g., Jacalin, BS-I, and UEA-I) that exhibited significantly decreased NFIs in ADC compared with SCLC and SqCC. Conclusions: This study can facilitate the discovery of potential biomarkers for the differential diagnosis of lung cancer based on the precise alteration in serum protein glycopatterns. The Royal Society of Chemistry 2020-02-18 /pmc/articles/PMC9049724/ /pubmed/35493902 http://dx.doi.org/10.1039/c9ra10077f Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by/3.0/
spellingShingle Chemistry
Jia, Liyuan
Ma, Tianran
Liang, Yiqian
Du, Haoqi
Shu, Jian
Liu, Xiawei
Zhang, Zhiwei
Yu, Hanjie
Chen, Mingwei
Li, Zheng
Alterations in serum protein glycopatterns related to small cell lung cancer, adenocarcinoma and squamous carcinoma of the lung
title Alterations in serum protein glycopatterns related to small cell lung cancer, adenocarcinoma and squamous carcinoma of the lung
title_full Alterations in serum protein glycopatterns related to small cell lung cancer, adenocarcinoma and squamous carcinoma of the lung
title_fullStr Alterations in serum protein glycopatterns related to small cell lung cancer, adenocarcinoma and squamous carcinoma of the lung
title_full_unstemmed Alterations in serum protein glycopatterns related to small cell lung cancer, adenocarcinoma and squamous carcinoma of the lung
title_short Alterations in serum protein glycopatterns related to small cell lung cancer, adenocarcinoma and squamous carcinoma of the lung
title_sort alterations in serum protein glycopatterns related to small cell lung cancer, adenocarcinoma and squamous carcinoma of the lung
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9049724/
https://www.ncbi.nlm.nih.gov/pubmed/35493902
http://dx.doi.org/10.1039/c9ra10077f
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