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The glycoproteomics of hawk and caiman tears

BACKGROUND: Glycoproteins are important tear components that participate in the stability of the ocular surface. However, the glycopeptides that are present in the tears of wild animals have not yet been described. This work aimed to describe the glycoproteomic profile of roadside hawk (Rupornis mag...

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Autores principales: Raposo, Ana Cláudia, Lebrilla, Carlito, Portela, Ricardo Wagner, Xu, Gege, Oriá, Arianne Pontes
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8656020/
https://www.ncbi.nlm.nih.gov/pubmed/34886864
http://dx.doi.org/10.1186/s12917-021-03088-1
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author Raposo, Ana Cláudia
Lebrilla, Carlito
Portela, Ricardo Wagner
Xu, Gege
Oriá, Arianne Pontes
author_facet Raposo, Ana Cláudia
Lebrilla, Carlito
Portela, Ricardo Wagner
Xu, Gege
Oriá, Arianne Pontes
author_sort Raposo, Ana Cláudia
collection PubMed
description BACKGROUND: Glycoproteins are important tear components that participate in the stability of the ocular surface. However, the glycopeptides that are present in the tears of wild animals have not yet been described. This work aimed to describe the glycoproteomic profile of roadside hawk (Rupornis magnirostris) and caiman (Caiman latirostris) tears. METHODS: Tears collected from 10 hawks and 70 caimans using Schirmer tear test strips were used in this study. The samples were submitted to trypsin digestion and separated using a reverse-phase column coupled to a mass spectrometer associated to a nanospray ionization source. The glycoproteins were categorized as: cellular components, biological processes and molecular function, according to the UniProt Knowledgebase. RESULTS: As shown by the liquid chromatography–mass spectrometry, all glycopeptides found were classified as N-type. Of the 51 glycoproteins that were identified in the hawk tear film, the most abundant were ovotransferrin, globulins and complement system proteins. In the caiman tear film, 29 glycoproteins were identified. The most abundant caiman glycoproteins were uncharacterized proteins, ATPases, globulins and proteasome components. Ontological characterization revealed that the glycoproteins were extracellular, and the most identified molecular function was endopeptidase activity for both species. CONCLUSION: Glycoproteins are abundant in the tear film of the bird and reptile species studied herein, and all these molecules were shown to have N-type modifications. Location at the extracellular space and an endopeptidase inhibitor activity were the main cell component and molecular function for both species, respectively. These profiles showed differences when compared to human tears, are possibly linked to adaptive processes and can be the basis for further studies on the search of disease biomarkers. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12917-021-03088-1.
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spelling pubmed-86560202021-12-10 The glycoproteomics of hawk and caiman tears Raposo, Ana Cláudia Lebrilla, Carlito Portela, Ricardo Wagner Xu, Gege Oriá, Arianne Pontes BMC Vet Res Research BACKGROUND: Glycoproteins are important tear components that participate in the stability of the ocular surface. However, the glycopeptides that are present in the tears of wild animals have not yet been described. This work aimed to describe the glycoproteomic profile of roadside hawk (Rupornis magnirostris) and caiman (Caiman latirostris) tears. METHODS: Tears collected from 10 hawks and 70 caimans using Schirmer tear test strips were used in this study. The samples were submitted to trypsin digestion and separated using a reverse-phase column coupled to a mass spectrometer associated to a nanospray ionization source. The glycoproteins were categorized as: cellular components, biological processes and molecular function, according to the UniProt Knowledgebase. RESULTS: As shown by the liquid chromatography–mass spectrometry, all glycopeptides found were classified as N-type. Of the 51 glycoproteins that were identified in the hawk tear film, the most abundant were ovotransferrin, globulins and complement system proteins. In the caiman tear film, 29 glycoproteins were identified. The most abundant caiman glycoproteins were uncharacterized proteins, ATPases, globulins and proteasome components. Ontological characterization revealed that the glycoproteins were extracellular, and the most identified molecular function was endopeptidase activity for both species. CONCLUSION: Glycoproteins are abundant in the tear film of the bird and reptile species studied herein, and all these molecules were shown to have N-type modifications. Location at the extracellular space and an endopeptidase inhibitor activity were the main cell component and molecular function for both species, respectively. These profiles showed differences when compared to human tears, are possibly linked to adaptive processes and can be the basis for further studies on the search of disease biomarkers. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12917-021-03088-1. BioMed Central 2021-12-09 /pmc/articles/PMC8656020/ /pubmed/34886864 http://dx.doi.org/10.1186/s12917-021-03088-1 Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/ (https://creativecommons.org/publicdomain/zero/1.0/) ) applies to the data made available in this article, unless otherwise stated in a credit line to the data.
spellingShingle Research
Raposo, Ana Cláudia
Lebrilla, Carlito
Portela, Ricardo Wagner
Xu, Gege
Oriá, Arianne Pontes
The glycoproteomics of hawk and caiman tears
title The glycoproteomics of hawk and caiman tears
title_full The glycoproteomics of hawk and caiman tears
title_fullStr The glycoproteomics of hawk and caiman tears
title_full_unstemmed The glycoproteomics of hawk and caiman tears
title_short The glycoproteomics of hawk and caiman tears
title_sort glycoproteomics of hawk and caiman tears
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8656020/
https://www.ncbi.nlm.nih.gov/pubmed/34886864
http://dx.doi.org/10.1186/s12917-021-03088-1
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