Lectin staining and Western blot data showing differential sialylation of nutrient-deprived cancer cells to sialic acid supplementation

Haitham A Badr; Dina M M AlSadek; Mohit P Mathew; Chen-Zhong Li; Leyla B Djansugurova; Kevin J Yarema; Hafiz Ahmed

doi:10.1016/j.dib.2015.09.043

Lectin staining and Western blot data showing differential sialylation of nutrient-deprived cancer cells to sialic acid supplementation

Data Brief. 2015 Oct 9:5:481-8. doi: 10.1016/j.dib.2015.09.043. eCollection 2015 Dec.

Authors

Haitham A Badr¹, Dina M M AlSadek², Mohit P Mathew³, Chen-Zhong Li⁴, Leyla B Djansugurova⁵, Kevin J Yarema³, Hafiz Ahmed⁶

Affiliations

¹ Department of Biochemistry, Faculty of Agriculture, Zagazig University, Zagazig 44511, Egypt.
² Department of Histology and Cytology, Faculty of Veterinary Medicine, Zagazig University, Zagazig 44511, Egypt.
³ Department of Biomedical Engineering and Translational Tissue Engineering Center, The Johns Hopkins University, 400 North Broadway Street MD, Baltimore 21231, USA.
⁴ Department of Biomedical Engineering, Florida International University, 10555 West Flagler Street, Miami, FL 33174 USA.
⁵ Institute of General Genetics and Cytology, Al-Farabi Ave, 93, Almaty 050060, Kazakhstan.
⁶ Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine and Institute of Marine and Environmental Technology, 701 East Pratt Street, Baltimore, MD 21202, USA.

Abstract

This report provides data that are specifically related to the differential sialylation of nutrient deprived breast cancer cells to sialic acid supplementation in support of the research article entitled, "Nutrient-deprived cancer cells preferentially use sialic acid to maintain cell surface glycosylation" [1]. Particularly, breast cancer cells, when supplemented with sialic acid under nutrient deprivation, display sialylated glycans at the cell surface, but non-malignant mammary cells show sialylated glycans intracellularly. The impact of sialic acid supplementation under nutrient deprivation was demonstrated by measuring levels of expression and sialylation of two markers, EGFR1 and MUC1. This Data in Brief article complements the main manuscript by providing detailed instructions and representative results for cell-level imaging and Western blot analyses of changes in sialylation during nutrient deprivation and sialic acid supplementation. These methods can be readily generalized for the study of many types of glycosylation and various glycoprotein markers through the appropriate selection of fluorescently-labeled lectins.

Keywords: Aberrant glycosylation; Differential sialylation; Metabolic glycoengineering.; Nutrient deprivation; Sialic acid biosynthesis.

Abstract

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