Journal
JOURNAL OF PROTEOME RESEARCH
Volume 7, Issue 10, Pages 4313-4325Publisher
AMER CHEMICAL SOC
DOI: 10.1021/pr8002547
Keywords
glycoproteins; membrane proteins; malignancy associated proteins; spectral count
Categories
Funding
- National Cancer Institute [R01CA100104, R01CA90503, R01CA108597]
- National Institute of Health [R01CM49500]
Ask authors/readers for more resources
The membrane glycoprotein component of the cellular proteome represents a promising source for potential disease biomarkers and therapeutic targets. Here we describe the development of a method that facilitates the analysis of membrane glycoproteins and apply it to the differential analysis of breast tumor cells with distinct malignant phenotypes. The approach combines two membrane extraction procedures, and enrichment using ConA and WGA lectin affinity columns, prior to digestion and analysis by LC-MS/MS. The glycoproteins are identified and quantified by spectral counting. Although the distribution of glycoprotein expression as a function of MW and p/ was very similar between the two related cell lines tested, the approach enabled the identification of several distinct membrane glycoproteins with an expression index correlated with either a precancerous (MCF10AT1), or a malignant, metastatic cellular phenotype (MCF10CA1a). Among the proteins associated with the malignant phenotype, Gamma-glutamyl hydrolase, CD44, Galectin-3-binding protein, and Syndecan-1 protein have been reported as potential biomarkers of breast cancer.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available