Cargando…

The Constitutive Proteome of Human Aqueous Humor and Race Specific Alterations

Aqueous humor (AH) is the fluid in the anterior and posterior chambers of the eye that contains proteins regulating ocular homeostasis. Analysis of aqueous humor proteome is challenging, mainly due to low sample volume and protein concentration. In this study, by utilizing state of the art technolog...

Descripción completa

Detalles Bibliográficos
Autores principales: Kodeboyina, Sai Karthik, Lee, Tae Jin, Churchwell, Lara, Ulrich, Lane, Bollinger, Kathryn, Bogorad, David, Estes, Amy, Zhi, Wenbo, Sharma, Shruti, Sharma, Ashok
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7709111/
https://www.ncbi.nlm.nih.gov/pubmed/33217969
http://dx.doi.org/10.3390/proteomes8040034
_version_ 1783617683271450624
author Kodeboyina, Sai Karthik
Lee, Tae Jin
Churchwell, Lara
Ulrich, Lane
Bollinger, Kathryn
Bogorad, David
Estes, Amy
Zhi, Wenbo
Sharma, Shruti
Sharma, Ashok
author_facet Kodeboyina, Sai Karthik
Lee, Tae Jin
Churchwell, Lara
Ulrich, Lane
Bollinger, Kathryn
Bogorad, David
Estes, Amy
Zhi, Wenbo
Sharma, Shruti
Sharma, Ashok
author_sort Kodeboyina, Sai Karthik
collection PubMed
description Aqueous humor (AH) is the fluid in the anterior and posterior chambers of the eye that contains proteins regulating ocular homeostasis. Analysis of aqueous humor proteome is challenging, mainly due to low sample volume and protein concentration. In this study, by utilizing state of the art technology, we performed Liquid-Chromatography Mass spectrometry (LC-MS/MS) analysis of 88 aqueous humor samples from subjects undergoing cataract surgery. A total of 2263 unique proteins were identified, which were sub-divided into four categories that were based on their detection in the number of samples: High (n = 152), Medium (n = 91), Low (n = 128), and Rare (n = 1892). A total of 243 proteins detected in at least 50% of the samples were considered as the constitutive proteome of human aqueous humor. The biological processes and pathways enriched in the AH proteins mainly include vesicle mediated transport, acute phase response signaling, LXR/RXR activation, complement system, and secretion. The enriched molecular functions are endopeptidase activity, and various binding functions, such as protein binding, lipid binding, and ion binding. Additionally, this study provides a novel insight into race specific differences in the AH proteome. A total of six proteins were upregulated, and five proteins were downregulated in African American subjects as compared to Caucasians.
format Online
Article
Text
id pubmed-7709111
institution National Center for Biotechnology Information
language English
publishDate 2020
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-77091112020-12-03 The Constitutive Proteome of Human Aqueous Humor and Race Specific Alterations Kodeboyina, Sai Karthik Lee, Tae Jin Churchwell, Lara Ulrich, Lane Bollinger, Kathryn Bogorad, David Estes, Amy Zhi, Wenbo Sharma, Shruti Sharma, Ashok Proteomes Article Aqueous humor (AH) is the fluid in the anterior and posterior chambers of the eye that contains proteins regulating ocular homeostasis. Analysis of aqueous humor proteome is challenging, mainly due to low sample volume and protein concentration. In this study, by utilizing state of the art technology, we performed Liquid-Chromatography Mass spectrometry (LC-MS/MS) analysis of 88 aqueous humor samples from subjects undergoing cataract surgery. A total of 2263 unique proteins were identified, which were sub-divided into four categories that were based on their detection in the number of samples: High (n = 152), Medium (n = 91), Low (n = 128), and Rare (n = 1892). A total of 243 proteins detected in at least 50% of the samples were considered as the constitutive proteome of human aqueous humor. The biological processes and pathways enriched in the AH proteins mainly include vesicle mediated transport, acute phase response signaling, LXR/RXR activation, complement system, and secretion. The enriched molecular functions are endopeptidase activity, and various binding functions, such as protein binding, lipid binding, and ion binding. Additionally, this study provides a novel insight into race specific differences in the AH proteome. A total of six proteins were upregulated, and five proteins were downregulated in African American subjects as compared to Caucasians. MDPI 2020-11-18 /pmc/articles/PMC7709111/ /pubmed/33217969 http://dx.doi.org/10.3390/proteomes8040034 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Kodeboyina, Sai Karthik
Lee, Tae Jin
Churchwell, Lara
Ulrich, Lane
Bollinger, Kathryn
Bogorad, David
Estes, Amy
Zhi, Wenbo
Sharma, Shruti
Sharma, Ashok
The Constitutive Proteome of Human Aqueous Humor and Race Specific Alterations
title The Constitutive Proteome of Human Aqueous Humor and Race Specific Alterations
title_full The Constitutive Proteome of Human Aqueous Humor and Race Specific Alterations
title_fullStr The Constitutive Proteome of Human Aqueous Humor and Race Specific Alterations
title_full_unstemmed The Constitutive Proteome of Human Aqueous Humor and Race Specific Alterations
title_short The Constitutive Proteome of Human Aqueous Humor and Race Specific Alterations
title_sort constitutive proteome of human aqueous humor and race specific alterations
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7709111/
https://www.ncbi.nlm.nih.gov/pubmed/33217969
http://dx.doi.org/10.3390/proteomes8040034
work_keys_str_mv AT kodeboyinasaikarthik theconstitutiveproteomeofhumanaqueoushumorandracespecificalterations
AT leetaejin theconstitutiveproteomeofhumanaqueoushumorandracespecificalterations
AT churchwelllara theconstitutiveproteomeofhumanaqueoushumorandracespecificalterations
AT ulrichlane theconstitutiveproteomeofhumanaqueoushumorandracespecificalterations
AT bollingerkathryn theconstitutiveproteomeofhumanaqueoushumorandracespecificalterations
AT bogoraddavid theconstitutiveproteomeofhumanaqueoushumorandracespecificalterations
AT estesamy theconstitutiveproteomeofhumanaqueoushumorandracespecificalterations
AT zhiwenbo theconstitutiveproteomeofhumanaqueoushumorandracespecificalterations
AT sharmashruti theconstitutiveproteomeofhumanaqueoushumorandracespecificalterations
AT sharmaashok theconstitutiveproteomeofhumanaqueoushumorandracespecificalterations
AT kodeboyinasaikarthik constitutiveproteomeofhumanaqueoushumorandracespecificalterations
AT leetaejin constitutiveproteomeofhumanaqueoushumorandracespecificalterations
AT churchwelllara constitutiveproteomeofhumanaqueoushumorandracespecificalterations
AT ulrichlane constitutiveproteomeofhumanaqueoushumorandracespecificalterations
AT bollingerkathryn constitutiveproteomeofhumanaqueoushumorandracespecificalterations
AT bogoraddavid constitutiveproteomeofhumanaqueoushumorandracespecificalterations
AT estesamy constitutiveproteomeofhumanaqueoushumorandracespecificalterations
AT zhiwenbo constitutiveproteomeofhumanaqueoushumorandracespecificalterations
AT sharmashruti constitutiveproteomeofhumanaqueoushumorandracespecificalterations
AT sharmaashok constitutiveproteomeofhumanaqueoushumorandracespecificalterations