Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 292, Issue 40, Pages 16491-16497Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M117.798512
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Funding
- National Institutes of Health [GM114731, HL128390, HD083418, DK085691, HL093242, HL118676]
- National Natural Science Foundation of China [81520108005, 81470825, 81370617]
- Jiangsu Province Key Medical Center Grant [ZX201102]
- Scientist Development Grants from the American Heart Association [11SDG7410022, 17SDG33630161]
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The kidney's filtration activity is essential for removing toxins and waste products from the body. The vascular endothelial cells of the glomerulus are fenestrated, flattened, and surrounded by podocytes, specialized cells that support glomerular endothelial cells. Mucin-type core 1-derived O-glycans (O-glycans) are highly expressed on both glomerular capillary endothelial cells and their supporting podocytes, but their biological role is unclear. Biosynthesis of core 1-derived O-glycans is catalyzed by the glycosyltransferase core 1 beta 1,3-galactosyltransferase (C1galt1). Here we report that neonatal or adult mice with inducible deletion of C1galt1 (iC1galt1(-/-)) exhibit spontaneous proteinuria and rapidly progressing glomerulosclerosis. Ultrastructural analysis of the glomerular filtration barrier components revealed that loss of O-glycans results in altered podocyte foot processes. Further analysis indicated that O-glycan is essential for the normal signaling function of podocalyxin, a podocyte foot process-associated glycoprotein. Our results reveal a new function of O-glycosylation in the integrity of the glomerular filtration barrier.
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