Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 20, Issue 10, Pages -Publisher
MDPI
DOI: 10.3390/ijms20102528
Keywords
breast cancer; N-glycan; core-fucose; N-acetyllactosamine
Funding
- South Carolina Clinical and Translational Research (SCTR) Institute
- NIH/NCATS [UL1 TR001450]
- Medical University of South Carolina
- South Carolina Centers of Economic Excellence
- National Institute of General Medical Sciences [P20 GM103542]
- Hollings Cancer Center's Cancer Center at the Medical University of South Carolina [P30 CA138313]
- Biostatistics Shared Resource, Hollings Cancer Center, Medical University of South Carolina [P30 CA138313]
- NIH
- [R21 CA225474]
- [U01 CA226052]
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(1) Glycoproteins account for similar to 80% of proteins located at the cell surface and in the extracellular matrix. A growing body of evidence indicates that -L-fucose protein modifications contribute to breast cancer progression and metastatic disease. (2) Using a combination of techniques, including matrix-assisted laser desorption/ionization imaging mass spectrometry (MALDI-IMS) based in cell and on tissue imaging and glycan sequencing using exoglycosidase analysis coupled to hydrophilic interaction ultra-high performance liquid chromatography (HILIC UPLC), we establish that a core-fucosylated tetra-antennary glycan containing a single N-acetyllactosamine (F(6)A4G4Lac1) is associated with poor clinical outcomes in breast cancer, including lymph node metastasis, recurrent disease, and reduced survival. (3) This study is the first to identify a single N-glycan, F(6)A4G4Lac1, as having a correlation with poor clinical outcomes in breast cancer.
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