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Protein O-glycosylation in the adult kidney

Thursday, September 17, 2015 — Poster Session III

3:30 p.m. – 5:00 p.m.
FAES Terrace
NIDCR
CELLBIO-21

Authors

  • E Tian
  • S Spitznagel
  • MC Malicdan
  • M Huizing
  • LA Tabak
  • KG Ten Hagen

Abstract

Kidney failure is a common disease affecting over 20 million people around the world, but the factors contributing to its onset and progression are largely undefined. To understand the role of conserved protein posttranslational modifications in both normal kidney function and kidney disease, we analyzed mice deficient for a member of the glycosyltransferase family that is expressed in the kidney. UDP-GalNAc:polypeptide acetylgalactosaminyltransferase 11 (Galnt11), which encodes an enzyme that initiates mucin-type O-linked glycosylation on secreted or membrane-bound proteins, is the most abundantly expressed family member in the adult kidney. Galnt11 null adult mice were significantly smaller than wild type littermate controls. Additionally, O-glycan expression was altered in Galnt11 null kidneys relative to littermate controls, as assessed by lectin blotting. Immunofluorescence showed decreased O-glycan expression specifically in the glomerulus and tubules of Galnt11 null animals. Also, increased extracellular matrix staining was observed in the Galnt11 null glomerular cells. Masson’s and Alcian blue-PAS staining revealed evidence of fibrosis in the Galnt11 null kidneys. Taken together, our research reveals new insights into the roles of mucin-type O-linked glycosylation in adult kidney formation and function and may provide information regarding factors that underlie kidney disease.

Category: Cell Biology