Altered <i>O</i>-glycomes of Renal Brush-Border Membrane in Model Rats with Chronic Kidney Diseases
Chronic kidney disease (CKD) is defined as a decrease in renal function or glomerular filtration rate (GFR), and proteinuria is often present. Proteinuria increases with age and can be caused by glomerular and/or proximal tubule (PT) alterations. PT cells have an apical brush border membrane (BBM),...
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oai:doaj.org-article:bbd8f5c80fb74ce9bf556ae79c00c53e2021-11-25T16:51:52ZAltered <i>O</i>-glycomes of Renal Brush-Border Membrane in Model Rats with Chronic Kidney Diseases10.3390/biom111115602218-273Xhttps://doaj.org/article/bbd8f5c80fb74ce9bf556ae79c00c53e2021-10-01T00:00:00Zhttps://www.mdpi.com/2218-273X/11/11/1560https://doaj.org/toc/2218-273XChronic kidney disease (CKD) is defined as a decrease in renal function or glomerular filtration rate (GFR), and proteinuria is often present. Proteinuria increases with age and can be caused by glomerular and/or proximal tubule (PT) alterations. PT cells have an apical brush border membrane (BBM), which is a highly dynamic, organized, and specialized membrane region containing multiple glycoproteins required for its functions including regulating uptake, secretion, and signaling dependent upon the physiologic state. PT disorders contribute to the dysfunction observed in CKD. Many glycoprotein functions have been attributed to their <i>N</i>- and <i>O</i>-glycans, which are highly regulated and complex. In this study, the <i>O</i>-glycans present in rat BBMs from animals with different levels of kidney disease and proteinuria were characterized and analyzed using liquid chromatography tandem mass spectrometry (LC–MS/MS). A principal component analysis (PCA) documented that each group has distinct <i>O</i>-glycan distributions. Higher fucosylation levels were observed in the CKD and diabetic groups, which may contribute to PT dysfunction by altering physiologic glycoprotein interactions. Fucosylated <i>O</i>-glycans such as 1-1-1-0 exhibited higher abundance in the severe proteinuric groups. These glycomic results revealed that differential <i>O</i>-glycan expressions in CKD progressions has the potential to define the mechanism of proteinuria in kidney disease and to identify potential therapeutic interventions.Aiying YuJingfu ZhaoJieqiang ZhongJunyao WangShiv Pratap S. YadavBruce A. MolitorisMark C. WagnerYehia MechrefMDPI AGarticle<i>O</i>-glycanbrush-border membraneproteinuria and hypertensionobese and diabeticchronic kidney diseasedifferential expression analysisMicrobiologyQR1-502ENBiomolecules, Vol 11, Iss 1560, p 1560 (2021) |
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<i>O</i>-glycan brush-border membrane proteinuria and hypertension obese and diabetic chronic kidney disease differential expression analysis Microbiology QR1-502 |
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<i>O</i>-glycan brush-border membrane proteinuria and hypertension obese and diabetic chronic kidney disease differential expression analysis Microbiology QR1-502 Aiying Yu Jingfu Zhao Jieqiang Zhong Junyao Wang Shiv Pratap S. Yadav Bruce A. Molitoris Mark C. Wagner Yehia Mechref Altered <i>O</i>-glycomes of Renal Brush-Border Membrane in Model Rats with Chronic Kidney Diseases |
description |
Chronic kidney disease (CKD) is defined as a decrease in renal function or glomerular filtration rate (GFR), and proteinuria is often present. Proteinuria increases with age and can be caused by glomerular and/or proximal tubule (PT) alterations. PT cells have an apical brush border membrane (BBM), which is a highly dynamic, organized, and specialized membrane region containing multiple glycoproteins required for its functions including regulating uptake, secretion, and signaling dependent upon the physiologic state. PT disorders contribute to the dysfunction observed in CKD. Many glycoprotein functions have been attributed to their <i>N</i>- and <i>O</i>-glycans, which are highly regulated and complex. In this study, the <i>O</i>-glycans present in rat BBMs from animals with different levels of kidney disease and proteinuria were characterized and analyzed using liquid chromatography tandem mass spectrometry (LC–MS/MS). A principal component analysis (PCA) documented that each group has distinct <i>O</i>-glycan distributions. Higher fucosylation levels were observed in the CKD and diabetic groups, which may contribute to PT dysfunction by altering physiologic glycoprotein interactions. Fucosylated <i>O</i>-glycans such as 1-1-1-0 exhibited higher abundance in the severe proteinuric groups. These glycomic results revealed that differential <i>O</i>-glycan expressions in CKD progressions has the potential to define the mechanism of proteinuria in kidney disease and to identify potential therapeutic interventions. |
format |
article |
author |
Aiying Yu Jingfu Zhao Jieqiang Zhong Junyao Wang Shiv Pratap S. Yadav Bruce A. Molitoris Mark C. Wagner Yehia Mechref |
author_facet |
Aiying Yu Jingfu Zhao Jieqiang Zhong Junyao Wang Shiv Pratap S. Yadav Bruce A. Molitoris Mark C. Wagner Yehia Mechref |
author_sort |
Aiying Yu |
title |
Altered <i>O</i>-glycomes of Renal Brush-Border Membrane in Model Rats with Chronic Kidney Diseases |
title_short |
Altered <i>O</i>-glycomes of Renal Brush-Border Membrane in Model Rats with Chronic Kidney Diseases |
title_full |
Altered <i>O</i>-glycomes of Renal Brush-Border Membrane in Model Rats with Chronic Kidney Diseases |
title_fullStr |
Altered <i>O</i>-glycomes of Renal Brush-Border Membrane in Model Rats with Chronic Kidney Diseases |
title_full_unstemmed |
Altered <i>O</i>-glycomes of Renal Brush-Border Membrane in Model Rats with Chronic Kidney Diseases |
title_sort |
altered <i>o</i>-glycomes of renal brush-border membrane in model rats with chronic kidney diseases |
publisher |
MDPI AG |
publishDate |
2021 |
url |
https://doaj.org/article/bbd8f5c80fb74ce9bf556ae79c00c53e |
work_keys_str_mv |
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