Abstract
Autosomal dominant polycystic kidney disease (ADPKD) is a common genetic disorder caused by mutations in the Pkd1 or Pkd2 genes, in which large cysts replace normal kidney tissue, leading to end-stage kidney disease. In this study we have utilized a powerful nano-HPLC-mass spectrometric approach to characterize patterns of normal and abnormal N-linked glycosylation of α3 integrin subunit in Pkd1-/- cells derived from mouse kidneys. Higher molecular weight glycan structures with a different monosaccharide composition were observed at two sites, namely, Asn-925 and Asn-928 sites in α3 integrin isolated from Pkd1+/+ cells compared with Pkd1-/- cells. In addition, an unusual and unique disialic acid glycan structure was observed solely in Pkd1-/- cells. Thus, these studies suggest that abnormal protein glycosylation may have a role on the pathogenesis of cyst formation in ADPKD.
Original language | English |
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Pages (from-to) | 4901-4909 |
Number of pages | 9 |
Journal | Journal of Proteome Research |
Volume | 13 |
Issue number | 11 |
DOIs | |
Publication status | Published - 7 Nov 2014 |
Externally published | Yes |
Keywords
- glycans
- glycopeptide analysis
- N-linked glycosylation
- Pkd1+/+ cells
- Pkd1-/- cells
- polycystic kidney disease
- site-specific identification
- α3 integrin