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Journal of Glycobiology | ISSN: 2168-958X | Volume 7
Glycobiology & Glycoproteomics
5th International Conference on
&
August 27-28, 2018 | Toronto, Canada
Molecular Biology & Nucleic Acids
3rd International Conference on
Aberrant sialoglycan patterns facilitate 3D multicellular spheroid and xenograft tumor formation
Multicellular tumor spheroids are now at the forefront of cancer research, designed to mimic tumor-like developmental
patterns in vitro. Tumor growth in vivo is known to be highly influenced by aberrant cell surface specific sialoglycan
structures on glycoproteins. Aberrant sialoglycan patterns that facilitate spheroid formation are not well defined. Here, matrix-
free spheroids from human breast, pancreatic and prostate cancer cell lines and their respective chemoresistant variants were
generatedusing a unique cyclicArg-Gly-Asp-D-Phe-Lys peptidemodifiedwith 4-carboxybutyl-triphenylphosphoniumbromide
(cyclo-RGDfK (TPP)) induced self-assembly platform. The cyclo-RGDfK(TPP) peptides mimic the natural extracellular
matrices (ECM) protein’s ability to induce cell aggregation via α5β1 integrin. We used the cyclo-RGDfK (TPP) approach to
biochemically induce cell aggregation and compaction, transmogrifying monolayer cancer cells into tumor spheroids. MCF-7
and PANC-1 cells, and their drug-resistant cancer cell lines (MCF-7 TMX, PANC1-GemR) express different sialic acid content,
which influenced their ability to form spheroids under cyclo-RGDfK (TPP)-induced self-assembly. Cancer cell aggregation and
compaction correlate with the presence of α-2.3- and α-2,6-sialic acid cell surface residues to form spheroids under cyclo-RGDfK
(TPP)-induced self-assembly and xenograft tumors. Removal or blockage of SA inhibited cell aggregation. Neuraminidase
inhibitor, oseltamivir phosphate, enhanced cell aggregation and promoted compaction of cell aggregates. Future studies should
build upon these findings and explore alternate and novel methods to target the cancer cell glycome and the unique sialylation
patterns of the adhesion molecules involved in the spheroid formation and tumor progression.
Biography
For the past 37 years, Dr Szewczuk is Full Professor of Immunology and Medicine, Queen’s University, Kingston, Ontario Canada. Dr Szewczuk’s recent research
has focused on the role of glycosylation in receptor activation with a particular focus of Toll-like, nerve growth factor Trk, EGFR and insulin receptors. He has
discovered a novel receptor-signaling platform and its targeted translation in multistage tumorigenesis.
Myron R Szewczuk
Queen’s University, Canada
Myron R Szewczuk, J Glycobiol 2018, Volume 7
DOI: 10.4172/2168-958X-C1-010