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Characterization of human tear proteome reveals differentially abundance proteins in thyroid-associated ophthalmopathy

BACKGROUND: Thyroid-associated ophthalmopathy (TAO) is a common orbital inflammatory disease, but the abnormal expression of proteins in tears of TAO patients has not been systematically studied. The purpose of this study is to compare and analyze the total tear protein profile of TAO patients and t...

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Autores principales: Zhou, Xiaoqing, Wei, Ruili, Wang, Rui
Formato: Online Artículo Texto
Lenguaje:English
Publicado: PeerJ Inc. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9285480/
https://www.ncbi.nlm.nih.gov/pubmed/35846879
http://dx.doi.org/10.7717/peerj.13701
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author Zhou, Xiaoqing
Wei, Ruili
Wang, Rui
author_facet Zhou, Xiaoqing
Wei, Ruili
Wang, Rui
author_sort Zhou, Xiaoqing
collection PubMed
description BACKGROUND: Thyroid-associated ophthalmopathy (TAO) is a common orbital inflammatory disease, but the abnormal expression of proteins in tears of TAO patients has not been systematically studied. The purpose of this study is to compare and analyze the total tear protein profile of TAO patients and to provide protein cues for TAO pathogenesis. METHODS: Tear samples were isolated from 30 TAO patients with obvious ocular surface damage and 30 healthy control subjects. Tear samples from 30 individuals were mixed and divided into three sample pools. Easy nano-scale LC-MS/MS based on labeling-free quantitative technology was utilized to profile tear proteome. RESULTS: Here, electrospray ionization mass spectra and SDS-PAGE results confirmed the good parallelisms among samples. A total of 313 proteins were obtained from six tear pools, among them, 103 differential abundance proteins (DAPs) were identified, including 99 up-regulated DAPs (including APOA1, HV103, IGH, and Transferrin variant) and four down-regulated DAPs (including FABA, VCC1, NUCB2, and E-cadherin) in the TAO group compared with the control group. GO analysis showed that up-regulated DAPs were mainly enriched in lipid metabolism and platelet molecular function, and down-regulated DAPs were involved in binding, cell junction, and cellular process. KEGG results indicated that DAPs were involved in 117 kinds of signal transduction pathways, among which the immune-related pathway of complement and coagulation cascades had the greatest relevance. CONCLUSION: In conclusion, label-free LC-MS/MS is an effective strategy for profiling tear proteins component. Our study provides proteins and pathways altered in TAO and provides protein cues for further study on the precise mechanism of TAO pathogenesis.
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spelling pubmed-92854802022-07-16 Characterization of human tear proteome reveals differentially abundance proteins in thyroid-associated ophthalmopathy Zhou, Xiaoqing Wei, Ruili Wang, Rui PeerJ Biochemistry BACKGROUND: Thyroid-associated ophthalmopathy (TAO) is a common orbital inflammatory disease, but the abnormal expression of proteins in tears of TAO patients has not been systematically studied. The purpose of this study is to compare and analyze the total tear protein profile of TAO patients and to provide protein cues for TAO pathogenesis. METHODS: Tear samples were isolated from 30 TAO patients with obvious ocular surface damage and 30 healthy control subjects. Tear samples from 30 individuals were mixed and divided into three sample pools. Easy nano-scale LC-MS/MS based on labeling-free quantitative technology was utilized to profile tear proteome. RESULTS: Here, electrospray ionization mass spectra and SDS-PAGE results confirmed the good parallelisms among samples. A total of 313 proteins were obtained from six tear pools, among them, 103 differential abundance proteins (DAPs) were identified, including 99 up-regulated DAPs (including APOA1, HV103, IGH, and Transferrin variant) and four down-regulated DAPs (including FABA, VCC1, NUCB2, and E-cadherin) in the TAO group compared with the control group. GO analysis showed that up-regulated DAPs were mainly enriched in lipid metabolism and platelet molecular function, and down-regulated DAPs were involved in binding, cell junction, and cellular process. KEGG results indicated that DAPs were involved in 117 kinds of signal transduction pathways, among which the immune-related pathway of complement and coagulation cascades had the greatest relevance. CONCLUSION: In conclusion, label-free LC-MS/MS is an effective strategy for profiling tear proteins component. Our study provides proteins and pathways altered in TAO and provides protein cues for further study on the precise mechanism of TAO pathogenesis. PeerJ Inc. 2022-07-12 /pmc/articles/PMC9285480/ /pubmed/35846879 http://dx.doi.org/10.7717/peerj.13701 Text en © 2022 Zhou et al. https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ) and either DOI or URL of the article must be cited.
spellingShingle Biochemistry
Zhou, Xiaoqing
Wei, Ruili
Wang, Rui
Characterization of human tear proteome reveals differentially abundance proteins in thyroid-associated ophthalmopathy
title Characterization of human tear proteome reveals differentially abundance proteins in thyroid-associated ophthalmopathy
title_full Characterization of human tear proteome reveals differentially abundance proteins in thyroid-associated ophthalmopathy
title_fullStr Characterization of human tear proteome reveals differentially abundance proteins in thyroid-associated ophthalmopathy
title_full_unstemmed Characterization of human tear proteome reveals differentially abundance proteins in thyroid-associated ophthalmopathy
title_short Characterization of human tear proteome reveals differentially abundance proteins in thyroid-associated ophthalmopathy
title_sort characterization of human tear proteome reveals differentially abundance proteins in thyroid-associated ophthalmopathy
topic Biochemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9285480/
https://www.ncbi.nlm.nih.gov/pubmed/35846879
http://dx.doi.org/10.7717/peerj.13701
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