Study on the differences in N-glycosylation of disease-specific immune and inflammatory proteins between lung cancer and lung benign disease

Objective To define the differences in N-glycosylation of disease-specific immune and inflammatory proteins between lung cancer and benign lung disease. Methods A group of disease-specific serum immunoin-flammation-related protein complexes (IIRPCs) were isolated from the sera of two patients wit...

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Main Author: DU Yu-ying, WANG Yue, LAI Zhi-zhen, TIAN Zhi-xin, LI Zhi-li
Format: Article
Language:zho
Published: Institute of Basic Medical Sciences and Peking Union Medical College Hospital, Chinese Academy of Medical Sciences / Peking Union Medical College. 2020-08-01
Series:Jichu yixue yu linchuang
Subjects:
Online Access:http://journal11.magtechjournal.com/Jwk_jcyxylc/fileup/1001-6325/PDF/a200443.pdf
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author DU Yu-ying, WANG Yue, LAI Zhi-zhen, TIAN Zhi-xin, LI Zhi-li
author_facet DU Yu-ying, WANG Yue, LAI Zhi-zhen, TIAN Zhi-xin, LI Zhi-li
author_sort DU Yu-ying, WANG Yue, LAI Zhi-zhen, TIAN Zhi-xin, LI Zhi-li
collection DOAJ
description Objective To define the differences in N-glycosylation of disease-specific immune and inflammatory proteins between lung cancer and benign lung disease. Methods A group of disease-specific serum immunoin-flammation-related protein complexes (IIRPCs) were isolated from the sera of two patients with lung adenocarcinoma and chronic pneumonia, by native-polyacrylamide gel electrophoresis (native-PAGE). The intact glycopeptides were obtained by in-gel trypsin digestion and then enriched by graphite phase carbon nitride. The glycopeptides were identified by high performance liquid chromatography-tandem mass spectrometry (HPLC-MS/MS) coupled with GPSeeker database software. Results Totally 89 glycopeptides from 12 proteins were identified, 21 of which only existed in benign lung disease and 38 only be found in lung cancer samples. Ten of the 63 unique glycoforms from the 89 glycopeptides only existed in benign lung disease and only 21 were found in lung cancer. Conclusions The specific differences in N-glycosylation of disease-specific immune and inflammatory proteins are found between benign lung disease and lung cancer. These findings indicate that N-glycosylation may function as potential biomarker applied in diagnosis and prognosis of chronic diseases as well as a novel sight to molecular mechanism of chronic diseases.
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spelling doaj.art-0a636f220c2b462c9dfeaed66b0869642024-01-05T03:17:00ZzhoInstitute of Basic Medical Sciences and Peking Union Medical College Hospital, Chinese Academy of Medical Sciences / Peking Union Medical College.Jichu yixue yu linchuang1001-63252020-08-0140810961102Study on the differences in N-glycosylation of disease-specific immune and inflammatory proteins between lung cancer and lung benign diseaseDU Yu-ying, WANG Yue, LAI Zhi-zhen, TIAN Zhi-xin, LI Zhi-li01. Department of Biophysics and Structural Biology, Institute of Basic Medical Sciences CAMS,School of Basic Medicine PUMC, Beijing 100005; ;2. Shanghai Key Laboratory of Chemical Assessment and Sustainability, School of Chemical Science & Engineering, Tongji University, Shanghai 200092, ChinaObjective To define the differences in N-glycosylation of disease-specific immune and inflammatory proteins between lung cancer and benign lung disease. Methods A group of disease-specific serum immunoin-flammation-related protein complexes (IIRPCs) were isolated from the sera of two patients with lung adenocarcinoma and chronic pneumonia, by native-polyacrylamide gel electrophoresis (native-PAGE). The intact glycopeptides were obtained by in-gel trypsin digestion and then enriched by graphite phase carbon nitride. The glycopeptides were identified by high performance liquid chromatography-tandem mass spectrometry (HPLC-MS/MS) coupled with GPSeeker database software. Results Totally 89 glycopeptides from 12 proteins were identified, 21 of which only existed in benign lung disease and 38 only be found in lung cancer samples. Ten of the 63 unique glycoforms from the 89 glycopeptides only existed in benign lung disease and only 21 were found in lung cancer. Conclusions The specific differences in N-glycosylation of disease-specific immune and inflammatory proteins are found between benign lung disease and lung cancer. These findings indicate that N-glycosylation may function as potential biomarker applied in diagnosis and prognosis of chronic diseases as well as a novel sight to molecular mechanism of chronic diseases.http://journal11.magtechjournal.com/Jwk_jcyxylc/fileup/1001-6325/PDF/a200443.pdfbiomarker disease-specific protein|disease-specific glycopeptide|disease-specific glycoform|benign and malignant lung diseases
spellingShingle DU Yu-ying, WANG Yue, LAI Zhi-zhen, TIAN Zhi-xin, LI Zhi-li
Study on the differences in N-glycosylation of disease-specific immune and inflammatory proteins between lung cancer and lung benign disease
Jichu yixue yu linchuang
biomarker disease-specific protein|disease-specific glycopeptide|disease-specific glycoform|benign and malignant lung diseases
title Study on the differences in N-glycosylation of disease-specific immune and inflammatory proteins between lung cancer and lung benign disease
title_full Study on the differences in N-glycosylation of disease-specific immune and inflammatory proteins between lung cancer and lung benign disease
title_fullStr Study on the differences in N-glycosylation of disease-specific immune and inflammatory proteins between lung cancer and lung benign disease
title_full_unstemmed Study on the differences in N-glycosylation of disease-specific immune and inflammatory proteins between lung cancer and lung benign disease
title_short Study on the differences in N-glycosylation of disease-specific immune and inflammatory proteins between lung cancer and lung benign disease
title_sort study on the differences in n glycosylation of disease specific immune and inflammatory proteins between lung cancer and lung benign disease
topic biomarker disease-specific protein|disease-specific glycopeptide|disease-specific glycoform|benign and malignant lung diseases
url http://journal11.magtechjournal.com/Jwk_jcyxylc/fileup/1001-6325/PDF/a200443.pdf
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