Glycomic and sialoproteomic data of gastric carcinoma cells overexpressing ST3GAL4

Stefan Mereiter; Ana Magalhães; Barbara Adamczyk; Chunsheng Jin; Andreia Almeida; Lylia Drici; Maria Ibáñez-Vea; Martin R Larsen; Daniel Kolarich; Niclas G Karlsson; Celso A Reis

doi:10.1016/j.dib.2016.03.022

Glycomic and sialoproteomic data of gastric carcinoma cells overexpressing ST3GAL4

Data Brief. 2016 Mar 14:7:814-33. doi: 10.1016/j.dib.2016.03.022. eCollection 2016 Jun.

Authors

Affiliations

¹ I3S - Instituto de Investigação e Inovação em Saúde, University of Porto, Portugal; Institute of Molecular Pathology and Immunology of the University of Porto - IPATIMUP, Porto, Portugal; Institute of Biomedical Sciences of Abel Salazar - ICBAS, University of Porto, Portugal.
² I3S - Instituto de Investigação e Inovação em Saúde, University of Porto, Portugal; Institute of Molecular Pathology and Immunology of the University of Porto - IPATIMUP, Porto, Portugal.
³ Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Sweden.
⁴ Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, 14424 Potsdam, Germany; Free University Berlin, Berlin, Germany.
⁵ Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense, Denmark.
⁶ Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, 14424 Potsdam, Germany.
⁷ I3S - Instituto de Investigação e Inovação em Saúde, University of Porto, Portugal; Institute of Molecular Pathology and Immunology of the University of Porto - IPATIMUP, Porto, Portugal; Institute of Biomedical Sciences of Abel Salazar - ICBAS, University of Porto, Portugal; Medical Faculty, University of Porto, Portugal.

Abstract

Gastric carcinoma MKN45 cells stably transfected with the full-length ST3GAL4 gene were characterised by glycomic and sialoproteomic analysis. Complementary strategies were applied to assess the glycomic alterations induced by ST3GAL4 overexpression. The N- and O-glycome data were generated in two parallel structural analyzes, based on PGC-ESI-MS/MS. Data on glycan structure identification and relative abundance in ST3GAL4 overexpressing cells and respective mock control are presented. The sialoproteomic analysis based on titanium-dioxide enrichment of sialopeptides with subsequent LC-MS/MS identification was performed. This analysis identified 47 proteins with significantly increased sialylation. The data in this article is associated with the research article published in Biochim Biophys Acta "Glycomic analysis of gastric carcinoma cells discloses glycans as modulators of RON receptor tyrosine kinase activation in cancer" [1].

Keywords: Gastric cancer; N-glycome; O-glycome; Sialoproteome; Sialyltransferase.