Identification of novel glycans with disialylated structures in α3 integrin from mouse kidney cells with the phenotype of polycystic kidney disease

Anna Fan Zhang, Shiaw Lin Wu, Yunjoon Jung, Shan Qin, William S. Hancock, Jordan A. Kreidberg*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)

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 languageEnglish
Pages (from-to)4901-4909
Number of pages9
JournalJournal of Proteome Research
Volume13
Issue number11
DOIs
Publication statusPublished - 7 Nov 2014
Externally publishedYes

Keywords

  • glycans
  • glycopeptide analysis
  • N-linked glycosylation
  • Pkd1+/+ cells
  • Pkd1-/- cells
  • polycystic kidney disease
  • site-specific identification
  • α3 integrin

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