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Related Experiment Videos

Increased N-acetyl-beta-glucosaminidase activity in primary breast carcinomas corresponds to a decrease in

C Slawson1, J Pidala, R Potter

  • 1Department of Chemistry and Institute for Biomolecular Science, University of South Florida, 4202 Fowler Avenue, Tampa, FL 33620, USA.

Biochimica Et Biophysica Acta
|September 22, 2001
PubMed
Summary

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Breast tumor tissue shows increased O-GlcNAcase activity and decreased protein O-GlcNAc levels compared to normal tissue. This suggests O-GlcNAcase may selectively remove N-acetylglucosamine modifications in breast cancer.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • N-acetylglucosamine (O-GlcNAc) is a dynamic intracellular modification on proteins.
  • O-GlcNAcase (OGA) is the enzyme responsible for removing O-GlcNAc.
  • Limited data exists on OGA activity and O-GlcNAc levels in cancer.

Purpose of the Study:

  • To investigate O-GlcNAcase activity in primary breast tumors versus adjacent normal tissue.
  • To examine the relationship between O-GlcNAcase activity and protein O-GlcNAc levels in breast tumors.
  • To explore the role of O-GlcNAcase in breast cancer biology.

Main Methods:

  • Assay for O-GlcNAcase and lysosomal hexosaminidase activity.
  • Immunoblotting, affinity blotting, and radioactive labeling to assess protein O-GlcNAc.

Related Experiment Videos

  • Comparison of enzymatic activity and protein modification in 12 matched pairs of tumor and adjacent normal breast tissue.

    • Main Results:

    • O-GlcNAcase and lysosomal hexosaminidase activity were significantly increased in breast tumor tissue (P<0.05).
    • The variety of O-GlcNAc modified proteins was greater in tumor tissue.
    • Total O-GlcNAc levels were significantly decreased in tumor tissue, particularly on proteins of 45-65 kDa.

    Conclusions:

    • O-GlcNAcase activity is elevated in primary breast tumors.
    • Despite increased O-GlcNAcase, overall protein O-GlcNAc levels are reduced in tumors.
    • O-GlcNAcase may play a role in the selective de-O-GlcNAcylation of specific proteins in breast cancer.