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The human neuraminidase enzyme, NEU3, regulates integrin-mediated cell migration via changes in glycolipid composition

  • Author / Creator
    Jia, Feng
  • The human neuraminidase enzyme, NEU3, is known to cleave sialic acid from ganglioside substrates. However, the biological effects of this cleavage are not clearly understood. This thesis describes our studies of the regulation of β1-integrins by neuraminidase enzymes, and the role of gangliosides in this process. In cell migration assays, NEU3 treatment of cells increased the rate of migration in HeLa. In contrast, NEU4 increased the rate of cell migration. Using a cell line that over-expressed a fluorescent fusion protein of NEU3, we were able to observe that the enzyme colocalized with β1-integrin in cells. These results strengthen the biochemical link between NEU3 and integrin receptors, and suggest that glycolipids may play a more direct role in the regulation of cellular migration

  • Subjects / Keywords
  • Graduation date
    2013-11
  • Type of Item
    Thesis
  • Degree
    Master of Science
  • DOI
    https://doi.org/10.7939/R3FJ29N0D
  • License
    This thesis is made available by the University of Alberta Libraries with permission of the copyright owner solely for non-commercial purposes. This thesis, or any portion thereof, may not otherwise be copied or reproduced without the written consent of the copyright owner, except to the extent permitted by Canadian copyright law.
  • Language
    English
  • Institution
    University of Alberta
  • Degree level
    Master's
  • Department
    • Department of Chemistry
  • Supervisor / co-supervisor and their department(s)
    • Cairo, Christopher W. (Chemistry)
  • Examining committee members and their departments
    • Sipione, Simonetta (Pharmacology)
    • Petersen, Nils O. (Chemistry)