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Comparison of camel tear proteins between summer and winter

PURPOSE: Proteins in the tear fluid have positive effects on maintaining the integrity and stabilization of the tear film, which is affected by several environmental factors. The aim of this study is to investigate seasonal variation of protein patterns in camel tears collected during the summer and...

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Autores principales: Chen, Ziyan, Shamsi, Farrukh A., Li, Kaijun, Huang, Qiang, Al-Rajhi, Ali A., Chaudhry, Imtiaz A., Wu, Kaili
Formato: Texto
Lenguaje:English
Publicado: Molecular Vision 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3032277/
https://www.ncbi.nlm.nih.gov/pubmed/21293736
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author Chen, Ziyan
Shamsi, Farrukh A.
Li, Kaijun
Huang, Qiang
Al-Rajhi, Ali A.
Chaudhry, Imtiaz A.
Wu, Kaili
author_facet Chen, Ziyan
Shamsi, Farrukh A.
Li, Kaijun
Huang, Qiang
Al-Rajhi, Ali A.
Chaudhry, Imtiaz A.
Wu, Kaili
author_sort Chen, Ziyan
collection PubMed
description PURPOSE: Proteins in the tear fluid have positive effects on maintaining the integrity and stabilization of the tear film, which is affected by several environmental factors. The aim of this study is to investigate seasonal variation of protein patterns in camel tears collected during the summer and winter season. METHODS: Tears from both eyes of 50 clinically normal camels (Camelus dromedarius) were collected in the summer (June – July) and in the winter (December – January) respectively. Pooled tear protein samples from two seasons were separated by SDS–PAGE and two-dimensional electrophoresis (2-DE). Protein spots of differential expression in two season gels were excised and subjected to in-gel digestion and identification by matrix assisted laser desorption/ionization-time of flight/time of flight-mass spectrum (MALDI-TOF/TOF-MS) analysis. Two differentially expressed proteins, lactoferrin (LF) and vitelline membrane outer layer protein 1 homolog (VMO1 homolog), were validated by western blotting. RESULTS: Thirteen well resolved bands were detected in SDS–PAGE gels of both summer and winter camel tears. By band densitometry, significantly higher intensities of band 6, 7, 11, and lower intensity of band 13 were observed in the summer group compared to the winter group. In 2-DE profiles of camel tears, four protein spots were found expressed differentially in two seasons. Further protein identification by MALDI-TOF/TOF-MS and confirmation by western blotting indicated that there was a significant decrease in LF (p=0.002) and an increase in VMO1 homolog (p=0.042) in tears in the summer compared to the winter. CONCLUSIONS: The seasonal variation of camel tear fluids has been found in the composition of proteins, including LF and VMO1 homolog. This result will expand our knowledge of physiologic characteristics of tear fluids and establish a foundation for the mechanistic studies and clinical practices on ocular surface disorders.
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spelling pubmed-30322772011-02-03 Comparison of camel tear proteins between summer and winter Chen, Ziyan Shamsi, Farrukh A. Li, Kaijun Huang, Qiang Al-Rajhi, Ali A. Chaudhry, Imtiaz A. Wu, Kaili Mol Vis Research Article PURPOSE: Proteins in the tear fluid have positive effects on maintaining the integrity and stabilization of the tear film, which is affected by several environmental factors. The aim of this study is to investigate seasonal variation of protein patterns in camel tears collected during the summer and winter season. METHODS: Tears from both eyes of 50 clinically normal camels (Camelus dromedarius) were collected in the summer (June – July) and in the winter (December – January) respectively. Pooled tear protein samples from two seasons were separated by SDS–PAGE and two-dimensional electrophoresis (2-DE). Protein spots of differential expression in two season gels were excised and subjected to in-gel digestion and identification by matrix assisted laser desorption/ionization-time of flight/time of flight-mass spectrum (MALDI-TOF/TOF-MS) analysis. Two differentially expressed proteins, lactoferrin (LF) and vitelline membrane outer layer protein 1 homolog (VMO1 homolog), were validated by western blotting. RESULTS: Thirteen well resolved bands were detected in SDS–PAGE gels of both summer and winter camel tears. By band densitometry, significantly higher intensities of band 6, 7, 11, and lower intensity of band 13 were observed in the summer group compared to the winter group. In 2-DE profiles of camel tears, four protein spots were found expressed differentially in two seasons. Further protein identification by MALDI-TOF/TOF-MS and confirmation by western blotting indicated that there was a significant decrease in LF (p=0.002) and an increase in VMO1 homolog (p=0.042) in tears in the summer compared to the winter. CONCLUSIONS: The seasonal variation of camel tear fluids has been found in the composition of proteins, including LF and VMO1 homolog. This result will expand our knowledge of physiologic characteristics of tear fluids and establish a foundation for the mechanistic studies and clinical practices on ocular surface disorders. Molecular Vision 2011-02-01 /pmc/articles/PMC3032277/ /pubmed/21293736 Text en Copyright © 2011 Molecular Vision. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Chen, Ziyan
Shamsi, Farrukh A.
Li, Kaijun
Huang, Qiang
Al-Rajhi, Ali A.
Chaudhry, Imtiaz A.
Wu, Kaili
Comparison of camel tear proteins between summer and winter
title Comparison of camel tear proteins between summer and winter
title_full Comparison of camel tear proteins between summer and winter
title_fullStr Comparison of camel tear proteins between summer and winter
title_full_unstemmed Comparison of camel tear proteins between summer and winter
title_short Comparison of camel tear proteins between summer and winter
title_sort comparison of camel tear proteins between summer and winter
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3032277/
https://www.ncbi.nlm.nih.gov/pubmed/21293736
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