Core-Fucosylated Tetra-Antennary N-Glycan Containing A Single N-Acetyllactosamine Branch Is Associated with Poor Survival Outcome in Breast Cancer.
Harmin HerreraTinslee DildayAllison UberDanielle A ScottJoelle N ZambranoMengjun WangPeggi M AngelAnand S MehtaRichard R DrakeElizabeth G HillElizabeth S YehPublished in: International journal of molecular sciences (2019)
(1) Glycoproteins account for ~80% of proteins located at the cell surface and in the extracellular matrix. A growing body of evidence indicates that α-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.
Keyphrases
- cell surface
- mass spectrometry
- lymph node metastasis
- extracellular matrix
- high resolution
- squamous cell carcinoma
- liquid chromatography
- tandem mass spectrometry
- ultra high performance liquid chromatography
- single cell
- simultaneous determination
- small cell lung cancer
- bone marrow
- cell therapy
- small molecule
- ms ms
- childhood cancer
- binding protein
- young adults
- capillary electrophoresis