|Title||Lectin microarray profiling of metastatic breast cancers|
|Authors||Fry, S., Afrough, B., Lomax-Browne, H., Timms, J.F., Velentzis, L.S. and Leathem, A.|
Altered protein glycosylation compared to the disease-free state is a universal feature of cancer cells. It has long been established that distinct glycan structures are associated with specific forms of cancer, but far less is known about the complete array of glycans associated with certain tumours. The cancer glycome has great potential as a source of biomarkers, but progress in this field has been hindered by a lack of available techniques for the elucidation of disease associated glycosylation. In the present study, lectin microarrays consisting of 45 lectins with different binding preferences covering N- and O-linked glycans were coupled with evanescent-field activated fluorescent detection in the glycomic analysis of primary breast tumours and the serum and urine of patients with metastatic breast cancer. A single 50 μm section of a primary breast tumour or less than 1 μL of breast cancer patient serum or urine was sufficient to detect glycosylation alterations associated with metastatic breast cancer, as inferred from lectin binding patterns. The high-throughput, sensitive and relatively simple nature of the simultaneous analysis of N- and O-linked glycosylation following minimal sample preparation and without the need for protein deglycosylation makes the lectin microarray analysis described a valuable tool for discovery phase glycomic profiling.
|Journal citation||21 (8), pp. 1060-1070|
|Publisher||Oxford University Press|
|Digital Object Identifier (DOI)||doi:10.1093/glycob/cwr045|