O-glycan truncation enhances cancer-related functions of CD44 in gastric cancer

FEBS Lett. 2019 Jul;593(13):1675-1689. doi: 10.1002/1873-3468.13432. Epub 2019 May 27.

Abstract

CD44 isoforms are often upregulated in gastric cancer and have been associated with increased metastatic potential and poor survival. To evaluate the functional impact of O-glycan truncation on CD44 we have analysed glyco-engineered cancer cell models displaying shortened O-glycans. Here, we demonstrate that induction of aberrant O-glycan termination through various molecular mechanisms affects CD44 molecular features. We show that CD44 is a major carrier of truncated O-glycans and that this truncation is accompanied by an increased hyaluronan binding capacity and affects extracellular shedding. In addition, short O-glycans promoted the colocalization of CD44v6 with the receptor tyrosine kinase RON and concomitantly increased activation. Our in vitro findings were validated in gastric cancer clinical samples.

Keywords: CD44; gastric cancer; glycosylation; hyaluronic acid; proximity ligation assay; sialylation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cell Line, Tumor
  • Glycosylation
  • Humans
  • Hyaluronan Receptors / chemistry
  • Hyaluronan Receptors / metabolism*
  • Hyaluronic Acid / metabolism
  • Molecular Weight
  • Polysaccharides / genetics*
  • Polysaccharides / metabolism
  • Protein Transport
  • Receptor Protein-Tyrosine Kinases / metabolism
  • Sequence Deletion*
  • Stomach Neoplasms / pathology*

Substances

  • CD44 protein, human
  • Hyaluronan Receptors
  • Polysaccharides
  • Hyaluronic Acid
  • RON protein
  • Receptor Protein-Tyrosine Kinases