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

被引:6
作者
Badr, Haitham A. [1 ]
AlSadek, Dina M. M. [2 ]
Mathew, Mohit P. [3 ,4 ]
Li, Chen-Zhong [5 ]
Djansugurova, Leyla B. [6 ]
Yarema, Kevin J. [3 ,4 ]
Ahmed, Hafiz [7 ,8 ]
机构
[1] Zagazig Univ, Fac Agr, Dept Biochem, Zagazig 44511, Egypt
[2] Zagazig Univ, Fac Vet Med, Dept Histol & Cytol, Zagazig 44511, Egypt
[3] Johns Hopkins Univ, Dept Biomed Engn, Baltimore, MD 21231 USA
[4] Johns Hopkins Univ, Translat Tissue Engn Ctr, Baltimore, MD 21231 USA
[5] Florida Int Univ, Dept Biomed Engn, Miami, FL 33174 USA
[6] Inst Gen Genet & Cytol, Alma Ata 050060, Kazakhstan
[7] Univ Maryland, Sch Med, Dept Biochem & Mol Biol, Baltimore, MD 21202 USA
[8] Inst Marine & Environm Technol, Baltimore, MD 21202 USA
来源
DATA IN BRIEF | 2015年 / 5卷
基金
美国国家科学基金会;
关键词
Differential sialylation; Aberrant glycosylation; Sialic acid biosynthesis; Nutrient deprivation; Metabolic glycoengineering;
D O I
10.1016/j.dib.2015.09.043
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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 MUCl. 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. (C) 2015 The Authors. Published by Elsevier Inc. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/40).
引用
收藏
页码:481 / 488
页数:8
相关论文
共 4 条
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